ROS and RNS production in phagocytes (Homo sapiens)

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6272, 7, 8, 2917243, 221, 5, 3010, 2512111, 19, 31149231, 1226, 284, 16cell wallcytosolbacterialhost cellbacterialphagocytic vesicle lumenhost cell cytosolH+NADP+OppB NCF2 Divalent metalstransported byNRAMP1ATP6V1B1 Fe3+NADPHH+ATP6V1C1 OppC H+NitriteH+CAMP(132-170)NOS1,2,3hydroperoxylATP6V1A SLC11A1Zn2+ ATP6V1G3 hemeZn2+ NODivalent metalstransported byNRAMP1ATP6V1B2 GSNOH+ATP6V1E2 CYBA GSHNOS1 Peptide-MethionineO2.-Latent infection ofHomo sapiens withMycobacteriumtuberculosisO2V-ATPaseCO3(2-)ATP6V0A1 NOX2 complexATP6V0D2 LTF ATP6V0D1 O2.-ATP6V0E2 ATP6V1H ATP6V0B NCF1 CAMP(134-170)ATP6V1D OppA CYBB ATP6V0A2 Mn2+ GSHFeHMNOS2 OligopeptideimporterH+ATP6V1F Lactoferrin (loaded)LTFO2Fe3+ L-ArgATP6V1G2 Mn2+ NOS3 FAD Fe2+ hydroperoxylPeroxynitriteATP6V0C CO3(2-) NADP+OppD Peroxynitriteheme NO+ATP6V1C2 NADPHATP6V1E1 TCIRG1 ATP6V0A4 NCF4 NOATP6V1G1 Fe2+ NOPeptide-Methionine(S)-SulfoxideATP6V0E1 L-Cit13, 15, 18, 20


Description

Alveolar macrophages normally develop their phagosome along the endolysosomal pathway. However, after having internalized Mtb, this development is arrested at an early stage and only includes acidification, nitric oxide and superoxide production, as well as the use of a few other proteins that can be gained from other endosomes which still can interact with the phagosome (Flannagan et al. 2009). View original pathway at:Reactome.

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Bibliography

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History

View all...
CompareRevisionActionTimeUserComment
114846view16:35, 25 January 2021ReactomeTeamReactome version 75
113292view11:36, 2 November 2020ReactomeTeamReactome version 74
112852view13:10, 12 October 2020DeSlOntology Term : 'immune response pathway' added !
112851view13:10, 12 October 2020DeSlOntology Term : 'phagocyte' added !
112850view13:09, 12 October 2020DeSlOntology Term : 'disease by infectious agent' added !
112504view15:46, 9 October 2020ReactomeTeamReactome version 73
101416view11:30, 1 November 2018ReactomeTeamreactome version 66
100954view21:06, 31 October 2018ReactomeTeamreactome version 65
100491view19:40, 31 October 2018ReactomeTeamreactome version 64
100036view16:24, 31 October 2018ReactomeTeamreactome version 63
99589view14:58, 31 October 2018ReactomeTeamreactome version 62 (2nd attempt)
99209view12:43, 31 October 2018ReactomeTeamreactome version 62
94500view09:06, 14 September 2017Mkutmonreactome version 61
83441view12:25, 18 November 2015ReactomeTeamNew pathway

