Specific cleavage of human type III collagen by human polymorphonuclear leukocyte elastase

Purified polymorphonuclear leukocyte elastase degraded native human liver type III collagen at 27 degrees C by making a cleavage through the triple helix. The enzyme had no effect on human type I collagen. The reaction was inhibited by phenylmethanesulfonyl fluoride (PhCH2SO2F) but not by EDTA. The...

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Bibliographic Details
Published in:The Journal of biological chemistry 1980-12, Vol.255 (24), p.12006-12010
Main Authors: Mainardi, C L, Hasty, D L, Seyer, J M, Kang, A H
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Amino Acids - analysis
Collagen
Humans
Liver Cirrhosis - metabolism
Microbial Collagenase - metabolism
Neutrophils - enzymology
Pancreatic Elastase - blood
Substrate Specificity
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Summary:Purified polymorphonuclear leukocyte elastase degraded native human liver type III collagen at 27 degrees C by making a cleavage through the triple helix. The enzyme had no effect on human type I collagen. The reaction was inhibited by phenylmethanesulfonyl fluoride (PhCH2SO2F) but not by EDTA. The collagen reaction products were identical with those generated by human rheumatoid synovial collagenase when analyzed by polyacrylamide gel electrophoresis and gel filtration. NH2-trminal sequence analysis indicated that the enzyme cleaved at an isoleucyl-threonyl bond located 4 residues on the carboxyl side of the established cleavage site for animal collagenases. Therefore, it is likely that in pathologic states, type III collagen can be selectively depleted from the matrix by this enzyme.
ISSN:0021-9258
1083-351X
DOI:10.1016/S0021-9258(19)70234-8