Cell recruitment (pro-inflammatory response) (Homo sapiens)

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<?xml version="1.0" encoding="UTF-8"?> <Pathway xmlns="http://pathvisio.org/GPML/2013a" Name="Cell recruitment (pro-inflammatory response)" Organism="Homo sapiens"> <Comment Source="WikiPathways-description">Migration of immune cells is orchestrated by a fine balance of cytokine and chemokine responses. During Leishmania macrophage interaction, either pro inflammatory or anti-inflammatory cytokines are produced, having an impact in the establishment of infection and further clinical outcome (Navas et al. 2014). Toll like receptors, GPCRs such as the purinergic receptors P2YRs, complement receptor 3A and interleukin receptor 15 amongst others, have been associated with the production of pro inflammatory cytokines (Lai and Gallo 2012 &amp; Cekic et al. 2016). A strong pro inflammatory response in the acute phase of the infection helps to control the parasite load when the recruited cells enhance microbiocidal mechanisms. However, alterations in the chemokine network may contribute to uncontrolled immune responses that can modulate parasite survival and promote or mitigate the associated immunopathology, thereby influencing the outcome of infection (Navas et al. 2014). 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<Attribute Key="copies_num" Value="2" /> <Graphics CenterX="100.0" CenterY="1397.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="P49961" /> </DataNode> <DataNode TextLabel="CDP " GraphId="c9779" Type="Metabolite" GroupRef="ca855"> <Attribute Key="cellular_location" Value="extracellular region" /> <Attribute Key="complex_id" Value="R-ALL-8936165" /> <Attribute Key="copies_num" Value="1" /> <Graphics CenterX="100.0" CenterY="1537.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" Color="0000ff" /> <Xref Database="ChEBI" ID="CHEBI:17239" /> </DataNode> <DataNode TextLabel="CASP1(1-404) " GraphId="c9ac1" Type="Protein" GroupRef="bed57"> <Attribute Key="cellular_location" Value="cytosol" /> <Attribute Key="complex_id" Value="R-HSA-925458" /> <Attribute Key="copies_num" Value="1" /> <Graphics CenterX="380.0" CenterY="1457.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="P29466" /> </DataNode> <DataNode TextLabel="P2RX7 " GraphId="ca87a" Type="Protein" GroupRef="b5789"> <Attribute Key="cellular_location" Value="plasma membrane" /> <Attribute Key="complex_id" Value="R-HSA-9660827" /> <Attribute Key="copies_num" Value="1" /> <Graphics CenterX="100.0" CenterY="1237.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="Q99572" /> </DataNode> <DataNode TextLabel="NTP" GraphId="ca9d5" Type="Metabolite"> <Attribute Key="cellular_location" Value="extracellular region" /> <Graphics CenterX="141.0" CenterY="253.0" Width="40.0" Height="30.0" ZOrder="32768" FontSize="10" Valign="Middle" Color="0000ff" /> <Xref Database="ChEBI" ID="CHEBI:17326" /> </DataNode> <DataNode TextLabel="Pyrin trimer:ASC" GraphId="cb971" Type="Complex"> <Attribute Key="cellular_location" Value="cytosol" /> <Graphics CenterX="636.5" CenterY="690.0" Width="105.0" Height="22.0" ZOrder="32768" FontSize="10" Valign="Middle" ShapeType="Hexagon" Color="a52a2a" /> <Xref Database="Reactome" ID="R-HSA-877352" /> </DataNode> <DataNode TextLabel="CASP1(120-297)" GraphId="cc121" Type="Protein"> <Attribute Key="cellular_location" Value="cytosol" /> <Graphics CenterX="1221.0" CenterY="515.0" Width="106.0" Height="22.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="P29466" /> </DataNode> <DataNode TextLabel="H2O" GraphId="cc52e" Type="Metabolite"> <Attribute Key="cellular_location" Value="extracellular region" /> <Graphics CenterX="140.5" CenterY="202.0" Width="43.0" Height="30.0" ZOrder="32768" FontSize="10" Valign="Middle" Color="0000ff" /> <Xref Database="ChEBI" ID="CHEBI:15377" /> </DataNode> <DataNode TextLabel="IL18 " GraphId="cc5a3" Type="Protein" GroupRef="d226d"> <Attribute Key="cellular_location" Value="extracellular region" /> <Attribute Key="complex_id" Value="R-HSA-449027" /> <Attribute Key="copies_num" Value="1" /> <Graphics CenterX="520.0" CenterY="1497.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="Q14116" /> </DataNode> <DataNode TextLabel="TXN " GraphId="cc945" Type="Protein" GroupRef="be78a"> <Attribute Key="cellular_location" Value="cytosol" /> <Attribute Key="complex_id" Value="R-HSA-1250277" /> <Attribute Key="copies_num" Value="1" /> <Graphics CenterX="240.0" CenterY="1537.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="P10599" /> </DataNode> <DataNode TextLabel="P2RX4 " GraphId="cd8da" Type="Protein" GroupRef="e4dd9"> <Attribute Key="cellular_location" Value="plasma membrane" /> <Attribute Key="complex_id" Value="R-HSA-9665556" /> <Attribute Key="copies_num" Value="5" /> <Graphics CenterX="240.0" CenterY="1277.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="Q99571" /> </DataNode> <DataNode TextLabel="2xHC-TXN " GraphId="ce1aa" Type="Protein" GroupRef="ce18a"> <Attribute Key="cellular_location" Value="cytosol" /> <Attribute Key="complex_id" Value="R-HSA-1250249" /> <Attribute Key="copies_num" Value="1" /> <Graphics CenterX="240.0" CenterY="1617.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="P10599" /> </DataNode> <DataNode TextLabel="IL18(1-193) " GraphId="cf1cb" Type="Protein" GroupRef="bc1d3"> <Attribute Key="cellular_location" Value="cytosol" /> <Attribute Key="complex_id" Value="R-HSA-449039" /> <Attribute Key="copies_num" Value="1" /> <Graphics CenterX="380.0" CenterY="1977.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="Q14116" /> </DataNode> <DataNode TextLabel="ADP,GDP,CDP,UDP" GraphId="cf233" Type="Complex"> <Attribute Key="cellular_location" Value="extracellular region" /> <Graphics CenterX="599.5" CenterY="125.0" Width="117.0" Height="22.0" ZOrder="32768" FontSize="10" Valign="Middle" ShapeType="RoundedRectangle" Color="a52a2a" /> <Xref Database="Reactome" ID="R-ALL-8936165" /> </DataNode> <DataNode TextLabel="IL18(1-36) " GraphId="cfeb8" Type="Protein" GroupRef="d2ec9"> <Attribute Key="cellular_location" Value="cytosol" /> <Attribute Key="complex_id" Value="R-HSA-449026" /> <Attribute Key="copies_num" Value="1" /> <Graphics CenterX="520.0" CenterY="1297.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="Q14116" /> </DataNode> <DataNode TextLabel="SiO2 " GraphId="d04b0" Type="Metabolite" GroupRef="eb5bc"> <Attribute Key="cellular_location" Value="cytosol" /> <Attribute Key="complex_id" Value="R-ALL-877245" /> <Attribute Key="copies_num" Value="1" /> <Graphics CenterX="240.0" CenterY="1897.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" Color="0000ff" /> <Xref Database="ChEBI" ID="CHEBI:30563" /> </DataNode> <DataNode TextLabel="NFKB1(1-433) " GraphId="d15ac" Type="Protein" GroupRef="f6431"> <Attribute Key="cellular_location" Value="nucleoplasm" /> <Attribute Key="complex_id" Value="R-HSA-177673" /> <Attribute Key="copies_num" Value="1" /> <Graphics CenterX="240.0" CenterY="1697.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="P19838" /> </DataNode> <DataNode TextLabel="C3AR1" GraphId="d1a23" Type="Protein"> <Attribute Key="cellular_location" Value="plasma membrane" /> <Graphics CenterX="830.0" CenterY="334.0" Width="48.0" Height="22.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="Q16581" /> </DataNode> <DataNode TextLabel="TXN" GraphId="d2ded" Type="Protein"> <Attribute Key="cellular_location" Value="cytosol" /> <Graphics CenterX="1105.5" CenterY="735.0" Width="33.0" Height="22.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="P10599" /> </DataNode> <DataNode TextLabel="RELA " GraphId="d333b" Type="Protein" GroupRef="f6431"> <Attribute Key="cellular_location" Value="nucleoplasm" /> <Attribute Key="complex_id" Value="R-HSA-177673" /> <Attribute Key="copies_num" Value="1" /> <Graphics CenterX="240.0" CenterY="1737.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="Q04206" /> </DataNode> <DataNode TextLabel="ATP" GraphId="d3718" Type="Metabolite"> <Attribute Key="cellular_location" Value="extracellular region" /> <Graphics CenterX="1072.5" CenterY="271.0" Width="39.0" Height="30.0" ZOrder="32768" FontSize="10" Valign="Middle" Color="0000ff" /> <Xref Database="ChEBI" ID="CHEBI:30616" /> </DataNode> <DataNode TextLabel="ENTPD5 " GraphId="d3eb4" Type="Protein" GroupRef="a9ad9"> <Attribute Key="cellular_location" Value="extracellular region" /> <Attribute Key="complex_id" Value="R-HSA-8851367" /> <Attribute Key="copies_num" Value="1" /> <Graphics CenterX="100.0" CenterY="1857.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="O75356" /> </DataNode> <DataNode TextLabel="2xMyri-IL1A " GraphId="d5c6f" Type="Protein" GroupRef="e5a79"> <Attribute Key="cellular_location" Value="cytosol" /> <Attribute Key="complex_id" Value="R-HSA-449063" /> <Attribute Key="copies_num" Value="2" /> <Graphics CenterX="520.0" CenterY="1217.