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Gene Review

RNASE1  -  ribonuclease, RNase A family, 1 (pancreatic)

Bos taurus

Synonyms: RAC1, SRN
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Disease relevance of SRN


High impact information on SRN

  • Seminal RNase belongs to an interesting group of RNases, the RISBASES (RIbonucleases with Special, i.e. non catalytic, Biological Actions) other members of which include angiogenin, selectively neurotoxic RNases, a lectin and the self-incompatibility factors from a flowering plant [6].
  • Both the primary and tertiary structures of the RNase A differ substantially from those of the seminal ribonuclease in the loop region 16-22 [7].
  • The results presented here, while confirming and expanding upon those previously reported on the antitumor effects of bovine seminal RNase in vivo on primary thyroid epithelial tumors, indicate for the first time that bovine seminal RNase can also be regarded as a potent antimetastatic agent on in vivo spontaneous metastases [8].
  • Seminal ribonuclease inhibits tumor growth and reduces the metastatic potential of Lewis lung carcinoma [8].
  • In vitro studies on selective inhibition of tumor cell growth by seminal ribonuclease [9].

Chemical compound and disease context of SRN


Biological context of SRN


Anatomical context of SRN


Associations of SRN with chemical compounds


Other interactions of SRN

  • A comparison of the sequences of three homologous ribonucleases (RNase A, angiogenin and bovine seminal RNase) identifies three surface loops that are highly variable between the three proteins [23].

