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J Biol Chem, Vol. 274, Issue 42, 29819-29825, October 15, 1999
4A Integrin Subunit in Relation to the
Differentiation State in Human Intestinal Cells
From the Centre de Recherche en Biologie du Développement des
Épitheliums et Thématique de Physiopathologie Digestive
du Centre de Recherche Clinique du CUSE, Département d'anatomie
et de biologie cellulaire, Faculté de médecine,
Université de Sherbrooke, Sherbrooke,
Québec, Canada J1H 5N4
Integrins are important mediators of cell-laminin
interactions. In the small intestinal epithelium, which consists of
spatially separated proliferative and differentiated cell populations
located, respectively, in the crypt and on the villus, laminins and
laminin-binding integrins are differentially expressed along the
crypt-villus axis. One exception to this is the integrin
6
4, which is thought to be
ubiquitously expressed by intestinal cells. However, in this study, a
re-evaluation of the
4 subunit expression with different
antibodies revealed that two forms of
4 exist in the human intestinal epithelium. Furthermore, we show that differentiated enterocytes express a full-length 205-kDa
4A subunit,
whereas undifferentiated crypt cells express a novel
4A
subunit that does not contain the COOH-terminal segment of the
cytoplasmic domain (
4Actd
). This new form
was not found to arise from alternative
4 mRNA
splicing. Moreover, we found that these two
4A forms can
associate into
6
4A complexes; however,
the
4Actd
integrin expressed by the
undifferentiated crypt cells is not functional for adhesion to
laminin-5. Hence, these studies identify a novel
6
4Actd
integrin expressed
in undifferentiated intestinal crypt cells that is functionally distinct.
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