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001-es BibID:	BIBFORM060770
Első szerző:	Zatloukal, Kurt
Cím:	High amount of epsilon-(gamma-glutamyl)lysine cross-links in Mallory bodies / K. Zatloukal, L. Fésüs, H. Denk, E. Tarcsa, G. Spurej, G. Bock
Dátum:	1992
ISSN:	0023-6837
Megjegyzések:	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.
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:	Laboratory Investigation 66 : 6 (1992), p. 774-777. -
További szerzők:	Fésüs László (1947-) (orvos biokémikus) Denk, H. Tarcsa Edit Spurej, G. Bock, G.
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