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="P01583" /> </DataNode> <DataNode TextLabel="NLRP3 elicitor small&#xA;molecules" GraphId="d6ce6" Type="Complex"> <Comment Source="Reactome">Several intact viruses, fungi and bacteria can induce NLRP3 activation, as can human proteins such as beta-amyloid (Schroder &amp; Tschopp 2010).</Comment> <BiopaxRef>b0b</BiopaxRef> <BiopaxRef>efd</BiopaxRef> <BiopaxRef>ae7</BiopaxRef> <Attribute Key="cellular_location" Value="cytosol" /> <Graphics CenterX="1152.0" CenterY="977.0" Width="128.0" Height="36.0" ZOrder="32768" FontSize="10" Valign="Middle" ShapeType="RoundedRectangle" Color="a52a2a" /> <Xref Database="Reactome" ID="R-ALL-877245" /> </DataNode> <DataNode TextLabel="GDP " GraphId="d6e1e" Type="Metabolite" GroupRef="ca855"> <Attribute Key="cellular_location" Value="extracellular region" /> <Attribute Key="complex_id" Value="R-ALL-8936165" /> <Attribute Key="copies_num" Value="1" /> <Graphics CenterX="100.0" CenterY="1517.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" Color="0000ff" /> <Xref Database="ChEBI" ID="CHEBI:17552" /> </DataNode> <DataNode TextLabel="CASP1(317-404) " GraphId="d72a1" Type="Protein" GroupRef="f3a6c"> <Attribute Key="cellular_location" Value="cytosol" /> <Attribute Key="complex_id" Value="R-HSA-448695" /> <Attribute Key="copies_num" Value="1" /> <Graphics CenterX="380.0" CenterY="1797.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="P29466" /> </DataNode> <DataNode TextLabel="IL1A(1-112) " GraphId="d77f3" Type="Protein" GroupRef="d2ec9"> <Attribute Key="cellular_location" Value="cytosol" /> <Attribute Key="complex_id" Value="R-HSA-449026" /> <Attribute Key="copies_num" Value="2" /> <Graphics CenterX="520.0" CenterY="1317.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="P01583" /> </DataNode> <DataNode TextLabel="IL1B " GraphId="d7c51" Type="Protein" GroupRef="d226d"> <Attribute Key="cellular_location" Value="extracellular region" /> <Attribute Key="complex_id" Value="R-HSA-449027" /> <Attribute Key="copies_num" Value="1" /> <Graphics CenterX="520.0" CenterY="1477.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="P01584" /> </DataNode> <DataNode TextLabel="Oxidized&#xA;thioredoxin:TXNIP" GraphId="d7d79" Type="Complex"> <Attribute Key="cellular_location" Value="cytosol" /> <Graphics CenterX="798.5" CenterY="765.0" Width="115.0" Height="36.0" ZOrder="32768" FontSize="10" Valign="Middle" ShapeType="Hexagon" Color="a52a2a" /> <Xref Database="Reactome" ID="R-HSA-1250249" /> </DataNode> <DataNode TextLabel="NPTDase5:Ca2+,Mg2+" GraphId="d86f9" Type="Complex"> <BiopaxRef>d75</BiopaxRef> <BiopaxRef>fd3</BiopaxRef> <Attribute Key="cellular_location" Value="extracellular region" /> <Graphics CenterX="432.5" CenterY="86.0" Width="107.0" Height="36.0" ZOrder="32768" FontSize="10" Valign="Middle" ShapeType="Hexagon" Color="a52a2a" /> <Xref Database="Reactome" ID="R-HSA-8851367" /> </DataNode> <DataNode TextLabel="ATP:P2X4,7 trimer" GraphId="d8f97" Type="Complex"> <Attribute Key="cellular_location" Value="plasma membrane" /> <Graphics CenterX="1435.5" CenterY="335.0" Width="115.0" Height="22.0" ZOrder="32768" FontSize="10" Valign="Middle" ShapeType="Hexagon" Color="a52a2a" /> <Xref Database="Reactome" ID="R-HSA-9665556" /> </DataNode> <DataNode TextLabel="IL18 " GraphId="d9689" Type="Protein" GroupRef="e5a79"> <Attribute Key="cellular_location" Value="cytosol" /> <Attribute Key="complex_id" Value="R-HSA-449063" /> <Attribute Key="copies_num" Value="1" /> <Graphics CenterX="520.0" CenterY="1197.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="Q14116" /> </DataNode> <DataNode TextLabel="CASP1(298-316)" GraphId="da8c2" Type="Protein"> <Attribute Key="cellular_location" Value="cytosol" /> <Graphics CenterX="1276.0" CenterY="635.0" Width="106.0" Height="22.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="P29466" /> </DataNode> <DataNode TextLabel="NLRP3" GraphId="db38e" Type="Protein"> <Attribute Key="cellular_location" Value="cytosol" /> <Graphics CenterX="926.0" CenterY="884.0" Width="46.0" Height="22.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="Q96P20" /> </DataNode> <DataNode TextLabel="Pyrin trimer" GraphId="db5f1" Type="Complex"> <Attribute Key="cellular_location" Value="cytosol" /> <Graphics CenterX="429.5" CenterY="691.0" Width="77.0" Height="22.0" ZOrder="32768" FontSize="10" Valign="Middle" ShapeType="Hexagon" Color="a52a2a" /> <Xref Database="Reactome" ID="R-HSA-879202" /> </DataNode> <DataNode TextLabel="uridine 5'-monophosphate " GraphId="dc4b1" Type="Metabolite" GroupRef="afb60"> <Attribute Key="cellular_location" Value="extracellular region" /> <Attribute Key="complex_id" Value="R-ALL-8851369" /> <Attribute Key="copies_num" Value="1" /> <Graphics CenterX="100.0" CenterY="1637.0" Width="100.0" Height="40.0" ZOrder="32768" FontSize="10" Valign="Middle" Color="0000ff" /> <Xref Database="ChEBI" ID="CHEBI:16695" /> </DataNode> <DataNode TextLabel="Interleukin-1 family&#xA;propeptides" GraphId="dc959" Type="Complex"> <Attribute Key="cellular_location" Value="cytosol" /> <Graphics CenterX="1380.5" CenterY="915.0" Width="129.0" Height="36.0" ZOrder="32768" FontSize="10" Valign="Middle" ShapeType="RoundedRectangle" Color="a52a2a" /> <Xref Database="Reactome" ID="R-HSA-449039" /> </DataNode> <DataNode TextLabel="MEFV " GraphId="de64c" Type="Protein" GroupRef="f03aa"> <Attribute Key="cellular_location" Value="cytosol" /> <Attribute Key="complex_id" Value="R-HSA-877352" /> <Attribute Key="copies_num" Value="3" /> <Graphics CenterX="380.0" CenterY="1717.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="O15553" /> </DataNode> <DataNode TextLabel="Pi" GraphId="dec77" Type="Metabolite"> <Attribute Key="cellular_location" Value="extracellular region" /> <Graphics CenterX="325.5" CenterY="199.0" Width="27.0" Height="30.0" ZOrder="32768" FontSize="10" Valign="Middle" Color="0000ff" /> <Xref Database="ChEBI" ID="CHEBI:43474" /> </DataNode> <DataNode TextLabel="P2RX7 " GraphId="df323" Type="Protein" GroupRef="e4dd9"> <Attribute Key="cellular_location" Value="plasma membrane" /> <Attribute Key="complex_id" Value="R-HSA-9665556" /> <Attribute Key="copies_num" Value="7" /> <Graphics CenterX="240.0" CenterY="1297.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="Q99572" /> </DataNode> <DataNode TextLabel="IL1A(1-271) " GraphId="df85d" Type="Protein" GroupRef="bc1d3"> <Attribute Key="cellular_location" Value="cytosol" /> <Attribute Key="complex_id" Value="R-HSA-449039" /> <Attribute Key="copies_num" Value="2" /> <Graphics CenterX="380.0" CenterY="1997.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="P01583" /> </DataNode> <DataNode TextLabel="TXNIP " GraphId="e0e6d" Type="Protein" GroupRef="ce18a"> <Attribute Key="cellular_location" Value="cytosol" /> <Attribute Key="complex_id" Value="R-HSA-1250249" /> <Attribute Key="copies_num" Value="1" /> <Graphics CenterX="240.0" CenterY="1637.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="Q9H3M7" /> </DataNode> <DataNode TextLabel="NFKB2(1-454) " GraphId="e0fee" Type="Protein" GroupRef="f6431"> <Attribute Key="cellular_location" Value="nucleoplasm" /> <Attribute Key="complex_id" Value="R-HSA-177673" /> <Attribute Key="copies_num" Value="1" /> <Graphics CenterX="240.0" CenterY="1717.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="Q00653" /> </DataNode> <DataNode TextLabel="NFKB2(1-454) " GraphId="e108a" Type="Protein" GroupRef="f9138"> <Attribute Key="cellular_location" Value="nucleoplasm" /> <Attribute Key="complex_id" Value="R-HSA-177673" /> <Attribute Key="copies_num" Value="1" /> <Graphics CenterX="520.0" CenterY="1397.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="Q00653" /> </DataNode> <DataNode TextLabel="NLRP3 " GraphId="e1a70" Type="Protein" GroupRef="c4368"> <Attribute Key="cellular_location" Value="cytosol" /> <Attribute Key="complex_id" Value="R-HSA-1250285" /> <Attribute Key="copies_num" Value="1" /> <Graphics CenterX="240.0" CenterY="1797.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="Q96P20" /> </DataNode> <DataNode TextLabel="CASP1(1-404)" GraphId="e2564" Type="Protein"> <Attribute Key="cellular_location" Value="cytosol" /> <Graphics CenterX="785.5" CenterY="550.5" Width="101.0" Height="25.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="P29466" /> </DataNode> <DataNode TextLabel="Asb " GraphId="e331e" Type="Metabolite" GroupRef="eb5bc"> <Attribute Key="cellular_location" Value="cytosol" /> <Attribute Key="complex_id" Value="R-ALL-877245" /> <Attribute Key="copies_num" Value="1" /> <Graphics CenterX="240.0" CenterY="1917.