KEGG   PATHWAY: rro05146
Entry
rro05146                    Pathway                                
Name
Amoebiasis - Rhinopithecus roxellana (golden snub-nosed monkey)
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 disease: parasitic
Pathway map
rro05146  Amoebiasis
rro05146

Organism
Rhinopithecus roxellana (golden snub-nosed monkey) [GN:rro]
Gene
104672547  IL1B; interleukin-1 beta [KO:K04519]
104680311  IL1R1; interleukin-1 receptor type 1 isoform X1 [KO:K04386]
104680312  IL1R2; interleukin-1 receptor type 2 isoform X2 [KO:K04387]
104662315  NFKB1; nuclear factor NF-kappa-B p105 subunit isoform X1 [KO:K02580]
104664815  RELA; transcription factor p65 [KO:K04735]
104681213  HSPB1; heat shock protein beta-1 [KO:K04455]
104655778  MUC2; LOW QUALITY PROTEIN: mucin-2 [KO:K10955]
104680270  COL1A1; collagen alpha-1(I) chain isoform X1 [KO:K06236]
104682783  COL1A2; collagen alpha-2(I) chain [KO:K06236]
104679242  COL4A1; collagen alpha-1(IV) chain [KO:K06237]
104658850  COL4A6; collagen alpha-6(IV) chain isoform X1 [KO:K06237]
104671965  COL4A3; collagen alpha-3(IV) chain [KO:K06237]
104671966  COL4A4; collagen alpha-4(IV) chain [KO:K06237]
104679243  COL4A2; collagen alpha-2(IV) chain [KO:K06237]
104665145  COL4A5; collagen alpha-5(IV) chain isoform X1 [KO:K06237]
104669238  FN1; fibronectin isoform X1 [KO:K05717]
104670221  LAMA1; LOW QUALITY PROTEIN: laminin subunit alpha-1 [KO:K05637]
104655298  LAMA2; laminin subunit alpha-2 isoform X1 [KO:K05637]
104678039  laminin subunit alpha-3 isoform X2 [KO:K06240]
104663822  LAMA5; LOW QUALITY PROTEIN: laminin subunit alpha-5 [KO:K06240]
104659760  LAMA4; laminin subunit alpha-4 isoform X1 [KO:K06241]
104677415  LAMB1; laminin subunit beta-1 isoform X1 [KO:K05636]
104667469  LAMB2; laminin subunit beta-2 [KO:K06243]
104664167  LAMB3; laminin subunit beta-3 [KO:K06244]
104672365  LAMB4; laminin subunit beta-4 isoform X1 [KO:K06245]
104666795  LAMC1; laminin subunit gamma-1 [KO:K05635]
104666798  LAMC2; laminin subunit gamma-2 [KO:K06246]
104660568  LAMC3; laminin subunit gamma-3 [KO:K06247]
104666783  caspase-3-like [KO:K02187] [EC:3.4.22.56]
104673791  CASP3; caspase-3 [KO:K02187] [EC:3.4.22.56]
104664696  LOW QUALITY PROTEIN: uncharacterized protein LOC104664696 [KO:K06856]
104674294  LOW QUALITY PROTEIN: uncharacterized protein LOC104674294 [KO:K06856]
104677074  uncharacterized protein LOC104677074 [KO:K06856]
104663314  GNAQ; guanine nucleotide-binding protein G(q) subunit alpha [KO:K04634]
104665456  GNA11; guanine nucleotide-binding protein subunit alpha-11 [KO:K04635]
104663317  GNA14; guanine nucleotide-binding protein subunit alpha-14 [KO:K04636]
104665455  GNA15; guanine nucleotide-binding protein subunit alpha-15 [KO:K04637]
104655777  PLCB4; 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-4 isoform X1 [KO:K05858] [EC:3.1.4.11]
104673127  PLCB3; 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-3 [KO:K05858] [EC:3.1.4.11]
104668296  PLCB1; 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-1 isoform X1 [KO:K05858] [EC:3.1.4.11]
104659669  PLCB2; 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-2 isoform X1 [KO:K05858] [EC:3.1.4.11]
104675428  PRKCA; protein kinase C alpha type isoform X1 [KO:K02677] [EC:2.7.11.13]