External references

DataNodes

View all...
NameTypeDatabase referenceComment
ATP6V0A1 ProteinQ93050 (Uniprot-TrEMBL)
ATP6V0A2 ProteinQ9Y487 (Uniprot-TrEMBL)
ATP6V0A4 ProteinQ9HBG4 (Uniprot-TrEMBL)
ATP6V0B ProteinQ99437 (Uniprot-TrEMBL)
ATP6V0C ProteinP27449 (Uniprot-TrEMBL)
ATP6V0D1 ProteinP61421 (Uniprot-TrEMBL)
ATP6V0D2 ProteinQ8N8Y2 (Uniprot-TrEMBL)
ATP6V0E1 ProteinO15342 (Uniprot-TrEMBL)
ATP6V0E2 ProteinQ8NHE4 (Uniprot-TrEMBL)
ATP6V1A ProteinP38606 (Uniprot-TrEMBL)
ATP6V1B1 ProteinP15313 (Uniprot-TrEMBL)
ATP6V1B2 ProteinP21281 (Uniprot-TrEMBL)
ATP6V1C1 ProteinP21283 (Uniprot-TrEMBL)
ATP6V1C2 ProteinQ8NEY4 (Uniprot-TrEMBL)
ATP6V1D ProteinQ9Y5K8 (Uniprot-TrEMBL)
ATP6V1E1 ProteinP36543 (Uniprot-TrEMBL)
ATP6V1E2 ProteinQ96A05 (Uniprot-TrEMBL)
ATP6V1F ProteinQ16864 (Uniprot-TrEMBL)
ATP6V1G1 ProteinO75348 (Uniprot-TrEMBL)
ATP6V1G2 ProteinO95670 (Uniprot-TrEMBL)
ATP6V1G3 ProteinQ96LB4 (Uniprot-TrEMBL)
ATP6V1H ProteinQ9UI12 (Uniprot-TrEMBL)
CAMP(132-170)ProteinP49913 (Uniprot-TrEMBL)
CAMP(134-170)ProteinP49913 (Uniprot-TrEMBL)
CO3(2-) MetaboliteCHEBI:41609 (ChEBI)
CO3(2-)MetaboliteCHEBI:41609 (ChEBI)
CYBA ProteinP13498 (Uniprot-TrEMBL)
CYBB ProteinP04839 (Uniprot-TrEMBL)
Divalent metals

transported by

NRAMP1		ComplexR-HSA-R-ALL-445829 (Reactome)
Divalent metals

transported by

NRAMP1		ComplexR-HSA-R-ALL-445832 (Reactome)
FAD MetaboliteCHEBI:16238 (ChEBI)
Fe2+ MetaboliteCHEBI:18248 (ChEBI)
Fe3+ MetaboliteCHEBI:29034 (ChEBI)
Fe3+MetaboliteCHEBI:29034 (ChEBI)
FeHMMetaboliteCHEBI:36144 (ChEBI)
GSHMetaboliteCHEBI:16856 (ChEBI)
GSNOMetaboliteCHEBI:50091 (ChEBI)
H+MetaboliteCHEBI:15378 (ChEBI)
L-ArgMetaboliteCHEBI:16467 (ChEBI)
L-CitMetaboliteCHEBI:16349 (ChEBI)
LTF ProteinP02788 (Uniprot-TrEMBL)
LTFProteinP02788 (Uniprot-TrEMBL)
Lactoferrin (loaded)ComplexR-HSA-1222432 (Reactome)
Latent infection of

Homo sapiens with Mycobacterium

tuberculosis		PathwayR-HSA-1222352 (Reactome) Infection by Mycobacterium tuberculosis (Mtb) is soon countered by the host's immune system, the organism is however almost never eradicated; ten per cent of infections will develop into "open tuberculosis", while the other ninety per cent become "latent", a state that can persist for decades until loss of immune control. A third of the world's population is estimated to harbour latent tuberculosis. Latent infection involves the bacterium being internalized by macrophages where it stops and counters the innate immune answer (Russell 2011, Russell et al. 2010). When a status-quo is reached, Mtb enters a non-replicating persistent state (Barry et al. 2009, Boshoff & Barry 2005).
Mn2+ MetaboliteCHEBI:29035 (ChEBI)
NADP+MetaboliteCHEBI:18009 (ChEBI)
NADPHMetaboliteCHEBI:16474 (ChEBI)
NCF1 ProteinP14598 (Uniprot-TrEMBL)
NCF2 ProteinP19878 (Uniprot-TrEMBL)
NCF4 ProteinQ15080 (Uniprot-TrEMBL)
NO+MetaboliteCHEBI:29120 (ChEBI)
NOMetaboliteCHEBI:16480 (ChEBI)
NOS1 ProteinP29475 (Uniprot-TrEMBL)
NOS1,2,3ComplexR-HSA-419294 (Reactome)
NOS2 ProteinP35228 (Uniprot-TrEMBL)
NOS3 ProteinP29474 (Uniprot-TrEMBL)
NOX2 complexComplexR-HSA-1222368 (Reactome)
NitriteMetaboliteCHEBI:16301 (ChEBI)
O2.-MetaboliteCHEBI:18421 (ChEBI)
O2MetaboliteCHEBI:15379 (ChEBI)
Oligopeptide importerComplexR-HSA-R-MTU-1500757 (Reactome)
OppA ProteinP9WGU5 (Uniprot-TrEMBL)
OppB ProteinP9WQJ5 (Uniprot-TrEMBL)
OppC ProteinP9WFZ9 (Uniprot-TrEMBL)
OppD ProteinP9WFZ7 (Uniprot-TrEMBL)
Peptide-Methionine (S)-SulfoxideR-NUL-1222452 (Reactome)
Peptide-MethionineR-NUL-1222500 (Reactome)
PeroxynitriteMetaboliteCHEBI:25941 (ChEBI)
SLC11A1ProteinP49279 (Uniprot-TrEMBL)
TCIRG1 ProteinQ13488 (Uniprot-TrEMBL)
V-ATPaseComplexR-HSA-1222549 (Reactome)
Zn2+ MetaboliteCHEBI:29105 (ChEBI)
heme MetaboliteCHEBI:17627 (ChEBI)
hemeMetaboliteCHEBI:17627 (ChEBI)
hydroperoxylMetaboliteCHEBI:25935 (ChEBI)