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" Color="0000ff" /> <Xref Database="ChEBI" ID="CHEBI:46661" /> </DataNode> <DataNode TextLabel="PYCARD " GraphId="e3812" Type="Protein" GroupRef="b9e81"> <Attribute Key="cellular_location" Value="cytosol" /> <Attribute Key="complex_id" Value="R-HSA-877381" /> <Attribute Key="copies_num" Value="1" /> <Graphics CenterX="380.0" CenterY="1337.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="Q9ULZ3" /> </DataNode> <DataNode TextLabel="SiO2 " GraphId="e42cd" Type="Metabolite" GroupRef="ca02f"> <Attribute Key="cellular_location" Value="cytosol" /> <Attribute Key="complex_id" Value="R-HSA-877226" /> <Attribute Key="copies_num" Value="1" /> <Graphics CenterX="380.0" CenterY="1197.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" Color="0000ff" /> <Xref Database="ChEBI" ID="CHEBI:30563" /> </DataNode> <DataNode TextLabel="CTSG" GraphId="e5a1e" Type="Protein"> <Comment Source="Reactome">After secretion Cathepsin G is extracellular and associated with the plasma membrane.</Comment> <BiopaxRef>ed5</BiopaxRef> <Attribute Key="cellular_location" Value="cytosol" /> <Graphics CenterX="1137.0" CenterY="609.0" Width="40.0" Height="22.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="P08311" /> </DataNode> <DataNode TextLabel="ADP " GraphId="e5d9c" Type="Metabolite" GroupRef="ca855"> <Attribute Key="cellular_location" Value="extracellular region" /> <Attribute Key="complex_id" Value="R-ALL-8936165" /> <Attribute Key="copies_num" Value="1" /> <Graphics CenterX="100.0" CenterY="1557.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" Color="0000ff" /> <Xref Database="ChEBI" ID="CHEBI:456216" /> </DataNode> <DataNode TextLabel="NLRP3 gene" GraphId="e64b1" Type="GeneProduct"> <Attribute Key="cellular_location" Value="nucleoplasm" /> <Graphics CenterX="409.0" CenterY="893.5" Width="78.0" Height="51.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Ensembl" ID="ENSG00000162711" /> </DataNode> <DataNode TextLabel="C3a" GraphId="e6586" Type="Protein"> <Attribute Key="cellular_location" Value="extracellular region" /> <Graphics CenterX="929.5" CenterY="225.0" Width="31.0" Height="22.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="P01024" /> </DataNode> <DataNode TextLabel="Mg2+ " GraphId="e6a9e" Type="Metabolite" GroupRef="a9ad9"> <Attribute Key="cellular_location" Value="extracellular region" /> <Attribute Key="complex_id" Value="R-HSA-8851367" /> <Attribute Key="copies_num" Value="1" /> <Graphics CenterX="100.0" CenterY="1837.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" Color="0000ff" /> <Xref Database="ChEBI" ID="CHEBI:18420" /> </DataNode> <DataNode TextLabel="NLRP3 elicitor small&#xA;molecules:NLRP3" GraphId="e6ff0" Type="Complex"> <Attribute Key="cellular_location" Value="cytosol" /> <Graphics CenterX="811.0" CenterY="992.0" Width="128.0" Height="36.0" ZOrder="32768" FontSize="10" Valign="Middle" ShapeType="Hexagon" Color="a52a2a" /> <Xref Database="Reactome" ID="R-HSA-877226" /> </DataNode> <DataNode TextLabel="MEFV " GraphId="e7411" Type="Protein" GroupRef="fd89b"> <Attribute Key="cellular_location" Value="cytosol" /> <Attribute Key="complex_id" Value="R-HSA-879197" /> <Attribute Key="copies_num" Value="5" /> <Graphics CenterX="380.0" CenterY="1657.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="O15553" /> </DataNode> <DataNode TextLabel="PYCARD " GraphId="e7f83" Type="Protein" GroupRef="bed57"> <Attribute Key="cellular_location" Value="cytosol" /> <Attribute Key="complex_id" Value="R-HSA-925458" /> <Attribute Key="copies_num" Value="1" /> <Graphics CenterX="380.0" CenterY="1437.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="Q9ULZ3" /> </DataNode> <DataNode TextLabel="NLRP3 " GraphId="e83c2" Type="Protein" GroupRef="ca02f"> <Attribute Key="cellular_location" Value="cytosol" /> <Attribute Key="complex_id" Value="R-HSA-877226" /> <Attribute Key="copies_num" Value="1" /> <Graphics CenterX="380.0" CenterY="1237.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="Q96P20" /> </DataNode> <DataNode TextLabel="Asb " GraphId="e9fc2" Type="Metabolite" GroupRef="ca02f"> <Attribute Key="cellular_location" Value="cytosol" /> <Attribute Key="complex_id" Value="R-HSA-877226" /> <Attribute Key="copies_num" Value="1" /> <Graphics CenterX="380.0" CenterY="1217.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" Color="0000ff" /> <Xref Database="ChEBI" ID="CHEBI:46661" /> </DataNode> <DataNode TextLabel="NFkB Complex" GraphId="ebf8c" Type="Complex"> <Attribute Key="cellular_location" Value="nucleoplasm" /> <Graphics CenterX="1506.0" CenterY="955.0" Width="94.0" Height="22.0" ZOrder="32768" FontSize="10" Valign="Middle" ShapeType="Hexagon" Color="a52a2a" /> <Xref Database="Reactome" ID="R-HSA-177673" /> </DataNode> <DataNode TextLabel="Interleukin-1 family" GraphId="ece17" Type="Complex"> <Attribute Key="cellular_location" Value="extracellular region" /> <Graphics CenterX="2042.5" CenterY="951.0" Width="125.0" Height="22.0" ZOrder="32768" FontSize="10" Valign="Middle" ShapeType="RoundedRectangle" Color="a52a2a" /> <Xref Database="Reactome" ID="R-HSA-449027" /> </DataNode> <DataNode TextLabel="IL1B(117-269) " GraphId="ed1c0" Type="Protein" GroupRef="e5a79"> <Attribute Key="cellular_location" Value="cytosol" /> <Attribute Key="complex_id" Value="R-HSA-449063" /> <Attribute Key="copies_num" Value="1" /> <Graphics CenterX="520.0" CenterY="1177.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="P01584" /> </DataNode> <DataNode TextLabel="NRNAM" GraphId="ed751" Type="Metabolite"> <Attribute Key="cellular_location" Value="extracellular region" /> <Graphics CenterX="595.5" CenterY="280.0" Width="61.0" Height="30.0" ZOrder="32768" FontSize="10" Valign="Middle" Color="0000ff" /> <Xref Database="ChEBI" ID="CHEBI:15927" /> </DataNode> <DataNode TextLabel="HSP90AB1" GraphId="edef9" Type="Protein"> <Attribute Key="cellular_location" Value="cytosol" /> <Graphics CenterX="665.5" CenterY="907.0" Width="69.0" Height="22.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="P08238" /> </DataNode> <DataNode TextLabel="adenosine 5'-monophosphate " GraphId="ee155" Type="Metabolite" GroupRef="afb60"> <Attribute Key="cellular_location" Value="extracellular region" /> <Attribute Key="complex_id" Value="R-ALL-8851369" /> <Attribute Key="copies_num" Value="1" /> <Graphics CenterX="100.0" CenterY="1757.0" Width="100.0" Height="40.0" ZOrder="32768" FontSize="10" Valign="Middle" Color="0000ff" /> <Xref Database="ChEBI" ID="CHEBI:16027" /> </DataNode> <DataNode TextLabel="H2O" GraphId="f06ac" Type="Metabolite"> <Attribute Key="cellular_location" Value="extracellular region" /> <Graphics CenterX="519.5" CenterY="219.0" Width="43.0" Height="30.0" ZOrder="32768" FontSize="10" Valign="Middle" Color="0000ff" /> <Xref Database="ChEBI" ID="CHEBI:15377" /> </DataNode> <DataNode TextLabel="NTPDase1:Ca2+,Mg2+" GraphId="f0a24" Type="Complex"> <BiopaxRef>d41</BiopaxRef> <Attribute Key="cellular_location" Value="plasma membrane" /> <Graphics CenterX="277.5" CenterY="336.0" Width="107.0" Height="36.0" ZOrder="32768" FontSize="10" Valign="Middle" ShapeType="Hexagon" Color="a52a2a" /> <Xref Database="Reactome" ID="R-HSA-8850845" /> </DataNode> <DataNode TextLabel="ATP:P2RX4,7" GraphId="f0f67" Type="Complex"> <Comment Source="Reactome">P2X1 protein readily forms stable trimers and hexamers, suggesting that the intact receptor is a multimer of three or six subunits in heterologous expression systems. However,assembly in native cells may be influenced significantly by associated proteins that are not present in heterologous expression systems.</Comment> <Attribute Key="cellular_location" Value="plasma membrane" /> <Graphics CenterX="1249.0" CenterY="336.5" Width="88.0" Height="23.0" ZOrder="32768" FontSize="10" Valign="Middle" ShapeType="Hexagon" Color="a52a2a" /> <Xref Database="Reactome" ID="R-HSA-9660825" /> </DataNode> <DataNode TextLabel="NLRP3 elicitors:NLRP3 oligomer " GraphId="f1b0d" GroupRef="bed57"> <Attribute Key="cellular_location" Value="cytosol" /> <Attribute Key="complex_id" Value="R-HSA-925458" /> <Attribute Key="copies_num" Value="1" /> <Graphics CenterX="380.0" CenterY="1417.0" Width="100.0" Height="40.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Reactome" ID="R-NUL-1296409" /> </DataNode> <DataNode TextLabel="Ca2+ " GraphId="f2927" Type="Metabolite" GroupRef="e055b"> <Attribute Key="cellular_location" Value="extracellular region" /> <Attribute Key="complex_id" Value="R-HSA-8850845" /> <Attribute Key="copies_num" Value="2" /> <Graphics CenterX="100.0" CenterY="1417.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" Color="0000ff" /> <Xref Database="ChEBI" ID="CHEBI:29108" /> </DataNode> <DataNode TextLabel="P2RX4,7" GraphId="f29fd" Type="Complex"> <Attribute Key="cellular_location" Value="plasma membrane" /> <Graphics CenterX="1120.0" CenterY="336.0" Width="60.