Detection and partial characterization of a specific plasminogen activator inhibitor in human chondrocyte cultures.

Detection and partial characterization of a specific plasminogen activator inhibitor in human chondrocyte cultures. Research Abstract Details 

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Detection and partial characterization of a specific plasminogen activator inhibitor in human chondrocyte cultures. Abstract Text:

H Yamada,R W Stephens,T Nakagawa,D McNicol,

Serum-free culture medium collected from primary monolayer cultures of human articular chondrocytes was found to inhibit human urokinase [EC 3.4.21.31] activity. Although chondrocyte culture medium contained a small amount of endothelial-type plasminogen activator inhibitor which could be demonstrated by reverse fibrin autography, most of the urokinase inhibitory activity of chondrocyte culture medium was shown to be due to a different molecule from endothelial-type inhibitor, since it did not react with a specific antibody to this type of inhibitor. The dominant urokinase inhibitor in chondrocyte culture medium was partially purified by concanavalin A-Sepharose affinity chromatography. The partially purified inhibitor inhibited high-Mr urokinase more effectively than low-Mr urokinase, but no obvious inhibition was detected against tissue-type plasminogen activator, plasmin, trypsin, and thrombin. The inhibitor had an apparent Mr of 43,000 on sodium dodecyl sulfate polyacrylamide gel electrophoresis, and it was unstable to sodium dodecyl sulfate, acid, and heat treatments. Inhibition of urokinase by the inhibitor was accompanied with the formation of a sodium dodecyl sulfate-stable high-Mr complex between them. Inhibition and complex formation required the active site of urokinase. The partially purified inhibitor was thought to be immunologically different from the known classes of plasminogen activator inhibitors, including endothelial-type inhibitor, macrophage/monocyte inhibitor, and protease nexin, since it did not react with specific antibodies to these inhibitors.

Detection and partial characterization of a specific plasminogen activator inhibitor in human chondrocyte cultures. Publishing Authors By Initials

H Yamada,RW Stephens,T Nakagawa,D McNicol,

For similar enzymes and coenzymes: enzymes: hydrolases: peptide hydrolases: endopeptidases: serine endopeptidases: urinary plasminogen activator research abstracts see: enzymes and coenzymes: enzymes: hydrolases: peptide hydrolases: endopeptidases: serine endopeptidases: urinary plasminogen activator research

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Detection and partial characterization of a specific plasminogen activator inhibitor in human chondrocyte cultures. Journal Published:

PUBLICATION TYPE: Research Support, Non-U.S. Gov

Journal: Journal of biochemistry

VOLUME: 104

Page Numbers: 960-7

Journal Abbreviation: J. Biochem.

ISSN: 0021-924X

DAY: 19

MONTH: Dec

YEAR: 1988

Detection and partial characterization of a specific plasminogen activator inhibitor in human chondrocyte cultures. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 376600

Detection and partial characterization of a specific plasminogen activator inhibitor in human chondrocyte cultures. Keywords Mesh Terms:

KEYWORDS: Urinary Plasminogen Activator

MESH TERMS: antagonists & inhibitors

Chemical & Substance for Abstract: Detection and partial characterization of a specific plasminogen activator inhibitor in human chondrocyte cultures. Information

Substance Name: Urinary Plasminogen Activator

Registry Number: EC 3.4.21.73

Grant and Affiliation Information for Detection and partial characterization of a specific plasminogen activator inhibitor in human chondrocyte cultures.

AFFILIATION: Department of Medicine and Clinical Science, John Curtin School of Medical Research, Australian National University, Canberra.

Country: JAPAN

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MEDLINETA: J Biochem

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