A novel integrin (alpha E beta 4) from human epithelial cells suggests a fourth family of integrin adhesion receptors.

Kajiji S, Tamura RN, Quaranta V
EMBO J. 1989 8 (3): 673-80

PMID: 2542022 · PMCID: PMC400860

A new member of the integrin superfamily of adhesion receptors was isolated from human epithelial cells. Analogously to other integrins, this molecule is a heterodimer comprised of structurally unrelated subunits, both glycosylated. Unequivocal amino-acid sequence homologies were observed between these subunits and integrin alpha and beta chain sequences, indicating that this epithelial heterodimer is a novel integrin. No obvious serologic cross-reactivities were detected with other integrins. The beta chain of the epithelial integrin displayed a mol. wt significantly higher than other integrin beta chains, possibly due to a large sialic acid content. Integrin heterodimers are grouped into three families, based on which of three beta chains (beta 1, beta 2 and beta 3) they contain. Therefore, the epithelial integrin may represent the prototype of a fourth integrin family, because it contains a structurally distinct beta chain. The designation alpha E beta 4 is proposed for this novel human integrin.

MeSH Terms (12)

Amino Acid Sequence Cell Adhesion Epithelium Humans Immunochemistry Integrin beta4 Integrins Membrane Glycoproteins Molecular Sequence Data Molecular Weight Protein Conformation Receptors, Cell Surface

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