PMID: 1968333Feb 1, 1990

Post-translational modification of apolipoprotein B by transglutaminases

The Biochemical Journal
E CocuzziS I Chung

Abstract

The major form of cross-link found in apolipoprotein B was identified as N1N12-bis-(gamma-glutamyl)spermine, a product known to be formed through the catalytic action of transglutaminases (EC 2.3.2.13). N1-(gamma-Glutamyl)spermine was present in a trace amount but epsilon-(gamma-glutamyl)lysine cross-links, which are formed during fibrin formation in plasma, were not detected. In the presence of catalytic amounts of plasma Factor XIIIa (a thrombin-dependent extracellular transglutaminase) or cellular transglutaminase (a cytosolic enzyme), apolipoprotein B and other plasma apolipoproteins (A-I, A-II and C) underwent covalently bridged polymerization and served as amine acceptor substrates. These results suggests that transglutaminases may participate in the covalent modification of apolipoproteins, either in the physiological state or during pathogenesis.

Citations

May 20, 2004·Clinica Chimica Acta; International Journal of Clinical Chemistry·A Gugliucci
Jul 31, 1990·Biochemical and Biophysical Research Communications·J M Bowness, A H Tarr
Jan 1, 1992·Cancer Immunology, Immunotherapy : CII·E B Reilly, G Antognetti
Sep 2, 2011·Current Opinion in Lipidology·Miriam Lee-Rueckert, Petri T Kovanen
Aug 1, 1994·International Journal of Cancer. Journal International Du Cancer·K Mehta

Related Concepts

Apoproteins B
Ion-Exchange Chromatography Procedure
Cross-Linking Reagents
SDS-PAGE
Cavia porcellus
Hydrolysis
Lipoproteins
Liver
Post-Translational Protein Processing
Transglutaminases

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