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Deficiency of 5'-deoxy-5'-methylthioadenosine phosphorylase activity in malignancy. Absence of the protein in human enzyme-deficient cell lines (Articolo in rivista)

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Deficiency of 5'-deoxy-5'-methylthioadenosine phosphorylase activity in malignancy. Absence of the protein in human enzyme-deficient cell lines (Articolo in rivista) (literal)

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Della Ragione, F. and Oliva, A. and Palumbo, R. and Russo, G.L. and Gragnaniello, V. and Zappia, V. (1992)
Deficiency of 5'-deoxy-5'-methylthioadenosine phosphorylase activity in malignancy. Absence of the protein in human enzyme-deficient cell lines
in Biochemical journal (Lond., 1984); Biochemical Society, London (Regno Unito)
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Della Ragione, F. and Oliva, A. and Palumbo, R. and Russo, G.L. and Gragnaniello, V. and Zappia, V. (literal)

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cited By (since 1996)8 Questa pubblicazione si riferisce a un periodo in cui gli autori non lavoravano presso il CNR PDF scaricabile gratuitamente al sito: http://www.biochemj.org/bj/281/bj2810533.htm (literal)

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Istituto di Biochimica, I Faclt di Med e Chirurgia, Universita di Napoli, 80138 Napoli, Italy (literal)

Titolo

Deficiency of 5'-deoxy-5'-methylthioadenosine phosphorylase activity in malignancy. Absence of the protein in human enzyme-deficient cell lines (literal)

Abstract

The absence of 5'-deoxy-5'methylthioadenosine phosphorylase (MTAase) activity in malignant cells, and the putative localization of its gene, suggest that this enzyme deficiency might be due to a genomic alteration also involving a tumour-suppressor gene. We studied the possible occurrence of inactive forms of the protein in two MTAase-negative cell lines, namely K562 and Jurkat, by immunochemical methods. Two highly specific antisera, directed against different epitopes of the phosphorylase [Della Ragione, Oliva, Gragnaniello, Russo, Palumbo and Zappia (1990) J. Biol. Chem. 265, 6241-6246], were used to carry out immunotitration and immunoblotting analyses, as well as to investigate the biosynthesis of the enzyme. No MTAase protein was detected by Western-blotting technique performed under conditions where all the phosphorylase-positive samples gave a clear band at the MTAase subunit molecular mass. No cross-reacting material was observed by a sensitive immunotitration method which permitted the detection of as low as 0.5 ng of protein. Moreover, the results obtained by [ 35S]methionine-labelling experiments ruled out phosphorylase biosynthesis in the negative cell lines. Altogether, these data suggest that an alteration at the gene level hampering the specific mRNA biosynthesis or resulting in an untranslatable mRNA is the cause of the enzyme deficiency in the MTAase-negative cell lines studied. (literal)

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