104665907  PRKCB; protein kinase C beta type isoform X1 [KO:K19662] [EC:2.7.11.13]
104676027  PRKCG; protein kinase C gamma type isoform X1 [KO:K19663] [EC:2.7.11.13]
104663797  GNAS; guanine nucleotide-binding protein G(s) subunit alpha isoforms XLas isoform X1 [KO:K04632]
104663799  neuroendocrine secretory protein 55 [KO:K04632]
104670245  GNAL; guanine nucleotide-binding protein G(olf) subunit alpha [KO:K04633]
104671165  ADCY1; adenylate cyclase type 1 isoform X1 [KO:K08041] [EC:4.6.1.1]
104662061  PRKACG; cAMP-dependent protein kinase catalytic subunit gamma isoform X1 [KO:K04345] [EC:2.7.11.11]
104677489  PRKACB; cAMP-dependent protein kinase catalytic subunit beta isoform X1 [KO:K04345] [EC:2.7.11.11]
104661051  LOW QUALITY PROTEIN: cAMP-dependent protein kinase catalytic subunit alpha [KO:K04345] [EC:2.7.11.11]
104665706  RAB5A; ras-related protein Rab-5A [KO:K07887]
104673699  RAB5B; ras-related protein Rab-5B [KO:K07888]
104680360  RAB5C; ras-related protein Rab-5C [KO:K07889]
104655224  RAB7A; ras-related protein Rab-7a [KO:K07897]
104661725  RAB7B; ras-related protein Rab-7b [KO:K07898]
104677747  TLR2; toll-like receptor 2 [KO:K10159]
104658520  TLR4; toll-like receptor 4 isoform X2 [KO:K10160]
104681766  CD14; monocyte differentiation antigen CD14 [KO:K04391]
104675233  IL6; interleukin-6 isoform X1 [KO:K05405]
104658884  growth-regulated alpha protein-like [KO:K05505]
104658876  CXCL1; growth-regulated alpha protein [KO:K05505]
104654807  C-X-C motif chemokine 3 isoform X2 [KO:K05505]
104658882  C-X-C motif chemokine 3-like [KO:K05505]
104659848  CSF2; granulocyte-macrophage colony-stimulating factor [KO:K05427]
104658873  CXCL8; LOW QUALITY PROTEIN: interleukin-8 [KO:K10030]
104661913  TNF; tumor necrosis factor isoform X1 [KO:K03156]
104665012  IL12A; interleukin-12 subunit alpha isoform X1 [KO:K05406]
104669104  IL12B; interleukin-12 subunit beta [KO:K05425]
104681020  CD1E; T-cell surface glycoprotein CD1e, membrane-associated isoform X2 [KO:K06448]
104681059  CD1B; T-cell surface glycoprotein CD1b isoform X1 [KO:K06448]
104676420  CD1C; T-cell surface glycoprotein CD1c isoform X2 [KO:K06448]
104676421  T-cell surface glycoprotein CD1a isoform X1 [KO:K06448]
104676422  CD1D; antigen-presenting glycoprotein CD1d isoform X2 [KO:K06448]
104676444  T-cell surface glycoprotein CD1a-like isoform X1 [KO:K06448]
104664085  IFNG; interferon gamma [KO:K04687]
104667744  COL3A1; collagen alpha-1(III) chain [KO:K19720]
104679749  PTK2; focal adhesion kinase 1 isoform X1 [KO:K05725] [EC:2.7.10.2]
104669976  VCL; vinculin isoform X1 [KO:K05700]
104679965  ACTN4; alpha-actinin-4 [KO:K05699]
104659630  ACTN1; LOW QUALITY PROTEIN: alpha-actinin-1 [KO:K05699]
104664958  ARG2; arginase-2, mitochondrial [KO:K01476] [EC:3.5.3.1]
104657737  ARG1; arginase-1 [KO:K01476] [EC:3.5.3.1]
104669357  NOS2; nitric oxide synthase, inducible [KO:K13241] [EC:1.14.13.39]
104659958  ITGB2; integrin beta-2 [KO:K06464]
104661578  ITGAM; integrin alpha-M isoform X1 [KO:K06461]
104662124  PIK3R3; phosphatidylinositol 3-kinase regulatory subunit gamma [KO:K02649]
104675620  PIK3R1; phosphatidylinositol 3-kinase regulatory subunit alpha isoform X1 [KO:K02649]
104680672  PIK3R2; phosphatidylinositol 3-kinase regulatory subunit beta [KO:K02649]
