Cleavage of native type I collagen by human neutrophil elastase

Author:

KAFIENAH Wa'el1,BUTTLE J. David1,BURNETT David2,HOLLANDER P. Anthony1

Affiliation:

1. Department of Human Metabolism and Clinical Biochemistry, and Institute for Bone and Joint Medicine, University of Sheffield Medical School, Beech Hill Road, Sheffield S10 2RX, U.K.

2. Micropathology Ltd, Institute for Research and Development, University of Birmingham Research Park, Vincent Drive, Birmingham B15 2SQ, U.K.

Abstract

The ability of purified human neutrophil elastase (EC 3.4.21.37) to cleave native type I collagen has been investigated. Soluble human, bovine or rat type I collagen was incubated with neutrophil elastase for 16 h at 25 °C before catalysis was stopped with 3,4-dichloroisocoumarin. Analysis by SDS/PAGE of the collagen digests revealed 3/4-length fragments similar in size to those produced by interstitial collagenase. The collagenolytic activity was dose dependent and was not due to a contaminating metalloproteinase or cysteine proteinase, as it was not inhibited by 1,10-phenanthroline, EDTA or L-trans-epoxysuccinyl-leucylamido-(4-guanidino)butane. The identity of the cleavage products was confirmed using a new antibody that recognizes the unwound α2(I)-chain. This detected the 3/4-length fragment of type I collagen following neutrophil elastase cleavage. In addition to cleaving soluble collagen, neutrophil elastase also cleaved reconstituted, radiolabelled type I collagen fibrils, at a rate of 16 μg/min per nmol. These results indicate that neutrophil elastase can cleave native type I collagen in the helix, an activity that might contribute to its roles in connective-tissue pathology.

Publisher

Portland Press Ltd.

Subject

Cell Biology,Molecular Biology,Biochemistry

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