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" ShapeType="RoundedRectangle" Color="a52a2a" /> <Xref Database="Reactome" ID="R-HSA-9660827" /> </DataNode> <DataNode TextLabel="P2RX4 " GraphId="f4cab" Type="Protein" GroupRef="a4673"> <Attribute Key="cellular_location" Value="plasma membrane" /> <Attribute Key="complex_id" Value="R-HSA-9660825" /> <Attribute Key="copies_num" Value="1" /> <Graphics CenterX="100.0" CenterY="1317.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="Q99571" /> </DataNode> <DataNode TextLabel="NMN" GraphId="f5b19" Type="Metabolite"> <Attribute Key="cellular_location" Value="extracellular region" /> <Graphics CenterX="787.5" CenterY="270.0" Width="45.0" Height="30.0" ZOrder="32768" FontSize="10" Valign="Middle" Color="0000ff" /> <Xref Database="ChEBI" ID="CHEBI:14649" /> </DataNode> <DataNode TextLabel="SUGT1 " GraphId="f69fd" Type="Protein" GroupRef="bb9c1"> <Attribute Key="cellular_location" Value="cytosol" /> <Attribute Key="complex_id" Value="R-HSA-874086" /> <Attribute Key="copies_num" Value="1" /> <Graphics CenterX="240.0" CenterY="1477.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="Q9Y2Z0" /> </DataNode> <DataNode TextLabel="TXNIP" GraphId="f6f97" Type="Protein"> <Attribute Key="cellular_location" Value="cytosol" /> <Graphics CenterX="1055.5" CenterY="765.0" Width="43.0" Height="22.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="Q9H3M7" /> </DataNode> <DataNode TextLabel="ATP" GraphId="f8428" Type="Metabolite"> <Attribute Key="cellular_location" Value="cytosol" /> <Graphics CenterX="1074.5" CenterY="477.0" Width="39.0" Height="30.0" ZOrder="32768" FontSize="10" Valign="Middle" Color="0000ff" /> <Xref Database="ChEBI" ID="CHEBI:30616" /> </DataNode> <DataNode TextLabel="P2RX7 " GraphId="f84bd" Type="Protein" GroupRef="a4673"> <Attribute Key="cellular_location" Value="plasma membrane" /> <Attribute Key="complex_id" Value="R-HSA-9660825" /> <Attribute Key="copies_num" Value="1" /> <Graphics CenterX="100.0" CenterY="1337.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="Q99572" /> </DataNode> <DataNode TextLabel="Pi" GraphId="f8fb8" Type="Metabolite"> <Attribute Key="cellular_location" Value="extracellular region" /> <Graphics CenterX="597.5" CenterY="220.0" Width="27.0" Height="30.0" ZOrder="32768" FontSize="10" Valign="Middle" Color="0000ff" /> <Xref Database="ChEBI" ID="CHEBI:43474" /> </DataNode> <DataNode TextLabel="NFkB Complex" GraphId="f9ff3" Type="Complex"> <Attribute Key="cellular_location" Value="nucleoplasm" /> <Graphics CenterX="766.0" CenterY="842.0" Width="94.0" Height="22.0" ZOrder="32768" FontSize="10" Valign="Middle" ShapeType="Hexagon" Color="a52a2a" /> <Xref Database="Reactome" ID="R-HSA-177673" /> </DataNode> <DataNode TextLabel="P2RX4 " GraphId="fbf9f" Type="Protein" GroupRef="b5789"> <Attribute Key="cellular_location" Value="plasma membrane" /> <Attribute Key="complex_id" Value="R-HSA-9660827" /> <Attribute Key="copies_num" Value="1" /> <Graphics CenterX="100.0" CenterY="1217.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="Q99571" /> </DataNode> <DataNode TextLabel="Thioredoxin:TXNIP" GraphId="fd7ea" Type="Complex"> <Attribute Key="cellular_location" Value="cytosol" /> <Graphics 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Database="ChEBI" ID="CHEBI:16336" /> </DataNode> <Interaction GraphId="a0650"> <Comment Source="Reactome">NTPDase5 (CD39L4), encoded by the ENTPD5 gene, is an E-NTPDase family member that is secreted to the extracellular space where it hydrolyzes nucleoside diphosphates UDP, GDP, CDP and ADP (listed in the order of preference) to nucleoside monophosphates UMP, GMP, CMP and AMP, respectively. In vitro, NTPDase5 can hydrolyze nucleoside triphosphates GTP, CTP, UTP and ATP to corresponding nucleoside diphosphates but with very low efficiency. NTPDase5 requires Ca2+ or Mg2+ for catalytic activity (Mulero et al. 1999). NTPDase5 is most catalytically active as a monomer, although it can also form disulfide-linked dimers (Mulero et al. 2000).&lt;p&gt;NTPDase5 may function in the endoplasmic reticulum (ER), where its UDPase activity could contribute to protein glycosylation and folding. NTPDase5 may alleviate ER stress induced by protein overload caused by oncogenic PI3K/AKT signaling in cancer cells. NTPDase5 is over-expressed in tumors with activated AKT and is known as the PCPH oncogene. The underlying mechanism of NTPDase5 over-expression may be AKT-mediated inhibition of FOXO proteins, which are probable transcriptional repressors of the ENTPD5 gene (Fang et al. 2010, Shen et al. 2011). </Comment> <BiopaxRef>fd3</BiopaxRef> <BiopaxRef>d75</BiopaxRef> <BiopaxRef>c50</BiopaxRef> <BiopaxRef>c13</BiopaxRef> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="478.0" Y="189.0" /> <Point X="400.0" Y="189.0" /> <Anchor Position="0.0" Shape="None" GraphId="fd863" /> <Anchor Position="0.99" Shape="None" GraphId="b4225" /> <Anchor Position="0.5" Shape="None" GraphId="db08d" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-8851356" /> </Interaction> <Interaction GraphId="a06c1"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="1088.0" Y="977.0" GraphRef="d6ce6" RelX="-1.0" RelY="0.0" /> <Point X="1031.0" Y="976.0" GraphRef="a204e" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-1306876" /> </Interaction> <Interaction GraphId="a1529"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="1224.0" Y="322.0" GraphRef="e7901" RelX="0.650000000000091" RelY="0.29000000000002046" /> <Point X="1205.0" Y="336.0" GraphRef="f0f67" RelX="-1.0" RelY="-0.043478260869565216" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-9660822" /> </Interaction> <Interaction GraphId="a432c"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="964.0" Y="706.0" GraphRef="de44f" RelX="-0.7999999999999545" RelY="0.01999999999998181" /> <Point X="960.0" Y="707.0" GraphRef="c8560" RelX="0.9746835443037974" RelY="0.0" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-1250280" /> </Interaction> <Interaction GraphId="a5bfb"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="1459.0" Y="955.0" GraphRef="ebf8c" RelX="-1.0" RelY="0.0" /> <Point X="1505.0" Y="914.0" GraphRef="ca781" RelX="7.0" RelY="0.0" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-448703" /> </Interaction> <Interaction GraphId="a65ab"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="432.0" Y="104.0" GraphRef="d86f9" RelX="-0.009345794392523364" RelY="1.0" /> <Point X="435.0" Y="189.0" GraphRef="db08d" RelX="-4.0" RelY="0.0" ArrowHead="mim-catalysis" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-8851356" /> </Interaction> <Interaction GraphId="a7b23"> <Comment Source="Reactome">Procaspase-1 is recruited via a CARD-CARD interaction with ASC. This creates procaspase-1 clustering which is believed to stimulate procaspase-1 autocleavage, generating the p10/p20 fragments that assemble into the active capsase-1 tetramer (Schroder &amp; Tschopp, 2010).</Comment> <BiopaxRef>a2a</BiopaxRef> <BiopaxRef>f9c</BiopaxRef> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="850.0" Y="621.0" /> <Point X="929.0" Y="621.0" /> <Anchor Position="0.0" Shape="None" GraphId="c4180" /> <Anchor Position="0.99" Shape="None" GraphId="e4b42" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-844612" /> </Interaction> <Interaction GraphId="a8470"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="161.0" Y="202.0" GraphRef="cc52e" RelX="0.9534883720930233" RelY="0.0" /> <Point X="200.0" Y="224.0" GraphRef="f70e0" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-8850846" /> </Interaction> <Interaction GraphId="a8a0a"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="1293.0" Y="336.0" GraphRef="f0f67" RelX="1.0" RelY="-0.043478260869565216" /> <Point X="1296.0" Y="335.0" GraphRef="f14b1" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-9665515" /> </Interaction> <Interaction GraphId="aaff5"> <Comment Source="Reactome">The presence of reactive oxygen species (ROS) leads to the oxidation of thioredoxin and consequent release of TXNIP (Zhou et al. 2010). The source of the ROS is unclear but they are known to be essential for caspase-1 activation (Cruz et al. 2007) and are produced in response to all known NLRP3 activators (Dostert et al. 2008, Zhou et al. 2010). The freed TXNIP binds NLRP3 and is proposed to activate the NLRP3 inflammasome, explaining how ROS can bring about NLRP3 activation.