Analytical, diagnostic and therapeutic context of SRN


  1. Ribonuclease A can be transformed into a dimeric ribonuclease with antitumor activity. Di Donato, A., Cafaro, V., D'Alessio, G. J. Biol. Chem. (1994) [Pubmed]
  2. Antitumor action of bovine seminal ribonuclease. Cytostatic effect on human melanoma and mouse seminoma. Poucková, P., Soucek, J., Jelínek, J., Zadinová, M., Hlousková, D., Polívková, J., Navrátil, L., Cinátl, J., Matousek, J. Neoplasma (1998) [Pubmed]
  3. RNase inhibition of human immunodeficiency virus infection of H9 cells. Youle, R.J., Wu, Y.N., Mikulski, S.M., Shogen, K., Hamilton, R.S., Newton, D., D'Alessio, G., Gravell, M. Proc. Natl. Acad. Sci. U.S.A. (1994) [Pubmed]
  4. Expression of bovine seminal ribonuclease in Escherichia coli. de Nigris, M., Russo, N., Piccoli, R., D'Alessio, G., Di Donato, A. Biochem. Biophys. Res. Commun. (1993) [Pubmed]
  5. Bovine seminal ribonuclease exerts selective cytotoxicity toward neuroblastoma cells both sensitive and resistant to chemotherapeutic drugs. Cinatl, J., Cinatl, J., Kotchetkov, R., Matousek, J., Woodcock, B.G., Koehl, U., Vogel, J.U., Kornhuber, B., Schwabe, D. Anticancer Res. (2000) [Pubmed]
  6. Seminal RNase: a unique member of the ribonuclease superfamily. D'Alessio, G., Di Donato, A., Parente, A., Piccoli, R. Trends Biochem. Sci. (1991) [Pubmed]
  7. Swapping structural determinants of ribonucleases: an energetic analysis of the hinge peptide 16-22. Mazzarella, K., Vitagliano, L., Zagari, A. Proc. Natl. Acad. Sci. U.S.A. (1995) [Pubmed]
  8. Seminal ribonuclease inhibits tumor growth and reduces the metastatic potential of Lewis lung carcinoma. Laccetti, P., Spalletti-Cernia, D., Portella, G., De Corato, P., D'Alessio, G., Vecchio, G. Cancer Res. (1994) [Pubmed]
  9. In vitro studies on selective inhibition of tumor cell growth by seminal ribonuclease. Vescia, S., Tramontano, D., Augusti-Tocco, G., D'Alessio, G. Cancer Res. (1980) [Pubmed]
  10. Bovine seminal ribonuclease attached to nanoparticles made of polylactic acid kills leukemia and lymphoma cell lines in vitro. Michaelis, M., Matousek, J., Vogel, J.U., Slavik, T., Langer, K., Cinatl, J., Kreuter, J., Schwabe, D., Cinatl, J. Anticancer Drugs (2000) [Pubmed]
  11. Origin of the catalytic activity of bovine seminal ribonuclease against double-stranded RNA. Opitz, J.G., Ciglic, M.I., Haugg, M., Trautwein-Fritz, K., Raillard, S.A., Jermann, T.M., Benner, S.A. Biochemistry (1998) [Pubmed]
  12. Bovine seminal ribonuclease produced from a synthetic gene. Kim, J.S., Raines, R.T. J. Biol. Chem. (1993) [Pubmed]
  13. Glutathione-facilitated refolding of reduced, denatured bovine seminal ribonuclease: kinetics and characterization of products. Smith, G.K., D'Alessio, G., Schaffer, S.W. Biochemistry (1978) [Pubmed]
  14. Dissociation of bovine seminal ribonuclease into catalytically active monomers by selective reduction and alkylation of the intersubunit disulfide bridges. D'Alessio, G., Malorni, M.C., Parente, A. Biochemistry (1975) [Pubmed]
  15. Engineering the refolding pathway and the quaternary structure of seminal ribonuclease by newly introduced disulfide bridges. Russo, A., Antignani, A., Giancola, C., D'Alessio, G. J. Biol. Chem. (2002) [Pubmed]
  16. Immunosuppressive activity of bovine seminal RNase on T-cell proliferation. Tamburrini, M., Scala, G., Verde, C., Ruocco, M.R., Parente, A., Venuta, S., D'Alessio, G. Eur. J. Biochem. (1990) [Pubmed]
  17. The RNase a superfamily: Generation of diversity and innate host defense. Dyer, K.D., Rosenberg, H.F. Mol. Divers. (2006) [Pubmed]
  18. Effect of wheat leaf ribonuclease on tumor cells and tissues. Skvor, J., Lipovová, P., Poucková, P., Soucek, J., Slavík, T., Matousek, J. Anticancer Drugs (2006) [Pubmed]
  19. A role for the intersubunit disulfides of seminal RNase in the mechanism of its antitumor action. Bracale, A., Castaldi, F., Nitsch, L., D'Alessio, G. Eur. J. Biochem. (2003) [Pubmed]
  20. A study of the intracellular routing of cytotoxic ribonucleases. Wu, Y., Saxena, S.K., Ardelt, W., Gadina, M., Mikulski, S.M., De Lorenzo, C., D'Alessio, G., Youle, R.J. J. Biol. Chem. (1995) [Pubmed]
  21. Preparation of potent cytotoxic ribonucleases by cationization: enhanced cellular uptake and decreased interaction with ribonuclease inhibitor by chemical modification of carboxyl groups. Futami, J., Maeda, T., Kitazoe, M., Nukui, E., Tada, H., Seno, M., Kosaka, M., Yamada, H. Biochemistry (2001) [Pubmed]
  22. Intrachain disulfide bridges of bovine seminal ribonuclease. di Donato, A., D'Alessio, G. Biochim. Biophys. Acta (1979) [Pubmed]
  23. A hybrid of bovine pancreatic ribonuclease and human angiogenin: an external loop as a module controlling substrate specificity? Allemann, R.K., Presnell, S.R., Benner, S.A. Protein Eng. (1991) [Pubmed]
  24. The differential pattern of tissue-specific expression of ruminant pancreatic type ribonucleases may help to understand the evolutionary history of their genes. Sasso, M.P., Lombardi, M., Confalone, E., Carsana, A., Palmieri, M., Furia, A. Gene (1999) [Pubmed]
  25. New muteins of RNase A with enhanced antitumor action. Cafaro, V., Bracale, A., Di Maro, A., Sorrentino, S., D'Alessio, G., Di Donato, A. FEBS Lett. (1998) [Pubmed]
  26. Sequence analysis of a cloned cDNA coding for bovine seminal ribonuclease. Palmieri, M., Carsana, A., Furia, A., Libonati, M. Eur. J. Biochem. (1985) [Pubmed]
  27. Isolation of bovine seminal ribonuclease by affinity chromatography. Krietsch, W.K., Simm, F.C., Hertenberger, B., Kuntz, G.W., Wachter, E. Anal. Biochem. (1983) [Pubmed]
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