Disease relevance of CSN2

• The objectives of the study were to purify porcine beta-casein from sow's milk, to determine N-terminal amino acid sequence, to develop specific antisera against porcine beta-casein, and to use that antisera to evaluate milk samples from a mastitis study [1].

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

• Partial sequencing of the glycosylated beta-casein permitted the identification of glutamine residues 56, 79, 167, 175, and 194 as the primary sites of incorporation in amidinated casein with residues 54 and 182 as possible sites for partial glycosylation [7].
• In order to prevent epsilon-(gamma-glutamyl)lysine cross-link formation, the lysine residues of beta-casein were first blocked either by amidination with ethyl acetimidate or by acylation with succinic anhydride [7].
• Cyclic analogues of the beta-casein-derived opioid peptide beta-casomorphin-5 (H-Tyr-Pro-Phe-Pro-Gly-OH) were prepared through substitution of the Pro2 residue with various alpha,omega-diamino acid residues (lysine, ornithine, 2,4-diaminobutyric acid) and cyclization of the omega-amino group to the C-terminal carboxyl function [8].
• It encodes 250 amino acids protein containing the conserved sequence motif of beta-casein [9].

Anatomical context of CSN2

• Digestion by pancreatic juice of a beta-casomorphin-containing fragment of buffalo beta-casein [10].

Associations of CSN2 with chemical compounds

• In the presence of insulin, hydrocortisone, and PRL, beta-casein and WAP mRNA levels increased in all transgenic pigs [6].
• When purified eIF-5A was incubated with GPLTG or Factor XIIIa in the presence of succinylated beta-casein, a covalent complex was identified [11].
• Oestradiol administration increased beta-casein mRNA levels in pseudopregnant pigs, but had no effect on mammary IGFBP-2 and IGFBP-3 mRNA levels [12].
• It was determined by Western blot procedure that mammary inflammation induced by lipopolysaccharide infusion resulted in a 41% decrease in the beta-casein concentration of sow milk [1].
• Pro-Q Diamond dye technology can detect as little as 1-2 ng of beta-casein, a pentaphosphorylated protein, and 8 ng of pepsin, a monophosphorylated protein [13].

Analytical, diagnostic and therapeutic context of CSN2

• Antiserum collected from one rabbit 112 d after primary immunization detected 30 to 100 ng beta-casein by Western blot procedure when used at a dilution of 1:2 x 10(6) [1].
• Porcine beta-casein was then purified by liquid chromatography on a Mono Q anion-exchange column, and checked for purity with SDS-PAGE [1].
• Molecular cloning and phylogenetic analysis of canine beta-casein [9].
• A canine beta-casein cDNA was isolated from mammary tissue by polymerase chain reaction (PCR) using degenerate primers [9].

References