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PMID: 284351 Published · ppublish English Journal Article

Glycoprotein, elastin, and collagen secretion by rat smooth muscle cells.

Jones PA, Scott-Burden T, Gevers W

Abstract

Smooth muscle cells from rat heart secreted extracellular matrix components at high rates for many generations in culture. The matrix proteins remained anchored to the culture dish and were characterized after removal of cellular material with sodium dodecyl sulfate. Sequential enzyme digestion demonstrated the presence of at least three components, including glycoprotein(s), elastin, and collagen. Prolonged extraction of the matrix with detergent under reducing conditions solubilized a fucosylated glycoprotein having an apparent molecular weight of 250,000 and two other proteins with molecular weights of 72,000 and 45,000, respectively. Sublines derived from discrete colonies of smooth muscle cells synthesized all of the matrix components, and the proportion of collagen secreted by some sublines increased with time in culture. The biosynthesis of a mixed extracellular matrix and the relationships among the component proteins were therefore studied in one system producing milligram quantities of material.

MeSH Terms
Animals Cells, Cultured Collagen/metabolism Elastin/metabolism Extracellular Space/metabolism Glycoproteins/metabolism Molecular Weight Muscle Proteins/metabolism Muscle, Smooth/metabolism Myocardium/metabolism Rats
Chemicals
Glycoproteins Muscle Proteins Collagen Elastin
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Jones P A
Scott-Burden T
Gevers W
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25 references, click to expand
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
Published
1979-01-00
Pages
353-7
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC382937
Subset
IM
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