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J Biol Chem, Vol. 273, Issue 32, 20383-20389, August 7, 1998
From the We have found that chondrocytes express a novel
collagen type II-binding integrin, a new member of the
Isolation, Cloning, and Sequence Analysis of the Integrin Subunit
10, a 
1-associated Collagen Binding Integrin Expressed on
Chondrocytes
,
Department of Cell and Molecular Biology,
1-integrin
family. The integrin 
subunit, which has a
Mr of 160 kDa reduced, was isolated from bovine
chondrocytes by collagen type II affinity purification. The human
homologue was obtained by screening a human chondrocyte library with a
bovine cDNA probe. Cloning and cDNA sequence analysis of the
human integrin subunit designated 10 show that it shares the
general structure of other integrin subunits. The predicted amino
acid sequence consists of a 1167-amino acid mature protein, including a
signal peptide (22 amino acids), a long extracellular domain (1098 amino acids), a transmembrane domain (25 amino acids), and a short
cytoplasmic domain (22 amino acids). The extracellular part contains a
7-fold repeated sequence, an I-domain (199 amino acids) and three
putative divalent cation-binding sites. The deduced amino acid sequence
of 10 is 35% identical to the integrin subunit 2 and 37%
identical to the integrin subunit 1. Northern blot analysis shows a
single mRNA of 5.4 kilobases in chondrocytes. A peptide antibody
against the predicted sequence of the cytoplasmic domain of 10
immunoprecipitated two proteins with masses of 125 and 160 kDa from
chondrocyte lysates under reducing conditions. The peptide antibody
specifically stained chondrocytes in tissue sections of human articular
cartilage, showing that 101 is expressed in cartilage tissue.
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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