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Research Article Free access | 10.1172/JCI1025

Evidence for a role of collagen synthesis in arterial smooth muscle cell migration.

E F Rocnik, B M Chan, and J G Pickering

John P. Robarts Research Institute, Vascular Biology Group, London Health Sciences Centre, London, Canada N6A 5K8.

Find articles by Rocnik, E. in: PubMed | Google Scholar

John P. Robarts Research Institute, Vascular Biology Group, London Health Sciences Centre, London, Canada N6A 5K8.

Find articles by Chan, B. in: PubMed | Google Scholar

John P. Robarts Research Institute, Vascular Biology Group, London Health Sciences Centre, London, Canada N6A 5K8.

Find articles by Pickering, J. in: PubMed | Google Scholar

Published May 1, 1998 - More info

Published in Volume 101, Issue 9 on May 1, 1998
J Clin Invest. 1998;101(9):1889–1898. https://doi.org/10.1172/JCI1025.
© 1998 The American Society for Clinical Investigation
Published May 1, 1998 - Version history
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Abstract

Migration of smooth muscle cells (SMCs) and collagen synthesis by SMCs are central to the pathophysiology of vascular disease. Both processes can be induced shortly after vascular injury; however, a functional relationship between them has not been established. In this study, we determined if collagen synthesis was required for SMC migration, using ethyl-3,4-dihydroxybenzoate (EDHB), an inhibitor of prolyl-4-hydroxylase, and 3,4-DL-dehydroproline (DHP), a proline analogue, which we demonstrate inhibit collagen elaboration by porcine arterial SMCs. SMCs exposed to EDHB or DHP attached normally to collagen- and vitronectin-coated substrates; however, spreading on collagen but not vitronectin was inhibited. SMC migration speed, quantified by digital time-lapse video microscopy, was significantly and reversibly reduced by EDHB and DHP. Flow cytometry revealed that expression of beta1 integrins, through which SMCs interact with collagen, was unaffected by EDHB or DHP. However, both inhibitors prevented normal clustering of beta1 integrins on the surface of SMCs, consistent with a lack of appropriate matrix ligands for integrin engagement. Moreover, there was impaired recruitment of vinculin into focal adhesion complexes of spreading SMCs and disassembly of the smooth muscle alpha-actin-containing cytoskeleton. These findings suggest that de novo collagen synthesis plays a role in SMC migration and implicates a mechanism whereby newly synthesized collagen may be necessary to maintain the transcellular traction system required for effective locomotion.

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