Molecular cloning and developmental expression of the Xenopus homolog of integrin alpha 4.

Abstract

Integrin receptors containing an alpha 4 subunit mediate cell-cell adhesion by binding to VCAM and MadCAM-1 in addition to supporting cell-extracellular matrix (ECM) adhesion by binding to the alternatively spliced V-region of fibronectin (FN). Studies in chick and mouse embryos have implicated these integrins in neural crest migration, myotube formation, heart development, and placentation. Because integrin-FN adhesive interactions have been shown to play essential roles in mammalian development, studies were initiated of integrin alpha 4 in amphibian embryos, which are better suited to experimental analyses of the earliest stages of embryogenesis. Here, the cDNA cloning and pattern of expression of the Xenopus laevis homolog of integrin alpha 4 is reported. Xenopus alpha 4 is 55% identical at the amino-acid level to both its human and mouse counterparts, including conservation of an alpha 4-specific protease cleavage site, 11 potential N-linked glycosylation sites, and 24 cysteine residues. In situ hybridization analysis reveals that transcripts encoding alpha 4 are expressed in epidermis and the branchial arches. Although alpha 4 transcripts can be detected as early as gastrulation, the protein is observed only after tailbud stages of development and is spatially restricted to the epidermis and gills of tadpole stage embryos. From these data it is concluded that Xenopus integrin alpha 4 has structural features in common with other vertebrate alpha 4 homologs, but is detected in a more restricted tissue distribution during development than alpha 4 in other species.