KEGG   PATHWAY: hsa05146Help
Entry
hsa05146                    Pathway                                

Name
Amoebiasis - Homo sapiens (human)
Description
Entamoeba histolytica, an extracellular protozoan parasite is a human pathogen that invades the intestinal epithelium. Infection occurs on ingestion of contaminated water and food. The pathogenesis of amoebiasis begins with parasite attachment and disruption of the intestinal mucus layer, followed by apoptosis of host epithelial cells. Intestinal tissue destruction causes severe dysentery and ulcerations in amoebic colitis. Several amoebic proteins such as lectins, cysteine proteineases, and amoebapores are associated with the invasion process. The parasite can cause extraintestinal infection like amoebic liver abscess by evading immune response.
Class
Human Diseases; Infectious diseases: Parasitic
BRITE hierarchy
Pathway map
hsa05146  Amoebiasis
hsa05146

Ortholog table
Disease
H00360  Amoebiasis
Organism
Homo sapiens (human) [GN:hsa]
Gene
3553  IL1B; interleukin 1 beta [KO:K04519]
3554  IL1R1; interleukin 1 receptor type 1 [KO:K04386]
7850  IL1R2; interleukin 1 receptor type 2 [KO:K04387]
4790  NFKB1; nuclear factor kappa B subunit 1 [KO:K02580]
5970  RELA; RELA proto-oncogene, NF-kB subunit [KO:K04735]
3315  HSPB1; heat shock protein family B (small) member 1 [KO:K04455]
4583  MUC2; mucin 2, oligomeric mucus/gel-forming [KO:K10955]
1277  COL1A1; collagen type I alpha 1 chain [KO:K06236]
1278  COL1A2; collagen type I alpha 2 chain [KO:K06236]
1284  COL4A2; collagen type IV alpha 2 chain [KO:K06237]
1286  COL4A4; collagen type IV alpha 4 chain [KO:K06237]
1288  COL4A6; collagen type IV alpha 6 chain [KO:K06237]
1282  COL4A1; collagen type IV alpha 1 chain [KO:K06237]
1287  COL4A5; collagen type IV alpha 5 chain [KO:K06237]
1285  COL4A3; collagen type IV alpha 3 chain [KO:K06237]
2335  FN1; fibronectin 1 [KO:K05717]
284217  LAMA1; laminin subunit alpha 1 [KO:K05637]
3908  LAMA2; laminin subunit alpha 2 [KO:K05637]
3909  LAMA3; laminin subunit alpha 3 [KO:K06240]
3911  LAMA5; laminin subunit alpha 5 [KO:K06240]
3910  LAMA4; laminin subunit alpha 4 [KO:K06241]
3912  LAMB1; laminin subunit beta 1 [KO:K05636]
3913  LAMB2; laminin subunit beta 2 [KO:K06243]
3914  LAMB3; laminin subunit beta 3 [KO:K06244]
22798  LAMB4; laminin subunit beta 4 [KO:K06245]
3915  LAMC1; laminin subunit gamma 1 [KO:K05635]
3918  LAMC2; laminin subunit gamma 2 [KO:K06246]
10319  LAMC3; laminin subunit gamma 3 [KO:K06247]
836  CASP3; caspase 3 [KO:K02187] [EC:3.4.22.56]
102723407  IGH; immunoglobulin heavy variable 4-38-2-like [KO:K06856]
2776  GNAQ; G protein subunit alpha q [KO:K04634]
2767  GNA11; G protein subunit alpha 11 [KO:K04635]
9630  GNA14; G protein subunit alpha 14 [KO:K04636]
2769  GNA15; G protein subunit alpha 15 [KO:K04637]
23236  PLCB1; phospholipase C beta 1 [KO:K05858] [EC:3.1.4.11]
5330  PLCB2; phospholipase C beta 2 [KO:K05858] [EC:3.1.4.11]
5331  PLCB3; phospholipase C beta 3 [KO:K05858] [EC:3.1.4.11]
5332  PLCB4; phospholipase C beta 4 [KO:K05858] [EC:3.1.4.11]
5578  PRKCA; protein kinase C alpha [KO:K02677] [EC:2.7.11.13]
5579  PRKCB; protein kinase C beta [KO:K19662] [EC:2.7.11.13]
5582  PRKCG; protein kinase C gamma [KO:K19663] [EC:2.7.11.13]
2778  GNAS; GNAS complex locus [KO:K04632]
2774  GNAL; G protein subunit alpha L [KO:K04633]
107  ADCY1; adenylate cyclase 1 [KO:K08041] [EC:4.6.1.1]
5566  PRKACA; protein kinase cAMP-activated catalytic subunit alpha [KO:K04345] [EC:2.7.11.11]