Annotated Interactions

View all...
SourceTargetTypeDatabase referenceComment
CAMP(132-170)ArrowR-HSA-1222685 (Reactome)
CAMP(134-170)R-HSA-1222685 (Reactome)
CO3(2-)R-HSA-1222491 (Reactome)
Divalent metals

transported by

NRAMP1		ArrowR-HSA-435171 (Reactome)
Divalent metals

transported by

NRAMP1		R-HSA-435171 (Reactome)
Fe3+R-HSA-1222491 (Reactome)
FeHMR-HSA-1222512 (Reactome)
GSHArrowR-HSA-1500817 (Reactome)
GSHR-HSA-1222384 (Reactome)
GSHR-HSA-1500817 (Reactome)
GSNOArrowR-HSA-1222384 (Reactome)
H+ArrowR-HSA-1222376 (Reactome)
H+ArrowR-HSA-1222384 (Reactome)
H+ArrowR-HSA-1222411 (Reactome)
H+ArrowR-HSA-1222516 (Reactome)
H+ArrowR-HSA-435171 (Reactome)
H+R-HSA-1222353 (Reactome)
H+R-HSA-1222411 (Reactome)
H+R-HSA-1222516 (Reactome)
H+R-HSA-435171 (Reactome)
L-ArgR-HSA-418436 (Reactome)
L-CitArrowR-HSA-418436 (Reactome)
LTFR-HSA-1222491 (Reactome)
Lactoferrin (loaded)ArrowR-HSA-1222491 (Reactome)
NADP+ArrowR-HSA-1222376 (Reactome)
NADP+ArrowR-HSA-418436 (Reactome)
NADPHR-HSA-1222376 (Reactome)
NADPHR-HSA-418436 (Reactome)
NO+ArrowR-HSA-1222512 (Reactome)
NO+R-HSA-1222384 (Reactome)
NOArrowR-HSA-1222662 (Reactome)
NOArrowR-HSA-1222686 (Reactome)
NOArrowR-HSA-418436 (Reactome)
NOR-HSA-1222407 (Reactome)
NOR-HSA-1222512 (Reactome)
NOR-HSA-1222662 (Reactome)
NOR-HSA-1222686 (Reactome)
NOS1,2,3mim-catalysisR-HSA-418436 (Reactome)
NOX2 complexmim-catalysisR-HSA-1222376 (Reactome)
NitriteArrowR-HSA-1222411 (Reactome)
O2.-ArrowR-HSA-1222376 (Reactome)
O2.-R-HSA-1222353 (Reactome)
O2.-R-HSA-1222407 (Reactome)
O2R-HSA-1222376 (Reactome)
O2R-HSA-418436 (Reactome)
Oligopeptide importermim-catalysisR-HSA-1500817 (Reactome)
Peptide-Methionine (S)-SulfoxideArrowR-HSA-1222411 (Reactome)
Peptide-MethionineR-HSA-1222411 (Reactome)
PeroxynitriteArrowR-HSA-1222407 (Reactome)
PeroxynitriteArrowR-HSA-1470073 (Reactome)
PeroxynitriteR-HSA-1222411 (Reactome)
PeroxynitriteR-HSA-1470073 (Reactome)
R-HSA-1222342 (Reactome) Superoxide can enter the bacterium when acidic conditions apply. Together with a proton it forms the hydroperoxyl radical (Nathan & Shiloh 2000, Zahrt & Deretic 2002, Warner & Mizrahi 2006, Spagnolo et al, 2004).
R-HSA-1222353 (Reactome) Superoxide gets protonated (Korshunov & Imlay 2002).
R-HSA-1222376 (Reactome) Macrophage NOX2 is a membrane complex that generates superoxide anions by reduction of oxygen with NADPH (Babior 1999, Dinauer et al. 1991).
R-HSA-1222384 (Reactome) Glutathione (GSH) scavenges nitrosyl, yielding S-nitrosoglutathione (GSNO). Both GSH and GSNO are effective against Mtb (Venketaraman et al. 2005).
R-HSA-1222407 (Reactome) Nitric oxide and superoxide rapidly combine to form peroxynitrite (Pryor & Squadrito 1995).
R-HSA-1222411 (Reactome) Peroxynitrite oxidizes methionine residues (Pryor et al. 1994).
R-HSA-1222491 (Reactome) Lactoferrin is secreted from many tissues to collect stray iron ions that can catalyze unwanted reactions, and to starve microorganisms of this important metal. One molecule of lactoferrin can load two ferric (Fe(3+)) ions together with two carbonate (CO3(2-)) anions (Haridas et al. 1995).