</Comment> <BiopaxRef>e8c</BiopaxRef> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="1044.0" Y="704.0" /> <Point X="964.0" Y="706.0" /> <Anchor Position="0.0" Shape="None" GraphId="c00c0" /> <Anchor Position="0.99" Shape="None" GraphId="de44f" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-1250280" /> </Interaction> <Interaction GraphId="ab060"> <Comment Source="Reactome">ROS induce the dissociation of TXNIP from thioredoxin, freeing TXNIP to subsequently bind NLRP3 and bring about activation of the NLRP3 inflammasome (Zhou et al. 2010). </Comment> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="859.0" Y="765.0" /> <Point X="935.0" Y="765.0" /> <Anchor Position="0.0" Shape="None" GraphId="df585" /> <Anchor Position="0.99" Shape="None" GraphId="bc302" /> </Graphics> <Xref 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GraphRef="add92" RelX="-1.0" RelY="0.0" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-873951" /> </Interaction> <Interaction GraphId="ae82b"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="835.0" Y="550.0" GraphRef="e2564" RelX="0.9801980198019802" RelY="-0.04" /> <Point X="850.0" Y="621.0" GraphRef="c4180" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-844612" /> </Interaction> <Interaction GraphId="ae959"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="929.0" Y="236.0" GraphRef="e6586" RelX="-0.03225806451612903" RelY="1.0" /> <Point X="893.0" Y="299.0" GraphRef="eaad8" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-444647" /> </Interaction> <Interaction GraphId="b0a0f"> <Comment Source="Reactome">NTPDase1 (CD39) is a plasma membrane-bound ectonucleotidase encoded by the ENTPD1 gene that hydrolyzes extracellular NTPs to NMPs, via corresponding NDP intermediates (Lemmens et al. 2000, Kukulski et al. 2005). NTPDase1 is expressed on endothelial cells, smooth muscle cells and most leukocytes. The vascular endothelial NTPDase1 regulates platelet aggregation and thrombosis (Kaczmarek et al. 1996, Enjoyji et al. 1999). In mice, NTPDase1 is expressed at the surface of epidermal dendritic cells (Langerhans cells) and is involved in regulation of immune response to skin irritants (Mizumoto et al. 2002). NTPDase1 expressed in vascular smooth muscle cells regulates vasomotion (Kauffenstein et al. 2010, reviewed by Kukulski et al. 2011). In regulatory T lymphocytes (Tregs) and other leukocytes NTPDase1 regulates inflammatory processes (Deaglio et al. 2007). </Comment> <BiopaxRef>d41</BiopaxRef> <BiopaxRef>e32</BiopaxRef> <BiopaxRef>c1b</BiopaxRef> <BiopaxRef>a53</BiopaxRef> <BiopaxRef>b78</BiopaxRef> <BiopaxRef>d19</BiopaxRef> <BiopaxRef>ed0</BiopaxRef> <BiopaxRef>b47</BiopaxRef> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="200.0" Y="224.0" /> <Point X="254.0" Y="224.0" /> <Anchor Position="0.0" Shape="None" GraphId="f70e0" /> <Anchor Position="0.99" Shape="None" GraphId="fc497" /> <Anchor Position="0.5" Shape="None" GraphId="d670c" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-8850846" /> </Interaction> <Interaction GraphId="b103e"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="224.0" Y="336.0" GraphRef="f0a24" RelX="-1.0" RelY="0.0" /> <Point X="233.0" Y="225.0" GraphRef="d670c" RelX="6.0" RelY="1.0" ArrowHead="mim-catalysis" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-8850846" /> </Interaction> <Interaction GraphId="b2a37"> <Comment Source="Reactome">Pro-interleukin-1 beta (pro-IL1B) is the primary substrate of caspase-1. IL1B production and processing is stimulated when pathogen-associated molecular patterns (PAMPs) such as bacterial LPS are detected by cells of the innate immune system, and in response to pro-inflammatory cytokines such as TNF. Detection of PAMPs by Toll receptors leads to rapid IL1 transcription/translation and subsequent processing by caspase-1 in macrophages and monocytes. Processing is triggered by the activation of members of the NLR family and their associated inflammasome complexes. IL1B lacks a signal peptide to direct it to the Golgi for subsequent secretion, so the mode of secretion is uncertain. Once secreted, IL1B binds membrane-bound IL1 receptors, followed by recruitment of the IL1 receptor accessory protein to form a high affinity receptor complex. Ligand induced receptor activation induces the intracellular association of a number of cytosolic adapter proteins triggering intracellular signal transduction. This series of steps facilitates the induction of nuclear factor-kappa B (NFkB) and mitogen-activated protein kinase (MAPK) activity, leading to downstream transcription of additional inflammatory cytokines, including IL1B itself. A calpain-like potease has been reported to be important for the processing of pro- IL1A, but much less is known about how IL1A is released from cells and what specific roles it plays in biology.</Comment> <BiopaxRef>a0d</BiopaxRef> <BiopaxRef>f41</BiopaxRef> <BiopaxRef>ae9</BiopaxRef> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="1451.0" Y="914.0" /> <Point X="1545.0" Y="914.0" /> <Anchor Position="0.0" Shape="None" GraphId="c0aa1" /> <Anchor Position="0.99" Shape="None" GraphId="a70ee" /> <Anchor Position="0.5" Shape="None" GraphId="dc9b8" /> <Anchor Position="0.5" Shape="None" GraphId="ca781" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-448703" /> </Interaction> <Interaction GraphId="b3966"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="1117.0" Y="609.0" GraphRef="e5a1e" RelX="-1.0" RelY="0.0" /> <Point X="1138.0" Y="554.0" GraphRef="f43b8" RelX="125.0" RelY="1.5" ArrowHead="mim-catalysis" /> </Graphics> 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ID="R-HSA-8850846" /> </Interaction> <Interaction GraphId="bd156"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="948.0" Y="335.0" GraphRef="e89e3" RelX="0.5499999999999545" RelY="0.36000000000001364" /> <Point X="951.0" Y="335.0" GraphRef="b3e19" RelX="-1.0" RelY="0.0" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-444647" /> </Interaction> <Interaction GraphId="bf8da"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="429.0" Y="702.0" GraphRef="db5f1" RelX="-0.012987012987012988" RelY="1.0" /> <Point X="452.0" Y="738.0" GraphRef="cdeb8" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-879221" /> </Interaction> <Interaction GraphId="bfe55"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="685.0" Y="961.0" GraphRef="c0c93" RelX="0.9574468085106383" RelY="0.0" /> <Point X="688.0" Y="931.0" GraphRef="b4651" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-874087" /> </Interaction> <Interaction GraphId="c1867"> <Comment Source="Reactome">TXNIP interacts with the redox-active domain of thioredoxin (TRX) and is believed to act as an oxidative stress mediator by inhibiting TRX activity or by limiting its bioavailability (Nishiyama et al. 1999, Liyanage et al. 2007).</Comment> <BiopaxRef>ac2</BiopaxRef> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="1098.0" Y="793.0" /> <Point X="1176.0" Y="793.0" /> <Anchor Position="0.0" Shape="None" GraphId="d9c89" /> <Anchor Position="0.99" Shape="None" GraphId="ce6a6" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-1250264" /> </Interaction> <Interaction GraphId="c48cc"> <Comment Source="Reactome">Two p10/p20 dimers associate to form the active tetramer</Comment> <BiopaxRef>a74</BiopaxRef> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="1505.0" Y="723.0" /> <Point X="1505.0" Y="836.0" /> <Anchor 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Reactive oxygen species (ROS) such as H2O2 increase this interaction, while the ROS inhibitor APDC blocks it (Zhou et al. 2010). This interaction is proposed to activate the NLRP3 inflammasome.</Comment> <BiopaxRef>e8c</BiopaxRef> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="1054.0" Y="883.0" /> <Point X="1138.0" Y="884.0" /> <Anchor Position="0.0" Shape="None" GraphId="cfa8b" /> <Anchor Position="0.99" Shape="None" GraphId="acb20" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-1250272" /> </Interaction> <Interaction GraphId="c575c"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="1150.0" Y="336.0" GraphRef="f29fd" RelX="1.0" RelY="0.0" /> <Point X="1159.0" Y="293.0" GraphRef="f18fb" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-9660822" /> </Interaction> <Interaction GraphId="c5921"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="929.0" Y="621.0" GraphRef="e4b42" RelX="0.7899999999999636" RelY="0.0" /> <Point X="932.0" Y="621.0" GraphRef="c0f59" RelX="-1.0" RelY="0.0" 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GraphRef="f44ca" RelX="0.8300000000000409" RelY="0.0" /> <Point X="774.0" Y="932.0" GraphRef="bdb56" RelX="-1.0" RelY="0.0" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-874087" /> </Interaction> <Interaction GraphId="cde8b"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="1076.0" Y="765.0" GraphRef="f6f97" RelX="0.9534883720930233" RelY="0.0" /> <Point X="1098.0" Y="793.0" GraphRef="d9c89" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-1250264" /> </Interaction> <Interaction