5567  PRKACB; protein kinase cAMP-activated catalytic subunit beta [KO:K04345] [EC:2.7.11.11]
5568  PRKACG; protein kinase cAMP-activated catalytic subunit gamma [KO:K04345] [EC:2.7.11.11]
5868  RAB5A; RAB5A, member RAS oncogene family [KO:K07887]
5869  RAB5B; RAB5B, member RAS oncogene family [KO:K07888]
5878  RAB5C; RAB5C, member RAS oncogene family [KO:K07889]
7879  RAB7A; RAB7A, member RAS oncogene family [KO:K07897]
338382  RAB7B; RAB7B, member RAS oncogene family [KO:K07898]
7097  TLR2; toll like receptor 2 [KO:K10159]
7099  TLR4; toll like receptor 4 [KO:K10160]
929  CD14; CD14 molecule [KO:K04391]
3569  IL6; interleukin 6 [KO:K05405]
1437  CSF2; colony stimulating factor 2 [KO:K05427]
3576  CXCL8; C-X-C motif chemokine ligand 8 [KO:K10030]
7124  TNF; tumor necrosis factor [KO:K03156]
3592  IL12A; interleukin 12A [KO:K05406]
3593  IL12B; interleukin 12B [KO:K05425]
3458  IFNG; interferon gamma [KO:K04687]
1281  COL3A1; collagen type III alpha 1 chain [KO:K19720]
5747  PTK2; protein tyrosine kinase 2 [KO:K05725] [EC:2.7.10.2]
7414  VCL; vinculin [KO:K05700]
87  ACTN1; actinin alpha 1 [KO:K05699]
81  ACTN4; actinin alpha 4 [KO:K05699]
384  ARG2; arginase 2 [KO:K01476] [EC:3.5.3.1]
383  ARG1; arginase 1 [KO:K01476] [EC:3.5.3.1]
4843  NOS2; nitric oxide synthase 2 [KO:K13241] [EC:1.14.13.39]
3689  ITGB2; integrin subunit beta 2 [KO:K06464]
3684  ITGAM; integrin subunit alpha M [KO:K06461]
5295  PIK3R1; phosphoinositide-3-kinase regulatory subunit 1 [KO:K02649]
5296  PIK3R2; phosphoinositide-3-kinase regulatory subunit 2 [KO:K02649]
8503  PIK3R3; phosphoinositide-3-kinase regulatory subunit 3 [KO:K02649]
5290  PIK3CA; phosphatidylinositol-4,5-bisphosphate 3-kinase catalytic subunit alpha [KO:K00922] [EC:2.7.1.153]
5293  PIK3CD; phosphatidylinositol-4,5-bisphosphate 3-kinase catalytic subunit delta [KO:K00922] [EC:2.7.1.153]
5291  PIK3CB; phosphatidylinositol-4,5-bisphosphate 3-kinase catalytic subunit beta [KO:K00922] [EC:2.7.1.153]
1992  SERPINB1; serpin family B member 1 [KO:K13963]
6317  SERPINB3; serpin family B member 3 [KO:K13963]
6318  SERPINB4; serpin family B member 4 [KO:K13963]
5269  SERPINB6; serpin family B member 6 [KO:K13963]
5272  SERPINB9; serpin family B member 9 [KO:K13963]
5273  SERPINB10; serpin family B member 10 [KO:K13963]
5275  SERPINB13; serpin family B member 13 [KO:K13963]
1511  CTSG; cathepsin G [KO:K01319] [EC:3.4.21.20]
3586  IL10; interleukin 10 [KO:K05443]
7040  TGFB1; transforming growth factor beta 1 [KO:K13375]
7042  TGFB2; transforming growth factor beta 2 [KO:K13376]
7043  TGFB3; transforming growth factor beta 3 [KO:K13377]
731  C8A; complement C8 alpha chain [KO:K03997]
732  C8B; complement C8 beta chain [KO:K03998]
733  C8G; complement C8 gamma chain [KO:K03999]
735  C9; complement C9 [KO:K04000]
2919  CXCL1; C-X-C motif chemokine ligand 1 [KO:K05505]
912  CD1D; CD1d molecule [KO:K06448]
Compound
C00027  Hydrogen peroxide
C00062  L-Arginine
C00076  Calcium cation
C00165  Diacylglycerol
C00219  Arachidonate
C00533  Nitric oxide
C00575  3',5'-Cyclic AMP
C00584  Prostaglandin E2
C01074  N-Acetylgalactosamine
C01245  D-myo-Inositol 1,4,5-trisphosphate
C01498  Gelatine
C02737  Phosphatidylserine
C18287  Monocyte locomotion inhibitory factor
Reference
  Authors
Stanley SL
  Title
Pathophysiology of amoebiasis.
  Journal
Trends Parasitol 17:280-5 (2001)
DOI:10.1016/S1471-4922(01)01903-1
Reference
  Authors
Espinosa-Cantellano M, Martinez-Palomo A
  Title
Pathogenesis of intestinal amebiasis: from molecules to disease.
