Document Detail

Entamoeba histolytica Cathepsin-Like Enzymes : Interactions with the Host Gut.
MedLine Citation:
PMID:  21660659     Owner:  NLM     Status:  In-Data-Review    
Cysteine proteases of the protozoan parasite Entamoeba histolytica are key virulence factors involved in overcoming host defences. These proteases are cathepsin-like enzymes with a cathepsin-L like structure, but cathepsin-B substrate specificity. In the host intestine, amoeba cysteine proteases cleave colonic mucins and degrade secretory immunoglobulin (Ig) A and IgG rendering them ineffective. They also act on epithelial tight junctions and degrade the extracellular matrix to promote Cell death. They are involved in the destruction of red blood cells and the evasion of neutrophils and macrophages and they activate pro-inflammatory cytokines IL- 1β and IL-18. In short, amoeba cysteine proteases manipulate and destroy host defences to facilitate nutrient acquisition, parasite colonization and/or invasion. Strategies to inhibit the activity of amoeba cysteine proteases could contribute significantly to host protection against E. histolytica.
Vanessa Kissoon-Singh; Leanne Mortimer; Kris Chadee
Related Documents :
386509 - Heparin: an old drug with a new paradigm.
7157229 - Interactions of anticoagulant insoluble modified polystyrene resins with plasmatic prot...
21644529 - N-fused imidazoles as novel anticancer agents that inhibit catalytic activity of topois...
15140589 - A small fraction of dermatan sulfate with significantly increased anticoagulant activit...
8548789 - Conformational analysis of heparin epoxide: molecular mechanics computations.
8615699 - Inhibition of human mast cell chymase by secretory leukocyte proteinase inhibitor: enha...
66229 - Beta-actinin, a regulatory protein of muscle. purification, characterization and function.
23683699 - Estimation of phosphoenolpyruvate carboxylation mediated by phosphoenolpyruvate carboxy...
16720379 - Matrix metalloproteinase dependent and independent collagen degradation.
Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  Advances in experimental medicine and biology     Volume:  712     ISSN:  0065-2598     ISO Abbreviation:  Adv. Exp. Med. Biol.     Publication Date:  2011  
Date Detail:
Created Date:  2011-06-10     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  0121103     Medline TA:  Adv Exp Med Biol     Country:  United States    
Other Details:
Languages:  eng     Pagination:  62-83     Citation Subset:  IM    
Gastrointestinal Research Group, University of Calgary, Calgary, Alberta, Canada.
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

Previous Document:  Cathepsin proteases in Toxoplasma gondii.
Next Document:  Cysteine peptidases of kinetoplastid parasites.