Structural Analysis of the α2 Integrin I Domain/Procollagenase-1 (Matrix Metalloproteinase-1) Interaction
Open Access
- 1 August 2001
- journal article
- Published by Elsevier BV
- Vol. 276 (31), 29375-29381
- https://doi.org/10.1074/jbc.m102217200
Abstract
Previous studies have established that ligation of keratinocyte alpha(2)beta(1) integrin by type I collagen induces expression of matrix metalloproteinase-1 (MMP-1) and that MMP-1 activity is required for the alpha(2)beta(1) integrin-dependent migration of primary keratinocytes across collagenous matrices. We now present evidence that MMP-1 binds the alpha(2)beta(1) integrin via the I domain of the alpha(2) integrin subunit. Using an enzyme-linked immunosorbent assay with purified human MMP-1 and recombinant alpha(2) integrin I domain, we showed that the alpha(2) integrin I domain specifically bound in a divalent cation-dependent manner to both the pro and active forms of MMP-1, but not to MMP-3 or MMP-13. Although both the I domain and MMP-1 bind divalent cations, MMP-1 bound, in a divalent cation-dependent manner, to alpha(2) integrin I domains containing metal ion-dependent adhesion sites motif mutations that prevent divalent cation binding to the I domain, demonstrating that the metal ion dependence is a function of MMP-1. Using a series of MMP-1-MMP-3 and MMP-1-MMP-13 chimeras, we determined that both the linker domain and the hemopexin-like domain of MMP-1 were required for optimal binding to the I domain. The alpha(2) integrin/MMP-1 interaction described here extends an emerging paradigm in matrix biology involving anchoring of proteinases to the cell surface to regulate their biological activitiesKeywords
This publication has 38 references indexed in Scilit:
- Pro-collagenase-1 (Matrix Metalloproteinase-1) Binds the α2β1 Integrin upon Release from Keratinocytes Migrating on Type I CollagenPublished by Elsevier BV ,2001
- Cell Surface-bound Collagenase-1 and Focal Substrate Degradation Stimulate the Rear Release of Motile Vascular Smooth Muscle CellsJournal of Biological Chemistry, 2000
- Inactivating Mutation of the Mouse Tissue Inhibitor of Metalloproteinases-2(Timp-2) Gene Alters ProMMP-2 ActivationPublished by Elsevier BV ,2000
- A Novel Protease-docking Function of Integrin at InvadopodiaPublished by Elsevier BV ,1999
- Cloning, expression, and type II collagenolytic activity of matrix metalloproteinase-13 from human osteoarthritic cartilage.JCI Insight, 1996
- Increased expression of matrix metalloproteinases and matrix degrading activity in vulnerable regions of human atherosclerotic plaques.JCI Insight, 1994
- Differential in vivo expression of collagenase messenger RNA in synovium and cartilage. Quantitative comparison with stromelysin messenger rna levels in human rheumatoid arthritis and osteoarthritis patients and in two animal models of acute inflammatory arthritisArthritis & Rheumatism, 1993
- Astacins, serralysins, snake venom and matrix metalloproteinases exhibit identical zinc‐binding environments (HEXXHXXGXXH and Met‐turn) and topologies and should be grouped into a common family, the ‘metzincins’FEBS Letters, 1993
- A model for interstitial collagen catabolism by mammalian collagenasesJournal of Theoretical Biology, 1991
- The primary structure of the VLA-2/collagen receptor alpha 2 subunit (platelet GPIa): homology to other integrins and the presence of a possible collagen-binding domain.The Journal of cell biology, 1989