  Journal
Clin Microbiol Rev 13:318-31 (2000)
DOI:10.1128/CMR.13.2.318-331.2000
Reference
PMID:9832261
  Authors
Huston CD, Petri WA Jr
  Title
Host-pathogen interaction in amebiasis and progress in vaccine development.
  Journal
Eur J Clin Microbiol Infect Dis 17:601-14 (1998)
DOI:10.1007/BF01708342
Reference
  Authors
Huston CD
  Title
Parasite and host contributions to the pathogenesis of amebic colitis.
  Journal
Trends Parasitol 20:23-6 (2004)
DOI:10.1016/j.pt.2003.10.013
Reference
  Authors
Campos-Rodriguezp R, Jarillo-Luna A
  Title
The pathogenicity of Entamoeba histolytica is related to the capacity of evading innate immunity.
  Journal
Parasite Immunol 27:1-8 (2005)
DOI:10.1111/j.1365-3024.2005.00743.x
Reference
  Authors
Lejeune M, Rybicka JM, Chadee K
  Title
Recent discoveries in the pathogenesis and immune response toward Entamoeba histolytica.
  Journal
Future Microbiol 4:105-18 (2009)
DOI:10.2217/17460913.4.1.105
Reference
  Authors
Carrero JC, Cervantes-Rebolledo C, Aguilar-Diaz H, Diaz-Gallardo MY, Laclette JP, Morales-Montor J
  Title
The role of the secretory immune response in the infection by Entamoeba histolytica.
  Journal
Parasite Immunol 29:331-8 (2007)
DOI:10.1111/j.1365-3024.2007.00955.x
Reference
  Authors
Stanley SL Jr
  Title
Amoebiasis.
  Journal
Lancet 361:1025-34 (2003)
DOI:10.1016/S0140-6736(03)12830-9
Reference
  Authors
Stauffer W, Ravdin JI
  Title
Entamoeba histolytica: an update.
  Journal
Curr Opin Infect Dis 16:479-85 (2003)
DOI:10.1097/01.qco.0000092821.42392.ca
Reference
  Authors
Petri WA Jr, Haque R, Mann BJ
  Title
The bittersweet interface of parasite and host: lectin-carbohydrate interactions during human invasion by the parasite Entamoeba histolytica.
  Journal
Annu Rev Microbiol 56:39-64 (2002)
DOI:10.1146/annurev.micro.56.012302.160959
Reference
  Authors
Baxt LA, Singh U
  Title
New insights into Entamoeba histolytica pathogenesis.
  Journal
Curr Opin Infect Dis 21:489-94 (2008)
DOI:10.1097/QCO.0b013e32830ce75f
Reference
  Authors
Petri WA Jr
  Title
Pathogenesis of amebiasis.
  Journal
Curr Opin Microbiol 5:443-7 (2002)
DOI:10.1016/S1369-5274(02)00335-1
Reference
  Authors
Guo X, Houpt E, Petri WA Jr
  Title
Crosstalk at the initial encounter: interplay between host defense and ameba survival strategies.
  Journal
Curr Opin Immunol 19:376-84 (2007)
DOI:10.1016/j.coi.2007.07.005
Reference
  Authors
Mortimer L, Chadee K
  Title
The immunopathogenesis of Entamoeba histolytica.
  Journal
Exp Parasitol 126:366-80 (2010)
DOI:10.1016/j.exppara.2010.03.005
Reference
  Authors
Meza I, Talamas-Rohana P, Vargas MA
  Title
The cytoskeleton of Entamoeba histolytica: structure, function, and regulation by signaling pathways.
  Journal
Arch Med Res 37:234-43 (2006)
DOI:10.1016/j.arcmed.2005.09.008
Reference
  Authors
Meza I
  Title
Extracellular matrix-induced signaling in Entamoeba histolytica: its role in invasiveness.
  Journal
Parasitol Today 16:23-8 (2000)
DOI:10.1016/S0169-4758(99)01586-0
Reference
  Authors
Stanley SL Jr, Reed SL
  Title
Microbes and microbial toxins: paradigms for microbial-mucosal interactions. VI. Entamoeba histolytica: parasite-host interactions.
  Journal
Am J Physiol Gastrointest Liver Physiol 280:G1049-54 (2001)
DOI:10.1152/ajpgi.2001.280.6.G1049
Reference
  Authors
Wong-Baeza I, Alcantara-Hernandez M, Mancilla-Herrera I, Ramirez-Saldivar I, Arriaga-Pizano L, Ferat-Osorio E, Lopez-Macias C, Isibasi A
  Title
The role of lipopeptidophosphoglycan in the immune response to Entamoeba histolytica.
  Journal
J Biomed Biotechnol 2010:254521 (2010)
DOI:10.1155/2010/254521
KO pathway
ko05146   

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