An involucrin-like protein in hepatocytes serves as a substrate for tissue transglutaminase during apoptosis

Edit Tarcsa, Noemi Kedei, Vilmos Thomazy, L. Fésüs

Research output: Contribution to journalArticle

34 Citations (Scopus)

Abstract

Cornified envelopes and apoptotic bodies are transglutaminase-cross-linked end-products of physiological cell death pathways. The two structures have similar amino acid composition. Involucrin has been considered as a cornified envelope precursor protein expressed specifically in terminally differentiating keratinocytes and squamous epithelia. We report the presence in hepatocytes of an involucrin-like protein which could be purified from dog liver with procedures characteristic to involucrins. When compared to purified dog esophagus involucrin, the liver protein also reacts with anti-involucrin antibodies, has the same relative molecular mass, possesses similar amino acid composition, and shows almost identical peptide mapping pattern. The involucrin-like protein is detectable by immunohistochemistry in normal and apoptotic hepatocytes, is a substrate of tissue transglutaminase, and is incorporated into cross-linked apoptotic bodies. These results suggest that there are overlapping molecular components in the two characteristic forms (cornification and apoptosis) of naturally occurring cell death.

Original languageEnglish
Pages (from-to)25648-25651
Number of pages4
JournalJournal of Biological Chemistry
Volume267
Issue number36
Publication statusPublished - Dec 25 1992

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Hepatocytes
Apoptosis
Substrates
Proteins
Cell death
Liver
Cell Death
Dogs
Amino Acids
Transglutaminases
Peptide Mapping
Protein Precursors
Molecular mass
Chemical analysis
Keratinocytes
Esophagus
involucrin
transglutaminase 2
Anti-Idiotypic Antibodies
Epithelium

ASJC Scopus subject areas

  • Biochemistry

Cite this

An involucrin-like protein in hepatocytes serves as a substrate for tissue transglutaminase during apoptosis. / Tarcsa, Edit; Kedei, Noemi; Thomazy, Vilmos; Fésüs, L.

In: Journal of Biological Chemistry, Vol. 267, No. 36, 25.12.1992, p. 25648-25651.

Research output: Contribution to journalArticle

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