Sequence identity between the alpha sub(2)-macroglobulin receptor and low density lipoprotein receptor-related protein suggest that this molecule is a multifunctional receptor

Ten peptides, derived from human alpha sub(2)-macroglobulin ( alpha sub(2)M) receptor by chemical or proteolytic digestion, were sequenced. Comparative analysis revealed that all of the resulting sequences were present within the cDNA-deduced structure of low density lipoprotein receptor-related pro...

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Published inThe Journal of biological chemistry Vol. 265; no. 29; pp. 17401 - 17404
Main Authors Strickland, D K, Ashcom, J D, Williams, S, Burgess, W H, Migliorini, M, Argraves, W S
Format Journal Article
LanguageEnglish
Published 01.01.1990
Subjects
alpha -macroglobulin
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Summary:Ten peptides, derived from human alpha sub(2)-macroglobulin ( alpha sub(2)M) receptor by chemical or proteolytic digestion, were sequenced. Comparative analysis revealed that all of the resulting sequences were present within the cDNA-deduced structure of low density lipoprotein receptor-related protein (LRP). The findings provide evidence that the alpha sub(2)M receptor and LRP are the same molecule. The apparent identity of LRP and the alpha sub(2)M receptor suggests that this molecule is a multifunctional receptor with the capacity to bind diverse biological ligands and highlights a possible relationship between two previously unrelated biological processes, lipid metabolism and proteinase regulation.
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ISSN:0021-9258