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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