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Gene Review

CSN2  -  casein beta

Sus scrofa

 
 
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Disease relevance of CSN2

 

High impact information on CSN2

  • The synthetic peptide NH2-Tyr-Pro-Phe-Pro-CONH2 (morphiceptin), which is the amide of a fragment of the milk protein beta-casein, has morphinelike activities and is highly specific for morphine (mu) receptors but not for enkephalin (delta) receptors [2].
  • The primary site of amine incorporation by factor XIIIa in beta-casein was identified as glutamine 167 [3].
  • The validity of the procedure is demonstrated by the preparation of photosensitive derivatives of substance P and glucagon 1-6 and in the cleavable covalent cross-linking of guanidinated beta-casein [4].
  • Evidence for intermolecular cross-linking through polyamines with both the liver enzyme and thrombin-activated human plasma blood coagulation factor XIII was obtained by the use of a guanidinated derivative of beta-casein [5].
  • This suggests that the regulation of the beta-lactoglobulin gene is distinct from that of beta-casein and WAP [6].
 

Biological context of CSN2

 

Anatomical context of CSN2

 

Associations of CSN2 with chemical compounds

 

Analytical, diagnostic and therapeutic context of CSN2

References

  1. Purification of porcine beta-casein, N-terminal sequence, quantification in mastitic milk. Kauf, A.C., Kensinger, R.S. J. Anim. Sci. (2002) [Pubmed]
  2. Morphiceptin (NH4-tyr-pro-phe-pro-COHN2): a potent and specific agonist for morphine (mu) receptors. Chang, K.J., Lillian, A., Hazum, E., Cuatrecasas, P., Chang, J.K. Science (1981) [Pubmed]
  3. Structural features of glutamine substrates for human plasma factor XIIIa (activated blood coagulation factor XIII). Gorman, J.J., Folk, J.E. J. Biol. Chem. (1980) [Pubmed]
  4. Transglutaminase amine substrates for photochemical labeling and cleavable cross-linking of proteins. Gorman, J.J., Folk, J.E. J. Biol. Chem. (1980) [Pubmed]
  5. Transglutaminase-catalyzed cross-linking through diamines and polyamines. Schrode, J., Folk, J.E. J. Biol. Chem. (1978) [Pubmed]
  6. Induction of lactogenesis in transgenic virgin pigs: evidence for gene and integration site-specific hormonal regulation. Shamay, A., Pursel, V.G., Wall, R.J., Hennighausen, L. Mol. Endocrinol. (1992) [Pubmed]
  7. Neoglycoproteins: in vitro introduction of glycosyl units at glutamines in beta-casein using transglutaminase. Yan, S.B., Wold, F. Biochemistry (1984) [Pubmed]
  8. Structure-activity relationships of cyclic beta-casomorphin-5 analogues. Schmidt, R., Neubert, K., Barth, A., Liebmann, C., Schnittler, M., Chung, N.N., Schiller, P.W. Peptides (1991) [Pubmed]
  9. Molecular cloning and phylogenetic analysis of canine beta-casein. Watanabe, M., Sugano, S., Togashi, T., Imai, J., Uchida, K., Yamaguchi, R., Tateyama, S. DNA Seq. (2000) [Pubmed]
  10. Digestion by pancreatic juice of a beta-casomorphin-containing fragment of buffalo beta-casein. Petrilli, P., Pucci, P., Pelissier, J.P., Addeo, F. Int. J. Pept. Protein Res. (1987) [Pubmed]
  11. Identification of a substrate site for transglutaminases on the human protein synthesis initiation factor 5A. Beninati, S., Nicolini, L., Jakus, J., Passeggio, A., Abbruzzese, A. Biochem. J. (1995) [Pubmed]
  12. Expression of components of the insulin-like growth factor system in pig mammary glands and serum during pregnancy and pseudopregnancy: effects of oestrogen. Lee, C.Y., Bazer, F.W., Simmen, F.A. J. Endocrinol. (1993) [Pubmed]
  13. Global quantitative phosphoprotein analysis using Multiplexed Proteomics technology. Steinberg, T.H., Agnew, B.J., Gee, K.R., Leung, W.Y., Goodman, T., Schulenberg, B., Hendrickson, J., Beechem, J.M., Haugland, R.P., Patton, W.F. Proteomics (2003) [Pubmed]
 
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