Preferential binding of collagenase to α2‐macroglobulin in the presence of the tissue inhibitor of metalloproteinases
- 1 December 1986
- journal article
- Published by Wiley in FEBS Letters
- Vol. 209 (1), 9-12
- https://doi.org/10.1016/0014-5793(86)81074-2
Abstract
The binding of collagenase to both α2-niacroglobulin and the tissue inhibitor of metalloproteinases was studied using purified materials. Collagenase bound preferentially to α2-macroglobulin although no transfer of collagenase to α2-macroglobulin occurred if the enzyme was first mixed with the tissue inhibitor of metalloproteinases. The sequences of amino acids in both inhibitors likely to be responsible for the binding of collagenase are discussed and compared to the cleavage site in the collagen molecule.Keywords
This publication has 21 references indexed in Scilit:
- Sequence of human tissue inhibitor of metalloproteinases and its identity to erythroid-potentiating activityNature, 1985
- Human Skin Fibroblast Collagenase: Interaction with Substrate and InhibitorCollagen and Related Research, 1985
- Metalloproteinases and collagenase inhibitors in rheumatoid synovial fluidArthritis & Rheumatism, 1984
- Alpha2-Macroglobulin in Connective Tissue Matrix MetabolismCollagen and Related Research, 1984
- Interaction of β1-Anticollagenase from Human Plasma with Collagenases from Various Tissues and Competition with α2-MacroglobulinEuropean Journal of Biochemistry, 1983
- Primary and secondary cleavage sites in the bait region of α2‐macroglobulinFEBS Letters, 1981
- [54] α2-MacroglobulinMethods in Enzymology, 1981
- A rapid and reproducible assay for collagenase using [1-14C]acetylated collagenAnalytical Biochemistry, 1979
- Small molecular weight β1 serum protein which specifically inhibits human collagenasesNature, 1976