Characterization of a Putative Clone for the 67-Kilodalton Elastin/Laminin Receptor Suggests That It Encodes a Cytoplasmic Protein Rather than a Cell Surface Receptor

Leonard E. Grosso, Pyong Woo Park, Robert P. Mecham

Research output: Contribution to journalArticle

42 Scopus citations

Abstract

The 67-kDa elastin binding protein shares many immunological and structural properties with the high-affinity 67-kDa tumor cell laminin receptor. Taking advantage of these similarities, we have screened a bovine cDNA library with a partial cDNA probe for the laminin receptor and have isolated and characterized a cDNA clone of 1038 bp that hybridizes to a single-size mRNA of 1.3 kb. The clone encodes a protein with a predicted molecular weight of 33K that lacks an N-terminal leader sequence, shows no posttranslational processing when translated in vitro in the presence of microsomes, and does not bind to elastin affinity columns. Although the bovine clone is nearly identical with clones encoding human and mouse proteins proported to be 67-kDa laminin receptor, physical and functional characteristics of the encoded protein suggest that it is a cytoplasmic protein that does not bind elastin. This finding calls into question the earlier conclusion that the clone encodes the 67-kDa receptor.

Original languageEnglish
Pages (from-to)3346-3350
Number of pages5
JournalBiochemistry
Volume30
Issue number13
DOIs
StatePublished - Apr 1 1991

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