R-HSA-1222512 (Reactome) Production of nitrosyl ion from nitric oxide is much faster when catalyzed by metal ions than via NO2 or N2O3. An alternative mechanism is by reaction with superoxide which is less probable in macrophages because they downregulate pathways leading to superoxide when NO is produced (Kharitonov et al. 1995, Clancy et al. 1994).
R-HSA-1222516 (Reactome) The function of V-type proton pumping ATPases is basically the same as that of F-type ATPases, except that V-ATPases cannot synthesize ATP from the proton motive force, the reverse reaction of pumping. When pumping, ATP hydrolysis drives a 120 degree rotation of the rotor which leads to movement of three protons into the phagosome (Adachi et al. 2007).
R-HSA-1222662 (Reactome) NO enters the bacterium (Clancy et al. 1994).
R-HSA-1222685 (Reactome) In macrophages, LL-37 expression is stimulated by contact with Mtb and it localizes to the cell wall (Rivas-Santiago et al. 2008).
R-HSA-1222686 (Reactome) Nitric oxide diffuses into the phagosome (Clancy et al. 1994). Although NO has been shown to be critical for control of Mtb infection in mice, it's role in human infection is less clear. Instead, the generation of antimicrobial defence molecules including cathelicidin in a vitamin D-dependent pathway is much better established (Fabri et al. 2011, Martineau et al. 2011).
R-HSA-1470073 (Reactome) Peroxynitrite can rapidly permeate biological membranes (Marla et al. 1997, Venugopal et al. 2011).
R-HSA-1500817 (Reactome) Glutathione is taken up by the bacterium by an ABC transporter called the oligopeptide importer. OppA determines substrate specificity (Dasgupta et al. 2010).
R-HSA-418436 (Reactome) Nitric oxide synthase (NOS) produces NO from L-arginine. There are three isoforms of NOS, endothelial, neuronal and inducible (eNOS, nNOS, and iNOS). eNOS and nNOS are constitutively expressed while iNOS is induced by immunostimulatory signals. The constitutive isoforms are regulated in vivo by the binding of calcium and calmodulin. NO produced by NOS acts as a signalling molecule by diffusing across cell membranes to activate soluble guanylate cyclase (sGC).
R-HSA-435171 (Reactome) Natural resistance-associated macrophage proteins (NRAMPs) regulates macrophage activation for antimicrobial activity against intracellular pathogens. They do this by mediating metal ion transport across macrophage membranes and the subsequent use of these ions in the control of free radical formation.
The human gene SLC11A1 encodes NRAMP1 (Kishi F, 2004; Kishi F and Nobumoto M, 1995) which can utilize the protonmotive force to mediate divalent iron (Fe2+), zinc (Zn2+) and manganese (Mn2+) influx to or efflux from phagosomes.
SLC11A1mim-catalysisR-HSA-435171 (Reactome)
V-ATPasemim-catalysisR-HSA-1222516 (Reactome)
hemeArrowR-HSA-1222512 (Reactome)
hydroperoxylArrowR-HSA-1222342 (Reactome)
hydroperoxylArrowR-HSA-1222353 (Reactome)
hydroperoxylR-HSA-1222342 (Reactome)
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