Chapter category: Adhesion Molecules
Integrin a1b1
I Domains in Integrins
Edited by: Donald GullbergISBN: 0-306-47836-6
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Chapter authors:
Humphrey Gardner
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Introduction The integrin a1 subunit was first discovered by Hemler et al as the a component of the Very Late Antigen I (VLA1) expressed on a subset of T cells in the joints of patients with rheumatoid arthritis,1 as well as in a subset of lymphocytes after long term in vitro culture.2 a1 is the largest of the a subunits, with an apparent mw of 190 kDa nonreduced and 210 kDa reduced. a1’s larger size compared to a2 is most likely due to a higher degree of glycosylation (see also Gullberg et al chapter 6). At the C terminus, the intracellular portion of a1 is the shortest of the a subunits, at 13 residues.
Functionally, a1 is one of four collagen binding bI domain containing a1 partners, along with a2, a10 and a11. The tissue distributions of these four, along with their differing relative affinities for different collagen types, suggest both the differences and potential overlaps in their physiological roles. None of the four are known to partner with any a subunit other than b1. The a1 I domain is likely to show, like a2, a10 and a11, affinity modulation of ligand binding activity in the same way as has been described for aL,4,5 but experimental evidence for this has not yet been published.
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