TAILIEUCHUNG - Báo cáo khoa học: A role for the intersubunit disulfides of seminal RNase in the mechanism of its antitumor action

The dimeric structure of seminal ribonuclease (BS-RNase) is maintained by noncovalent interactions and by two intersubunit disulfide unusual feature of this enzyme is its antitumour action, consisting in a cyto-toxic activity selective for malignant cytotoxic action is exerted when the protein reaches the cytosol of the affected cells, where it degrades ribosomal RNA, thus blocking protein synthesis and leading cells to death. | Eur. J. Biochem. 270 1980-1987 2003 FEBS 2003 doi A role for the intersubunit disulfides of seminal RNase in the mechanism of its antitumor action Aurora Bracale1 Francesco Castaldi1 Lucio Nitsch2 and Giuseppe D Alessio1 1Dipartimento di Chimica Biologica and 2Dipartimento di Biologia e Patologia Cellulare e Molecolare L. Califano Universita di Napoli Italy The dimeric structure of seminal ribonuclease BS-RNase is maintained by noncovalent interactions and by two intersubunit disulfide bridges. Aiiothr unusual I eat lire Iff this enzyme is its antitumour action consisting in a cytotoxic activity selective for malignant cells. This cytotoxic action is exerted when the protein reaches the cytosol of the affected cells where it degrades ribosomal RNA thus blocking protein synthesis and leading cells to death. The current model proposed for the mechanism of antitumour action of BS-RNase is based on the ability of the protein to resist the neutralizing action of the cytosolic RNase inhibitor a resistance due to the dimeric structure of the enzyme. Monomeric RNases and monomeric derivatives of BS-RNase are strongly bound by the inhibitor and inactive as antitumor agents. Hue we enort OTt mono meric derivatives of BS-RNase that although strongly inhibited by the cytosolic RNase inhibitor are cytotoxic towards malignant cells. Terere monomess are pnnduvdd by reductive cleavage of the intersubunit disulfides of the native dimeric protein followed by linking the exposed sulfhydryls to small thiols through formation of mixed disulfides. We okokI that uillIhydiySs I oom cell monolayess and cell membranes can attack these mixed disulfides in the monomeric derivatives and reconstitute through sulfhyd-ryl-disulfide interchange reactions the native dimeric protein which is internalized as such and displays its antitumour action. Keywords antitumor BS-RNase disulfides RNase. Seminal RNase from bovine seminal vesicles BS-RNase reviewed in 1 is a .

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