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

B S Knudsen; P C Harpel; R L Nachman

doi:10.1172/JCI113164

Division of Hematology-Oncology, Cornell University Medical College, New York 10021.

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Division of Hematology-Oncology, Cornell University Medical College, New York 10021.

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Division of Hematology-Oncology, Cornell University Medical College, New York 10021.

Find articles by Nachman, R. in: PubMed | Google Scholar

Published in Volume 80, Issue 4 on October 1, 1987
J Clin Invest. 1987;80(4):1082–1089. https://doi.org/10.1172/JCI113164.
© 1987 The American Society for Clinical Investigation

Published October 1, 1987 - Version history

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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