High impact information on CSN2

• The DNA binding activity of MGF is hormonally regulated and essential for beta-casein promoter activity [1].
• Prolactin-dependent transactivation of a beta-casein promoter-luciferase reporter gene construct was observed in transfected cells [1].
• The derived 216 amino acid sequence of rat beta-casein was compared to the previously determined sequences of beta-caseins from several other species [2].
• The complete sequence of a 1072 nucleotide rat beta-casein cDNA insertion in the hybrid plasmid pC beta 23 has been determined [2].
• Total polysomal RNA or poly A- containing RNA extracted from free polysomes of lactating ewe mammary gland was unable to direct a significant synthesis of alpha-s- and beta-casein [3].

Biological context of CSN2

• In particular, three single-nucleotide polymorphisms (SNP) are described at CSN1S1, CSN2, and CSN3, all resulting in amino acid exchanges [4].
• Complete nucleotide sequence of ovine beta-casein cDNA: inter-species comparison [5].
• The deduced amino acid sequence differs at 3 positions from that previously determined by direct sequencing of mature beta-casein [5].
• The complete nucleotide sequence of ovine beta-casein mRNA has been determined by sequencing, according to Sanger-Messing, both a recombinant clone isolated from a mammary cDNA pUC 18 library and a single-stranded cDNA generated by reverse transcription from a synthetic 17-mer primer complementary to the 5' part of the mRNA coding frame [5].
• A region located between positions -221 and -170 of the rat beta-casein promoter contains overlapping binding sites for DNA binding factors with positive and negative regulatory activity [6].

Anatomical context of CSN2

• Purification of the mRNAs for Ewe alphaS-casein and beta-casein by immunoprecipitation of polysomes [7].
• In response to mitogenic stimulation, the proliferative response of both T and B lymphocytes was significantly enhanced by beta-casein [8].
• Additionally, pre-beta-casein was post-translationally converted into authentic beta-casein by a specific proteinase(s) extracted from rough microsomes with Na deoxycholate [9].
• When mammary mRNAs were translated in a wheat germ cell-free system in the presence of mammary microsomal membranes, pre-beta-casein was converted into authentic beta-casein as demonstrated by amino terminal sequence analyses [9].

Associations of CSN2 with chemical compounds

• Finally, it was observed that beta-casein from caprine and ovine caseinates was degraded by O. ficus-indica faster than its alpha(S) counterpart, but the reverse was observed for bovine caseinate [10].
• The probe pTZ-E4 was a fragment of the ovine beta-casein gene inserted in the plasmid pTZ18R and labeled with biotin-11-dUTP [11].
• Pectic acid administered orally to mature virgin rats induced the accumulation of beta-casein in mammary gland [12].

Other interactions of CSN2

• Genetic variants A and D of bovine alpha s2-casein, beta-casein variants A1, A2, A3, B and C and alpha s1-casein variants B and C were determined by CE [13].
• During the last third of pregnancy, the expression of beta-lactoglobulin gene is significantly more elevated than that of alpha s1- or beta-casein whose mRNA levels were found to change very slightly during this period [14].
• Ovine placental lactogen was very efficient in provoking the accumulation of beta-casein mRNA in rabbit mammary explants but was much less active on ewe mammary explants [15].

Analytical, diagnostic and therapeutic context of CSN2

• Electrophoretic mobility shift assays using the specific anti-Stat5a1 antisera demonstrated that Stat5a1 comprises part of the heterogeneous, PRL-inducible, protein-DNA complex associated with the beta-casein GAS site [16].
• Chromosomal localization of the ovine beta-casein gene by non-isotopic in situ hybridization and R-banding [11].
• Immunoblotting, however, allowed antibodies to beta-casein to be identified and compared with available monoclonal antibodies [17].
• After four days of treatment, beta-casein estimated by a radioimmunoassay was present in the mammary glands of the rats to which beer or barley extracts were given [18].

References