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Gewählte Publikation:

ZATLOUKAL, K; FESUS, L; DENK, H; TARCSA, E; SPUREJ, G; BOCK, G.
High amount of epsilon-(gamma-glutamyl)lysine cross-links in Mallory bodies.
LAB INVEST. 1992; 66(6): 774-777.
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Führende Autor*innen der Med Uni Graz
Zatloukal Kurt
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Abstract:
Alcoholic hepatitis, the most severe form of alcoholic liver disease, is associated with inflammation, liver cell necrosis, and the appearance of Mallory bodies (MBs) in hepatocytes. Identical MBs can be experimentally induced in mouse livers by chronic griseofulvin or 3,5-diethoxycarbonyl-1,4-dihydrocollidine treatment. MBs are filamentous cytoplasmic inclusions containing insoluble high molecular weight protein material. Covalent polymerization of intracellular proteins may occur through formation of epsilon-(gamma-glutamyl)lysine cross-links catalyzed by Ca(2+)-dependent transglutaminases. Therefore, isolated experimentally-induced MBs were analyzed for the presence of epsilon-(gamma-glutamyl)lysine bonds. Highly purified MBs contained 19.7 nmole (griseofulvin-induced) and 14.4 nmoles (3,5-diethoxycarbonyl-1,4-dihydrocollidine induced) of isodipeptide linkage, respectively, per mg of protein. These results suggest that transglutaminase-induced cross-linking of proteins plays a major role in MB formation.
Find related publications in this database (using NLM MeSH Indexing)
Animals -
Dicarbethoxydihydrocollidine -
Dipeptides - analysis
Griseofulvin - analysis
Inclusion Bodies - metabolism
Liver Diseases - chemically induced
Male - chemically induced
Mice - chemically induced
Transglutaminases - metabolism

Find related publications in this database (Keywords)
TRANSGLUTAMINASE
ALCOHOLIC HEPATITIS
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