GraphId="cdefb"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="813.0" Y="622.0" GraphRef="c36ee" RelX="0.9844961240310077" RelY="0.0" /> <Point X="850.0" Y="621.0" GraphRef="c4180" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-844612" /> </Interaction> <Interaction GraphId="ce7c1"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="1072.0" Y="289.0" GraphRef="a63a7" RelX="-0.009999999999990905" RelY="-1.6999999999999886" /> <Point X="1072.0" Y="286.0" GraphRef="d3718" RelX="-0.02564102564102564" RelY="1.0" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-9665524" /> </Interaction> <Interaction GraphId="cf4c7"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="1439.0" Y="849.0" GraphRef="b1918" RelX="-1.0" RelY="-0.047619047619047616" /> <Point X="1505.0" Y="914.0" GraphRef="dc9b8" RelX="7.0" RelY="0.0" ArrowHead="mim-catalysis" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-448703" /> </Interaction> <Interaction GraphId="cf718"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="949.0" Y="974.0" GraphRef="c7f99" RelX="-0.8199999999999363" RelY="-0.01999999999998181" /> <Point X="875.0" Y="992.0" GraphRef="e6ff0" RelX="1.0" RelY="0.0" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-1306876" /> </Interaction> <Interaction GraphId="d02e1"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="1031.0" Y="944.0" GraphRef="add92" RelX="-0.007751937984496124" RelY="1.0" /> <Point X="1031.0" Y="976.0" GraphRef="a204e" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-1306876" /> </Interaction> <Interaction GraphId="d0859"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="855.0" Y="765.0" GraphRef="d7d79" RelX="0.9826086956521739" RelY="0.0" /> <Point X="859.0" Y="765.0" GraphRef="df585" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-1250253" /> </Interaction> <Interaction GraphId="d11ef"> <Comment Source="Reactome">The ubiquitin ligase–associated protein SGT1 (SUGT1) has two putative HSP90 binding domains, a tetratricopeptide repeat and a p23-like CHORD and Sgt1 (CS) domain. The CS domain of human SGT1 physically interacts with HSP90. SGT1 and related proteins are believed to recruit heat shock proteins to multiprotein assemblies (Lee et al. 2004).</Comment> <BiopaxRef>b00</BiopaxRef> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="688.0" Y="931.0" /> <Point X="771.0" Y="931.0" /> <Anchor Position="0.0" Shape="None" GraphId="b4651" /> <Anchor Position="0.99" Shape="None" GraphId="f44ca" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-874087" /> </Interaction> <Interaction GraphId="d504b"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="1025.0" Y="335.0" GraphRef="b3e19" RelX="0.9733333333333334" RelY="0.0" /> <Point X="1072.0" Y="383.0" GraphRef="fcdcb" RelX="-0.5" RelY="9.0" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-9665524" /> </Interaction> <Interaction GraphId="d6ed1"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="699.0" Y="907.0" GraphRef="edef9" RelX="0.9710144927536232" RelY="0.0" /> <Point X="688.0" Y="931.0" GraphRef="b4651" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-874087" /> </Interaction> <Interaction GraphId="d92df"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="1187.0" Y="555.0" GraphRef="c63e7" RelX="3.480000000000018" RelY="0.049999999999954525" /> <Point X="1223.0" Y="635.0" GraphRef="da8c2" RelX="-1.0" RelY="0.0" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-448678" /> </Interaction> <Interaction GraphId="da975"> <Comment Source="Reactome">NLRP3 interacts with ASC (Manji et al. 2003) via their PYD domains (Dowds et al. 2004). NLRP3 oligomerization leads to PYD domain clustering which is believed to facilitate the interaction of NLRP3 with the PYD domain of ASC (Schroder &amp; Tschopp, 2010).</Comment> <BiopaxRef>fa2</BiopaxRef> <BiopaxRef>e58</BiopaxRef> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="582.0" Y="622.0" /> <Point X="682.0" Y="622.0" /> <Anchor Position="0.0" Shape="None" GraphId="eb8d0" /> <Anchor Position="0.99" Shape="None" GraphId="ac100" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-844610" /> </Interaction> <Interaction GraphId="daf20"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="1074.0" Y="462.0" GraphRef="f8428" RelX="-0.02564102564102564" RelY="-1.0" /> <Point X="1073.0" Y="459.0" GraphRef="dd7a3" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-9665524" /> </Interaction> <Interaction GraphId="db575"> <Comment Source="Reactome">Trimeric pyrin interacts with ASC through its Pyrin domains, leading to oligomerization of ASC. This interaction interferes with the ability of NLRP3 (Cyropyrin) to associate with ASC and thus inhibits inflammasome activation (Chae et al. 2003).</Comment> <BiopaxRef>c54</BiopaxRef> <BiopaxRef>e58</BiopaxRef> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="498.0" Y="691.0" /> <Point X="581.0" Y="690.0" /> <Anchor Position="0.0" Shape="None" GraphId="a0206" /> <Anchor Position="0.99" Shape="None" GraphId="e587b" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-877361" /> </Interaction> <Interaction GraphId="dc407"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="1187.0" Y="555.0" GraphRef="c63e7" RelX="3.480000000000018" RelY="0.049999999999954525" /> <Point X="1259.0" Y="558.0" GraphRef="be7a8" RelX="-1.0" RelY="0.0" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-448678" /> </Interaction> <Interaction GraphId="dcbcb"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="1187.0" Y="555.0" GraphRef="c63e7" RelX="3.480000000000018" RelY="0.049999999999954525" /> <Point X="1257.0" Y="597.0" GraphRef="a9cd7" RelX="-1.0" RelY="0.0" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-448678" /> </Interaction> <Interaction GraphId="dd8d3"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="935.0" Y="765.0" GraphRef="bc302" RelX="0.7599999999999909" RelY="0.0" /> <Point X="921.0" Y="720.0" GraphRef="c8560" RelX="-0.012658227848101266" RelY="1.0" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-1250253" /> </Interaction> <Interaction GraphId="de1b9"> <Comment Source="Reactome">Caspase 1 is expressed as a precursor that is cleaved to generate the p10 and p20 subunits that subsequently form the active tetramer. </Comment> <BiopaxRef>a74</BiopaxRef> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="839.0" Y="550.0" /> <Point X="1187.0" Y="555.0" /> <Anchor Position="0.0" Shape="None" GraphId="edb3a" /> <Anchor Position="0.99" Shape="None" GraphId="c63e7" /> <Anchor Position="0.5" Shape="None" GraphId="f43b8" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-448678" /> </Interaction> <Interaction GraphId="de96b"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="643.0" Y="252.0" GraphRef="f4bb7" RelX="-0.7599999999999909" RelY="0.009999999999990905" /> <Point X="625.0" Y="280.0" GraphRef="ed751" RelX="0.9672131147540983" RelY="0.0" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-8940074" /> </Interaction> <Interaction GraphId="dfe12"> <Comment Source="Reactome">It has been shown that anaphylatoxin C3a binding to its receptor C3AR1 indirectly activates the proinflammatory cytokine IL1β (Laudisi, 2013 and Asgari, 2013). Asgari et al. suggest a mechanism; after the binding of C3a to C3AR1, ATP release is promoted from the cytosol to the extracellular space through an unknown channel. From here, ATP binding to P2X purinoceptors activates the inflammasome that results in the production of IL1β (Asgari 2013).</Comment> <BiopaxRef>e60</BiopaxRef> <BiopaxRef>d38</BiopaxRef> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="1073.0" Y="459.0" /> <Point X="1072.0" Y="289.0" /> <Anchor Position="0.0" Shape="None" GraphId="dd7a3" /> <Anchor Position="0.99" Shape="None" GraphId="a63a7" /> <Anchor Position="0.5" Shape="None" GraphId="fcdcb" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-9665524" /> </Interaction> <Interaction GraphId="e080d"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="1098.0" Y="683.0" GraphRef="b0704" RelX="-1.0" RelY="0.0" /> <Point X="1044.0" Y="704.0" GraphRef="c00c0" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-1250280" /> </Interaction> <Interaction GraphId="e14bf"> <Comment Source="Reactome">Proline-serine-threonine phosphatase-interacting protein 1 (PSTPIP1) is a pyrin-binding protein, involved in regulation of the actin cytoskeleton (Li et al. 1998) and suggested as a regulator of inflammasome activation (Khare et al. 2010). A naturally occurring mutation of PSTPIP1 where Y344 is replaced by F blocks tyrosine phosphorylation and reduces pyrin binding. Mutations of PSTPIP1 that increase pyrin binding are associated with the inflammatory syndrome pyogenic arthritis, pyoderma gangrenosum, and acne (PAPA). Expression of PSTPIP1 with these mutations in THP-11 cells resulted in substantially increased caspase-1 activation and IL-1beta secretion. PSTPIP1 binding to pyrin is believed to promote the unmasking of its PYD domain and enhance interactions with ASC, facilitating ASC oligomerization and caspase-1 recruitment (Yu et al. 2007).