104663050  PIK3CD; phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit delta isoform isoform X1 [KO:K00922] [EC:2.7.1.153]
104665061  PIK3CB; phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit beta isoform isoform X1 [KO:K00922] [EC:2.7.1.153]
104670605  PIK3CA; phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit alpha isoform [KO:K00922] [EC:2.7.1.153]
104662136  PRDX1; peroxiredoxin-1 [KO:K13279] [EC:1.11.1.24]
104661231  SERPINB6; serpin B6 isoform X1 [KO:K13963]
104661233  SERPINB9; serpin B9 [KO:K13963]
104682240  serpin B3-like [KO:K13963]
104682241  serpin B3 [KO:K13963]
104682235  SERPINB10; serpin B10 [KO:K13963]
104682242  SERPINB13; serpin B13 isoform X1 [KO:K13963]
104682234  serpin B6-like isoform X1 [KO:K13963]
104662664  CTSG; cathepsin G [KO:K01319] [EC:3.4.21.20]
104661740  IL10; interleukin-10 [KO:K05443]
104676086  TGFB1; transforming growth factor beta-1 proprotein isoform X2 [KO:K13375]
104662252  TGFB2; transforming growth factor beta-2 proprotein isoform X1 [KO:K13376]
104677599  TGFB3; transforming growth factor beta-3 proprotein isoform X1 [KO:K13377]
104664272  C8A; complement component C8 alpha chain [KO:K03997]
104664293  C8B; complement component C8 beta chain [KO:K03998]
104669647  C8G; complement component C8 gamma chain isoform X1 [KO:K03999]
104665748  C9; complement component C9 [KO:K04000]
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
PMID:11378035
  Authors
Stanley SL
  Title
Pathophysiology of amoebiasis.
  Journal
Trends Parasitol 17:280-5 (2001)
DOI:10.1016/S1471-4922(01)01903-1
Reference
PMID:10756002
  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
PMID:14700586
  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
PMID:15813717
  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
PMID:19207103
  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
PMID:17576362
  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
PMID:12660071
  Authors
Stanley SL Jr
  Title
Amoebiasis.
  Journal
Lancet 361:1025-34 (2003)
DOI:10.1016/S0140-6736(03)12830-9
Reference
PMID:14502002
  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
PMID:12142490
  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
PMID:18725798
  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
PMID:12160867
  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
PMID:17702556
  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
PMID:20303955
  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
PMID:16380324
  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
PMID:10637584
  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
PMID:11352795
  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
PMID:20145703
  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
Related
pathway
rro00330  Arginine and proline metabolism
rro00590  Arachidonic acid metabolism
rro04144  Endocytosis
rro04210  Apoptosis
rro04510  Focal adhesion
rro04610  Complement and coagulation cascades
rro04612  Antigen processing and presentation
rro04620  Toll-like receptor signaling pathway
rro04672  Intestinal immune network for IgA production
rro04810  Regulation of actin cytoskeleton
KO pathway
ko05146   
LinkDB

DBGET integrated database retrieval system