We have described a protein (Hep27) [Donadel, G., Garzelli, C., Frank, R. & Gabrielli, F. (1991) Eur. J. Biochem. 195, 723-729] which is synthesized and accumulated in the nucleus of human hepatoblastoma (HepG2) cells, following growth arrest induced by butyrate treatment. The synthesis of Hep27 is inhibited in cells that, released from the butyrate block, have resumed DNA synthesis. This report describes the cloning and the characterization of the cDNA coding for the Hep27 protein. The translation of the Hep27 cDNA predicts an amino acid sequence that can be aligned with those of the known short-chain alcohol dehydrogenase enzymes (SCAD) family. Both the recognition of enzymic functional domains and the similarity with the SCAD family of proteins of several amino acid blocks throughout the molecule, strongly suggest that this protein is a new member of the SCAD family. In agreement with its nuclear localization Hep27 has a region similar to the bipartite nuclear-targeting sequence. The study of Hep27 mRNA expression and protein synthesis suggests the existence of a regulation at the post-transcriptional level. The possible nuclear role of the Hep27 protein is discussed.

Gabrielli, F., Donadel, G., Bensi, G., Heguy, A., Melli, M. (1995). A nuclear protein, synthesized in growth-arrested human hepatoblastoma cells, is a novel member of the short-chain alcohol dehydrogenase family. EUROPEAN JOURNAL OF BIOCHEMISTRY, 232(2), 473-477 [10.1111/j.1432-1033.1995.tb20833.x].

A nuclear protein, synthesized in growth-arrested human hepatoblastoma cells, is a novel member of the short-chain alcohol dehydrogenase family

DONADEL, GIULIA;
1995-09-01

Abstract

We have described a protein (Hep27) [Donadel, G., Garzelli, C., Frank, R. & Gabrielli, F. (1991) Eur. J. Biochem. 195, 723-729] which is synthesized and accumulated in the nucleus of human hepatoblastoma (HepG2) cells, following growth arrest induced by butyrate treatment. The synthesis of Hep27 is inhibited in cells that, released from the butyrate block, have resumed DNA synthesis. This report describes the cloning and the characterization of the cDNA coding for the Hep27 protein. The translation of the Hep27 cDNA predicts an amino acid sequence that can be aligned with those of the known short-chain alcohol dehydrogenase enzymes (SCAD) family. Both the recognition of enzymic functional domains and the similarity with the SCAD family of proteins of several amino acid blocks throughout the molecule, strongly suggest that this protein is a new member of the SCAD family. In agreement with its nuclear localization Hep27 has a region similar to the bipartite nuclear-targeting sequence. The study of Hep27 mRNA expression and protein synthesis suggests the existence of a regulation at the post-transcriptional level. The possible nuclear role of the Hep27 protein is discussed.
1-set-1995
Pubblicato
Rilevanza internazionale
Articolo
Esperti anonimi
Settore MED/04 - PATOLOGIA GENERALE
English
Con Impact Factor ISI
Alcohol Dehydrogenase; Hydroxysteroid Dehydrogenases; Carcinoma, Hepatocellular; Humans; Protein Processing, Post-Translational; Alcohol Oxidoreductases; Amino Acid Sequence; Cloning, Molecular; RNA, Messenger; Liver Neoplasms; DNA, Complementary; Base Sequence; Neoplasm Proteins; Tumor Cells, Cultured; Nuclear Proteins; Molecular Sequence Data; 11-beta-Hydroxysteroid Dehydrogenases; G1 Phase; Sequence Homology, Amino Acid
Gabrielli, F., Donadel, G., Bensi, G., Heguy, A., Melli, M. (1995). A nuclear protein, synthesized in growth-arrested human hepatoblastoma cells, is a novel member of the short-chain alcohol dehydrogenase family. EUROPEAN JOURNAL OF BIOCHEMISTRY, 232(2), 473-477 [10.1111/j.1432-1033.1995.tb20833.x].
Gabrielli, F; Donadel, G; Bensi, G; Heguy, A; Melli, M
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/2108/53219
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