</Comment> <BiopaxRef>bff</BiopaxRef> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="452.0" Y="738.0" /> <Point X="521.0" Y="739.0" /> <Anchor Position="0.0" Shape="None" GraphId="cdeb8" /> <Anchor Position="0.99" Shape="None" GraphId="fd457" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-879221" /> </Interaction> <Interaction GraphId="e3a16"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="949.0" Y="884.0" GraphRef="db38e" RelX="1.0" RelY="0.0" /> <Point X="1054.0" Y="883.0" GraphRef="cfa8b" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-1250272" /> </Interaction> <Interaction GraphId="e3a82"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="1089.0" Y="735.0" GraphRef="d2ded" RelX="-1.0" RelY="0.0" /> <Point X="1044.0" Y="704.0" GraphRef="c00c0" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-1250280" /> </Interaction> <Interaction GraphId="e5002"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="1187.0" Y="555.0" GraphRef="c63e7" RelX="3.480000000000018" RelY="0.049999999999954525" /> <Point X="1168.0" Y="515.0" GraphRef="cc121" RelX="-1.0" RelY="0.0" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-448678" /> </Interaction> <Interaction GraphId="e5bfd"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="1375.0" Y="334.0" GraphRef="b65f4" RelX="0.7899999999999636" RelY="-0.009999999999990905" /> <Point X="1378.0" Y="335.0" GraphRef="d8f97" RelX="-1.0" RelY="0.0" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-9665515" /> </Interaction> <Interaction GraphId="e6b17"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="949.0" Y="974.0" GraphRef="c7f99" RelX="-0.8199999999999363" RelY="-0.01999999999998181" /> <Point X="862.0" Y="932.0" GraphRef="bdb56" RelX="1.0" RelY="0.0" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-1306876" /> </Interaction> <Interaction GraphId="e84c2"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="765.0" Y="270.0" GraphRef="f5b19" RelX="-1.0" RelY="0.0" /> <Point X="719.0" Y="251.0" GraphRef="b3705" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-8940074" /> </Interaction> <Interaction GraphId="e9b89"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="538.0" Y="572.0" GraphRef="a747f" RelX="1.0" RelY="0.0" /> <Point X="582.0" Y="622.0" GraphRef="eb8d0" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-844610" /> </Interaction> <Interaction GraphId="ea338"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="854.0" Y="334.0" GraphRef="d1a23" RelX="1.0" RelY="0.0" /> <Point X="893.0" Y="299.0" GraphRef="eaad8" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-444647" /> </Interaction> <Interaction GraphId="eaa1d"> <Comment Source="Reactome">P2X receptors are a family of cation-permeable ligand gated ion channels that open in response to the binding of extracellular adenosine triphosphate (ATP) (Gicquel et al. 2015). All members of the family are thought to be functionally trimeric. </Comment> <BiopaxRef>bcd</BiopaxRef> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="1159.0" Y="293.0" /> <Point X="1224.0" Y="322.0" /> <Anchor Position="0.0" Shape="None" GraphId="f18fb" /> <Anchor Position="0.99" Shape="None" GraphId="e7901" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-9660822" /> </Interaction> <Interaction GraphId="ebce9"> <Comment Source="Reactome">The complement component 3a receptor (C3AR) binds C3a, a 77-amino acid anaphylatoxin generated after proteolytic cleavage of C3 and C5 in response to complement activation. C3a is involved in a variety of inflammatory responses including chemotaxis and activation of granulocytes, mast cells and macrophages (Peng et al. 200, Klos et al. 2009).</Comment> <BiopaxRef>c90</BiopaxRef> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="893.0" Y="299.0" /> <Point X="948.0" Y="335.0" /> <Anchor Position="0.0" Shape="None" GraphId="eaad8" /> <Anchor Position="0.99" Shape="None" GraphId="e89e3" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-444647" /> </Interaction> <Interaction GraphId="efe4e"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="1505.0" Y="836.0" GraphRef="c7218" RelX="0.0" RelY="1.1299999999999955" /> <Point X="1505.0" Y="839.0" GraphRef="b1918" RelX="-0.007518796992481203" RelY="-1.0" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-448702" /> </Interaction> <Interaction GraphId="f05fc"> <Comment Source="Reactome">5'-nucleotidase (NT5E, CD73) is able to hydrolyse extracellular nucleotides into membrane permeable nucleosides. It displays a broad specificity, acting on mono- or di-nucleotide nicotinamides and different adenosine phosphates, with maximal activity on 5'-adenosine monophosphate. Human NT5E can hydrolyse both NAD+ and NMN, suggesting a role in NAD metabolism (Garavaglia et al. 2012). NT5E is a glycolipid-anchored plasma membrane enzyme (Misumi et al. 1990) that is active in dimeric form and requires one zinc ion per subunit (Zimmermann 1992).</Comment> <BiopaxRef>dc3</BiopaxRef> <BiopaxRef>fc8</BiopaxRef> <BiopaxRef>c59</BiopaxRef> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="719.0" Y="251.0" /> <Point X="643.0" Y="252.0" /> <Anchor Position="0.0" Shape="None" GraphId="b3705" /> <Anchor Position="0.99" Shape="None" GraphId="f4bb7" /> <Anchor Position="0.5" Shape="None" GraphId="cae4b" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-8940074" /> </Interaction> <Interaction GraphId="f073a"> <Comment Source="Reactome">The NLRP3 inflammasome is activated by a range of stimuli of microbial, endogenous and exogenous origins including several viruses, bacterial pore forming toxins (e.g. Craven et al. 2009), and various irritants that form crystalline or particulate structures (see Cassel et al. 2009). Multiple studies have shown that phagocytosis of particulate elicitors is necessary for activation (e.g. Hornung et al. 2008) but not for the response to ATP, which is mediated by the P2X7 receptor (Kahlenberg &amp; Dubyak, 2004) and appears to involve the pannexin membrane channel (Pellegrin &amp; Suprenenant 2006), which is also involved in the response to nigericin and maitotoxin (Pellegrin &amp; Suprenenant 2007). Direct binding of elicitors to NLRP3 has not been demonstrated and the exact process of activation is unclear, though speculated to involve changes in conformation that make available the NACHT domain for oligomerization (Inohara &amp; Nunez 2001, 2003).&lt;br&gt;&lt;br&gt;Three overlapping mechanisms are believed to be involved in NLRP3 activation. ATP stimulates the P2X7 ATP-gated ion channel leading to K+ efflux which appears necessary for NLRP3 inflammasome activation (Kahlenberg &amp; Dubyak 2004, Dostert et al. 2008), and is believed to induce formation of pannexin-1 membrane pores. These pores give direct access of NLPR3 agonists to the cytosol. A second mechanism is the endocytosis of crystalline or particulate structures, leading to damaged lysosomes which release their contents (Hornung et al. 2008, Halle et al. 2008). The third element is the generation of reactive oxygen species (ROS) which activate NLRP3, shown to be a critical step for the activation of caspase-1 following ATP stimulation (Cruz et al. 2007). The source of the ROS is unclear.</Comment> <BiopaxRef>f1f</BiopaxRef> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="1031.0" Y="976.0" /> <Point X="949.0" Y="974.0" /> <Anchor Position="0.0" Shape="None" GraphId="a204e" /> <Anchor Position="0.99" Shape="None" GraphId="c7f99" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-1306876" /> </Interaction> <Interaction GraphId="f1060"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="581.0" Y="690.0" GraphRef="e587b" RelX="0.8300000000000409" RelY="-0.009999999999990905" /> <Point X="584.0" Y="690.0" GraphRef="cb971" RelX="-1.0" RelY="0.0" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-877361" /> </Interaction> <Interaction GraphId="f1d63"> <Comment Source="Reactome">At low to intermediate concentrations of extracellular ATP, P2X4 and P2X7 probably function as heterotrimeric, reversible ATP-gated, non-desensitizing cation channels (Markwardt 2007).