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High amount of epsilon-(gamma-glutamyl)lysine cross-links in Mallory bodies

K Zatloukal1, L Fesus, H Denk

  • 1Laboratory of Molecular Pathology, University of Graz School of Medicine, Austria.

Laboratory Investigation; a Journal of Technical Methods and Pathology
|June 1, 1992
PubMed

Insights

Mallory bodies (MBs) in alcoholic hepatitis result from protein cross-linking. This study found epsilon-(gamma-glutamyl)lysine bonds in experimentally induced MBs, suggesting transglutaminase activity is key to their formation.

Area of Science:

  • Hepatology
  • Biochemistry
  • Cell Biology

Background:

  • Alcoholic hepatitis is the most severe form of alcoholic liver disease.
  • It is characterized by inflammation, hepatocyte necrosis, and Mallory bodies (MBs).
  • MBs are filamentous cytoplasmic inclusions composed of insoluble, high molecular weight proteins.

Purpose of the Study:

  • To investigate the role of protein cross-linking in the formation of experimentally induced Mallory bodies.
  • To analyze for the presence of epsilon-(gamma-glutamyl)lysine bonds in MBs.

Main Methods:

  • Experimental induction of MBs in mouse livers using griseofulvin or 3,5-diethoxycarbonyl-1,4-dihydrocollidine.
  • Isolation and purification of MBs.
  • Quantification of epsilon-(gamma-glutamyl)lysine cross-links in purified MBs.

Main Results:

  • Highly purified MBs contained significant amounts of epsilon-(gamma-glutamyl)lysine isodipeptide linkages.
  • Griseofulvin-induced MBs had 19.7 nmoles of linkage per mg of protein.
  • 3,5-diethoxycarbonyl-1,4-dihydrocollidine-induced MBs had 14.4 nmoles of linkage per mg of protein.

Conclusions:

  • Transglutaminase-catalyzed protein cross-linking plays a significant role in Mallory body formation.
  • The presence of these cross-links provides a molecular explanation for MBs in alcoholic hepatitis.
  • This finding may open new avenues for understanding and potentially treating alcoholic liver disease.

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