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Interaction of peptide substrates of fibroblast collagenase with divalent cations: Ca2+ binding by substrate as a suggested recognition signal for collagenase action.

Abstract：

:To correlate structural data on substrates of human fibroblast collagenase with their interaction with the enzyme, we have studied: Ac-PLG-s-LLG-O-ethyl ester (I), Dnp-PLGLWA(d-Arg)-NH2 (II), AcGPEGLRVG-O-ethyl ester (III) and Succ-GPLGP-O-amidomethylcoumaryl ester (IV). Peptides I and II represent collagenase cleavage sequences in collagen, peptide III is a mimic for the cleavage site in alpha 2-macroglobulin and peptide IV represents a non-substrate model. Kinetic data showed that peptides I, II and III were substrates of the enzyme. In contrast, peptide IV was not acted upon by the enzyme. Circular dichroism data on the peptides showed that the peptides assume ordered structures in water and trifluoroethanol. In the latter solvent, peptides I and III bound Ca2+ and Zn2+ while peptide II bound Ca2+ but not Zn2+. Peptide IV did not bind either cation in this solvent. Together with the kinetic data, the results suggest that the collagenase cleavage segments in collagen and non-collagen substrates of collagenase could interact with Ca2+ and the enzyme to form a ternary complex. This, in turn, would imply a cofactor role for Ca2+ in collagenase action in addition to the solely structural role ascribed so far to this cation.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Upadhye S,Ananthanarayanan VS

doi

10.1006/bbrc.1995.2489

subject

Has Abstract

pub_date

1995-10-13 00:00:00

pages

474-82

issue

2

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(85)72489-8

journal_volume

215

pub_type

杂志文章

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