Elastin Binds to a Multifunctional 67-Kilodalton Peripheral Membrane Protein

Robert P. Mecham, Aleksander Hinek, Ruth Entwistle, Gail L. Griffin, Robert M. Senior, David S. Wrenn

Research output: Contribution to journalArticlepeer-review

156 Scopus citations

Abstract

Elastin binding proteins from plasma membranes of elastin-producing cells were isolated by affinity chromatography on immobilized elastin peptides. Three proteins of 67, 61, and 55 kDa were released from the elastin resin by guanidine/detergent, soluble elastin peptides, synthetic peptide VGVAPG, or galactoside sugars, but not by synthetic RGD-containing peptide or sugars not related to galactose. All three proteins incorporated radiolabel upon extracellular iodination and contained [3H]leucine following metabolic labeling, confirming that each is a synthetic product of the cell. The 67-kDa protein could be released from the cell surface with lactose-containing buffers, whereas solubilization of the 61- and 55-kDa components required the presence of detergent. Although all three proteins were retained on elastin affinity columns, the 61- and 55-kDa components were retained only in the presence of 67-kDa protein, suggesting that the 67-kDa protein binds elastin and the 61- and 55-kDa proteins bind to the 67-kDa protein. We propose that the 67-, 61-, and 55-kDa proteins constitute an elastin-receptor complex that forms a transmembrane link between the extracellular matrix and the intracellular compartment.

Original languageEnglish
Pages (from-to)3716-3722
Number of pages7
JournalBiochemistry
Volume28
Issue number9
DOIs
StatePublished - May 1 1989

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