</Comment> <BiopaxRef>f33</BiopaxRef> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="1296.0" Y="335.0" /> <Point X="1375.0" Y="334.0" /> <Anchor Position="0.0" Shape="None" GraphId="f14b1" /> <Anchor Position="0.99" Shape="None" GraphId="b65f4" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-9665515" /> </Interaction> <Interaction GraphId="f244e"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="682.0" Y="622.0" GraphRef="ac100" RelX="1.0" RelY="0.0" /> <Point X="685.0" Y="622.0" GraphRef="c36ee" RelX="-1.0" RelY="0.0" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-844610" /> </Interaction> <Interaction GraphId="f2d40"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="1785.0" Y="951.0" GraphRef="b623b" RelX="0.984" RelY="0.0" /> <Point X="1792.0" Y="950.0" GraphRef="f248e" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-449058" /> </Interaction> <Interaction GraphId="f3399"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="1055.0" Y="776.0" GraphRef="f6f97" RelX="-0.023255813953488372" RelY="1.0" /> <Point X="1054.0" Y="883.0" GraphRef="cfa8b" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-1250272" /> </Interaction> <Interaction GraphId="f3d9b"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="935.0" Y="765.0" GraphRef="bc302" RelX="0.7599999999999909" RelY="0.0" /> <Point X="1034.0" Y="765.0" GraphRef="f6f97" RelX="-1.0" RelY="0.0" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-1250253" /> </Interaction> <Interaction GraphId="f49e3"> <Comment Source="Reactome">SGT1 and HSP90 bind the NLRP3 (NALP3) LRR domain. Genetic studies in plants suggest a role for SGT1-HSP90 as co-chaperones of plant resistance (R) proteins, serving to maintain them in an inactive but signaling-competent state. R-protein activation is beleived to lead to dissociation of the SGT1-HSP90 complex. SGT1 and HSP90 are highly conserved, while R proteins are structurally related to mammalian NLRs. Human SGT1 and HSP90 were found to bind NLRP3 (Mayor et al. 2007). Knockdown of human SGT1 by small interfering RNA or chemical inhibition of HSP90 by geldanamycin abrogated NLRP3 inflammasome activity in human monocytic cell line THP-1 (Mayor et al. 2007). Similarly, NLRP3 inflammasome activation was abrogated in geldanamycin-treated human retinal pigment epithelial (RPE) cells (Piippo N et al. 2018). These data indicate that SGT1 and HSP90 are involved in regulation of NLRP3 inflammasome signaling (Mayor et al. 2007; Piippo N et al. 2018). </Comment> <BiopaxRef>eef</BiopaxRef> <BiopaxRef>ac8</BiopaxRef> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="893.0" Y="930.0" /> <Point X="964.0" Y="930.0" /> <Anchor Position="0.0" Shape="None" GraphId="b3d38" /> <Anchor Position="0.99" Shape="None" GraphId="ab916" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-873951" /> </Interaction> <Interaction GraphId="f544b"> <Comment Source="Reactome">Two signals are required for NLRP3 inflammasome activation. Signal 1, also known as the priming signal, is mediated by microbial ligands recognised by TLRs or cytokines such as TNF-α which activate the NF-κB pathway, leading to upregulation of pro-IL-1β and NLRP3 protein levels (Bauernfeind et al. 2009, Jo et al. 2016).</Comment> <BiopaxRef>d1f</BiopaxRef> <BiopaxRef>e4c</BiopaxRef> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="457.0" Y="870.0" /> <Point X="900.0" Y="883.0" /> <Anchor Position="0.0" Shape="None" GraphId="b8f43" /> <Anchor Position="0.99" Shape="None" GraphId="f8456" /> <Anchor Position="0.5" Shape="None" GraphId="ad142" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-9603905" /> </Interaction> <Interaction GraphId="f5709"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="467.0" Y="691.0" GraphRef="db5f1" RelX="0.974025974025974" RelY="0.0" /> <Point X="498.0" Y="691.0" GraphRef="a0206" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-877361" /> </Interaction> <Interaction GraphId="f891a"> <Comment Source="Reactome">Interleukin-1β (IL-1β) lacks signal sequences for compartmentation within the Golgi and classical secretory vesicles, so release of the mature form to extracellular compartments requires nonclassical mechanisms of secretion which are poorly understood (Eder C 2009; Piccioli P &amp; Rubartelli A 2013). Several secretory pathways were proposed involving secretory lysosomes, exosomes, microvesicles, and autophagic vesicles, possibly through a mechanism similar to chaperone-mediated autophagy (CMA) (Andrei C et al. 2004; Ward JR et al. 2010; MacKenzie A et al. 2001; Gudipaty L et al. 2003; Qu Y et al. 2007; Iula L et al. 2018: reviewed by Eder C 2009; Piccioli P &amp; Rubartelli A 2013; Claude-Taupin A et al. 2018). Further, the route of IL-1β secretion was found to be dependent on the type and strength of the inflammatory stimuli (Semino C et al. 2018; Sitia R &amp; Rubartelli A 2018). Thus, in primary human monocytes small trauma or low pathogen load (LPS) activated a pathway involving secretory lysosomes that allows slow release of IL-1β, followed by apoptotic cell death that switches off the inflammatory response (Semino C et al. 2018). 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xmlns:bp="http://www.biopax.org/release/biopax-level3.owl#" xmlns:rdf="http://www.w3.org/1999/02/22-rdf-syntax-ns#" rdf:id="aeb"> <bp:ID rdf:datatype="http://www.w3.org/2001/XMLSchema#string">24752514</bp:ID> <bp:DB rdf:datatype="http://www.w3.org/2001/XMLSchema#string">PubMed</bp:DB> <bp:TITLE rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Chronicity of dermal leishmaniasis caused by Leishmania panamensis is associated with parasite-mediated induction of chemokine gene expression.</bp:TITLE> <bp:AUTHORS rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Navas A, Vargas DA, Freudzon M, McMahon-Pratt D, Saravia NG, Gómez MA.</bp:AUTHORS> </bp:PublicationXref> <bp:PublicationXref xmlns:bp="http://www.biopax.org/release/biopax-level3.owl#" xmlns:rdf="http://www.w3.org/1999/02/22-rdf-syntax-ns#" rdf:id="efd"> <bp:ID rdf:datatype="http://www.w3.org/2001/XMLSchema#string">18577586</bp:ID> <bp:DB rdf:datatype="http://www.w3.org/2001/XMLSchema#string">PubMed</bp:DB> <bp:TITLE rdf:datatype="http://www.w3.org/2001/XMLSchema#string">The Nalp3 inflammasome is essential for the development of silicosis.</bp:TITLE> <bp:AUTHORS rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Cassel SL, Eisenbarth SC, Iyer SS, Sadler JJ, Colegio OR, Colegio OR, Tephly LA, Carter AB, Rothman PB, Flavell RA, Sutterwala FS.</bp:AUTHORS> </bp:PublicationXref> <bp:PublicationXref xmlns:bp="http://www.biopax.org/release/biopax-level3.owl#" xmlns:rdf="http://www.w3.org/1999/02/22-rdf-syntax-ns#" rdf:id="f33"> <bp:ID rdf:datatype="http://www.w3.org/2001/XMLSchema#string">11313357</bp:ID> <bp:DB rdf:datatype="http://www.w3.org/2001/XMLSchema#string">PubMed</bp:DB> <bp:TITLE rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Differential assembly of rat purinergic P2X7 receptor in immune cells of the brain and periphery.</bp:TITLE> <bp:AUTHORS rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Kim M, Spelta V, Sim J, North RA, Surprenant A.</bp:AUTHORS> </bp:PublicationXref> <bp:PublicationXref xmlns:bp="http://www.biopax.org/release/biopax-level3.owl#" xmlns:rdf="http://www.w3.org/1999/02/22-rdf-syntax-ns#" rdf:id="dc3"> <bp:ID rdf:datatype="http://www.w3.org/2001/XMLSchema#string">21933152</bp:ID> <bp:DB rdf:datatype="http://www.w3.org/2001/XMLSchema#string">PubMed</bp:DB> <bp:TITLE rdf:datatype="http://www.w3.org/2001/XMLSchema#string">The high-resolution crystal structure of periplasmic Haemophilus influenzae NAD nucleotidase reveals a novel enzymatic function of human CD73 related to NAD metabolism.</bp:TITLE> <bp:AUTHORS rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Garavaglia S, Bruzzone S, Cassani C, Canella L, Allegrone G, Sturla L, Mannino E, Millo E, De Flora A, Rizzi M.</bp:AUTHORS> </bp:PublicationXref> <bp:PublicationXref xmlns:bp="http://www.biopax.org/release/biopax-level3.owl#" xmlns:rdf="http://www.w3.org/1999/02/22-rdf-syntax-ns#" rdf:id="eef"> <bp:ID rdf:datatype="http://www.w3.org/2001/XMLSchema#string">17435760</bp:ID> <bp:DB rdf:datatype="http://www.w3.org/2001/XMLSchema#string">PubMed</bp:DB> <bp:TITLE rdf:datatype="http://www.w3.org/2001/XMLSchema#string">A crucial function of SGT1 and HSP90 in inflammasome activity links mammalian and plant innate immune responses.</bp:TITLE> <bp:AUTHORS rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Mayor A, Martinon F, De Smedt T, Pétrilli V, Tschopp J.</bp:AUTHORS> </bp:PublicationXref> <bp:openControlledVocabulary xmlns:bp="http://www.biopax.org/release/biopax-level3.owl#"> <bp:TERM xmlns:rdf="http://www.w3.org/1999/02/22-rdf-syntax-ns#" rdf:datatype="http://www.w3.org/2001/XMLSchema#string">immune response pathway</bp:TERM> <bp:ID xmlns:rdf="http://www.w3.org/1999/02/22-rdf-syntax-ns#" rdf:datatype="http://www.w3.org/2001/XMLSchema#string">PW:0000023</bp:ID> <bp:Ontology xmlns:rdf="http://www.w3.org/1999/02/22-rdf-syntax-ns#" rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Pathway Ontology</bp:Ontology> </bp:openControlledVocabulary> </Biopax> 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