Cloning and sequence of the cDNA encoding the beta 4 integrin subunit in rat peripheral nerve

Abstract

beta 4 and alpha 6 integrin subunits dimerize to form an adhesion receptor that is necessary to nucleate hemidesmosomes and to anchor epithelial cells to their basal laminae. beta 4 is also expressed in Schwann cell (which do not contain hemidesmosomes) in peripheral nerve, where it may function in the formation or maintenance of myelin. The cDNA for beta 4 integrin has been cloned from epithelia-derived human and mouse tissues. We cloned cDNAs encoding beta 4 integrin from libraries derived from rat peripheral nerve, and determined the complete nucleotide sequence encoding the signal peptide and mature protein. Comparison of the deduced amino acid (aa) sequence revealed 95.1% and 87.5% identity with the mouse and human epithelia-derived sequences, respectively. The amino acid sequence of postulated signal transduction domains in beta 4 was 100% identical among rat, mouse, and human. Our cDNA clones included two of the four postulated alternatively spliced variants previously described in epithelial clones. Despite the potentially diverse functions of beta 4 integrin in Schwann cells and keratinocytes, the cDNAs for nerve-derived beta 4 integrin are highly similar to those cloned from epithelia.