PMID: 2481149Dec 1, 1989Paper

Hepatocellular cytokeratins as substrates of transglutaminases.

Laboratory Investigation; a Journal of Technical Methods and Pathology
K ZatloukalI Rainer

Abstract

To examine whether hepatocellular cytokeratins can serve as substrates of transglutaminases (TG) TG-catalyzed incorporation of [3H]putrescine into, as well as cross-linking of, cytokeratins was studied. Purified guinea pig liver TG and mouse liver TG present in 105,000 x g supernatants were used as enzymes. Isolated mouse liver cytokeratin filaments, heterotypic tetramers (A2D2), as well as cytokeratin filaments reconstituted from isolated and column-purified liver cytokeratin polypeptides A and D served as substrates. Moreover, to more closely mimic the situation within the cell, mouse liver homogenate containing cytokeratins was also used. Cross-linked proteins were identified as cytokeratins by immunoblotting after sodium dodecyl sulfate-polyacrylamide gel electrophoresis using cytokeratin antibodies. The results indicated that mouse liver cytokeratins can serve as substrates of homologous and heterologous TG. However, liver cytokeratin components A and D differed in this respect. Depending on the experimental conditions either components D or components A were better substrates of TG-mediated cross-linking as revealed by increased high molecular weight aggregates, which failed to enter the gels, concomitant with a decrease ...Continue Reading

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