Chapter category: Adhesion Molecules

Structure and Function of a11b1

This chapter appears in the following book:

I Domains in Integrins

Edited by: Donald Gullberg
ISBN: 0-306-47836-6
» Get more information about this book at landesbioscience.com «

Chapter authors:
Donald Gullberg, Svetlana N. Popova and Carl-Fredrik Tiger

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The a11 integrin chain constitutes the latest addition to the integrin family. a11b1 was originally identified on cultured human muscle cells, but recent studies have shown that it is not expressed on muscle cells in vivo. It remains to be determined if satellite cells in regenerating muscle express a11. Distribution data indicate that the a11 chain in vivo is expressed on a subset of mesenchymal cells in the developing human embryo. Expression is high in the developing musculoskeletal system in areas of cartilage, bone and in tendon formation. High a11 expression is also seen in mesenchymal tissues characterized by elaborately organized collagen matrices such as the intervertebral disc and the cornea. In agreement with the distribution data, ligand binding studies suggest that a11 prefers collagen I over collagen IV. We will review the current knowledge about a11b1 and discuss the possible in vivo functions of a11b1 and also address the issue of functional redundancy among collagen-binding integrins.

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Chapter category: Adhesion Molecules

Structure and Function of a11b1

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