Document Detail

Matrix metalloproteinase dependent and independent collagen degradation.
MedLine Citation:
PMID:  16720379     Owner:  NLM     Status:  MEDLINE    
Cleavage of the fibrillar collagens occurs during physiological conditions, as well as pathological conditions. The resistance of the fibrillar collagens to degradation is due to their rigid and compact structures. There are only a limited number of proteinases that have the capability to initiate the cleavage of the fibrillar collagens. These include some of the matrix metalloproteinases (MMPs) and cathepsins, as well as a few serine proteinases. The MMPs have long been implicated in the collagen degradation and remodeling that occurs at physiological pHs. The cathepsins, on the other hand, have been implicated in the collagen cleavage that occurs at acidic pHs, particularly the collagen degradation that is mediated by osteoclasts. In addition to the MMPs, a few serine proteinases have been implicated in the collagen degradation that occurs at neutral pH. The characteristics that contribute to the resistance of the fibrillar collagens to cleavage are discussed along with the MMPs, cathepsins, and serine proteinases that can cleave these collagens.
Fengyu Song; Kessiri Wisithphrom; Jing Zhou; L Jack Windsor
Related Documents :
19491049 - Molecular interactions of cholinesterases inhibitors using in silico methods: current s...
12054629 - Adamts1 cleaves aggrecan at multiple sites and is differentially inhibited by metallopr...
16026329 - Inhibition of enzyme activity of and cell-mediated substrate cleavage by membrane type ...
20417629 - Interactions of pyridinium oximes with acetylcholinesterase.
8107689 - Myocardial matrix metalloproteinase(s): localization and activation.
17943549 - Activity of matrix metalloproteinase-2 and -9 and contents of their tissue inhibitors i...
16143309 - Unique binding of a non-natural l,l,l-substrate by isopenicillin n synthase.
16080169 - Printing biomacromolecules on a bovine serum albumin precursor layer.
1655979 - Interactions between the argininyl moieties of neurotensin and the catechol protons of ...
Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural; Review     Date:  2006-09-01
Journal Detail:
Title:  Frontiers in bioscience : a journal and virtual library     Volume:  11     ISSN:  1093-4715     ISO Abbreviation:  Front. Biosci.     Publication Date:  2006  
Date Detail:
Created Date:  2006-05-24     Completed Date:  2006-06-27     Revised Date:  2007-11-14    
Medline Journal Info:
Nlm Unique ID:  9709506     Medline TA:  Front Biosci     Country:  United States    
Other Details:
Languages:  eng     Pagination:  3100-20     Citation Subset:  IM    
Department of Oral Biology, Indiana University School of Dentistry, Indianapolis, Indiana 46202, USA.
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Cathepsins / biosynthesis,  metabolism*
Extracellular Matrix / metabolism
Fibrillar Collagens / chemistry,  metabolism*
Matrix Metalloproteinases / metabolism*
Protein Structure, Secondary
Serine Endopeptidases / metabolism*
Substrate Specificity
Grant Support
Reg. No./Substance:
0/Fibrillar Collagens; EC 3.4.-/Cathepsins; EC 3.4.21.-/Serine Endopeptidases; EC 3.4.24.-/Matrix Metalloproteinases

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

Previous Document:  Detection of predefecatory rectosigmoid wave activity for prevention of fecal soiling in infants.
Next Document:  MMP-9 expression is associated with leukocytic but not endothelial markers in brain arteriovenous ma...