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. 1987 Oct;80(4):1082–1089. doi: 10.1172/JCI113164

Plasminogen activator inhibitor is associated with the extracellular matrix of cultured bovine smooth muscle cells.

B S Knudsen 1, P C Harpel 1, R L Nachman 1
PMCID: PMC442350  PMID: 3116043

Abstract

The extracellular matrix secreted by cultured bovine smooth muscle cells (BSMC) contains an endothelial type plasminogen activator (PA) inhibitor. When PA is incubated with the matrix, a high molecular weight complex containing a truncated PA inhibitor is released into the supernatant. The inhibitor also dissociates from the matrix by treatment with glycine, pH 2.7, in its intact, functionally active, 45-kD form, whereas treatment of the matrix with thrombin results in the release of a cleaved, inactive, 41 kD PA inhibitor. Bowes melanoma cells but not smooth muscle cells cultured on BSMC matrices decrease available matrix associated PA inhibitor. PA inhibitor incorporated into the extracellular matrix may serve an important role in the regulation of plasminogen activator mediated matrix degradation.

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