Transglutaminase-catalysed cross-linking: a potential mechanism for the interaction of fibrinogen, low density lipoprotein and arterial type III procollagen

Thrombosis Research
J M BownessR I Wiebe

Abstract

Bovine type III [3H]procollagen or its [125I]aminopropeptide were shown by chromatography under dissociating conditions to form very high molecular weight compounds with excess bovine fibrinogen after incubation with purified tissue transglutaminase, though none is formed with other major plasma proteins. Larger compounds of this type formed from fibrinogen or fibrin monomer can be separated by centrifugation and they are insoluble on washing with 1% SDS. Ultracentrifugation showed that a significant fraction of [3H]procollagen III forms a low density complex on incubation with transglutaminase plus excess IDL or LDL, but not HDL. SDS polyacrylamide gel electrophoresis showed that type III collagen [125I]aminopropeptide forms high molecular weight compounds after incubation with transglutaminase plus excess IDL or LDL but not with HDL. It is hypothesized that, in the presence of excessive concentrations of LDL and/or fibrinogen and of tissue transglutaminase, crosslinking reactions of the type demonstrated may interfere with normal injury-repair processes and stimulate the formation of atherosclerotic lesions in arteries.

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Citations

Aug 11, 2011·Amino Acids·Shobana ShanmugasundaramMaria V Nurminskaya
Dec 12, 2001·Neurochemistry International·Soo Youl KimPeter M Steinert
Dec 1, 1990·Proceedings of the National Academy of Sciences of the United States of America·S N Murthy, L Lorand
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Jan 28, 2021·International Journal of Molecular Sciences·Mariya E Semkova, J Justin Hsuan

Related Concepts

Metazoa
Catalysis
Bos indicus
Chromatography, Affinity
Cross-Linking Reagents
SDS-PAGE
Gamma-Fibrinogen
LDL-1
Chemical Precipitation
Procollagen Type M

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