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CALB1  -  calbindin 1, 28kDa

Bos taurus

 
 
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High impact information on MGC138959

  • The effects of Ca(2+) binding on the side-chain methyl dynamics of calbindin D(9k) have been characterized by (2)H NMR relaxation rate measurements [1].
  • Calbindin D(9k) is a dicalcium binding protein consisting of two helix-loop-helix EF-hand motifs joined together by a flexible linker region where one metal ion can bind to each of the two loops [2].
  • Two calbindin D(9k) mutants, (Q22E+P43M) and (Q22N+P43M), were constructed to examine the interaction between Gln 22 and the water molecule in the C-terminal calcium binding site II [3].
  • In 1,25(OH)2D3 treated cells, calbindin D-28K was enhanced in cytosol and was detected within the nucleus [4].
  • Here we describe the measurement and modeling of pK(a) values for all aspartic and glutamic acid residues in apo calbindin D(9k), a representative of calmodulin-related proteins [5].
 

Biological context of MGC138959

 

Anatomical context of MGC138959

 

Associations of MGC138959 with chemical compounds

  • The ionization state of seven glutamate residues, one aspartate, and the C-terminal alpha-COOH group in bovine apo calbindin D(9k) has been studied by measurement and modeling of the pH titration curves and apparent pK(a) values [9].
  • According to X-ray crystallographic data the OH group of the single tyrosine of calbindin (Tyr-13) is hydrogen-bonded to the carboxyl group of Glu-35, thus linking the two alpha helices flanking the N-terminal Ca2+ site [10].
  • We previously reported that 24 h treatment with 1 alpha, 25-dihydroxyvitamin D3 (1,25-D3), the active form of vitamin D3, induces calbindin-D28K and activates protein kinase C (PKC) in MDBK (Madin-Darby bovine kidney) cells [7].
 

Other interactions of MGC138959

  • The expression of calbindin-D9K (CaBP9K) and calbindin-D28K (CaBP28K) genes in the reproductive system is well established for rodent and avian species, but not for domestic livestock [11].
  • The enhancement of calbindin-D28K expression is preceded by activation and translocation of PKC alpha [7].
 

Analytical, diagnostic and therapeutic context of MGC138959

References

  1. Effects of calcium binding on the side-chain methyl dynamics of calbindin D9k: a 2H NMR relaxation study. Johnson, E., Chazin, W.J., Rance, M. J. Mol. Biol. (2006) [Pubmed]
  2. A 15N NMR mobility study on the dicalcium P43M calbindin D9k and its mono-La3+-substituted form. Bertini, I., Carrano, C.J., Luchinat, C., Piccioli, M., Poggi, L. Biochemistry (2002) [Pubmed]
  3. Symmetrical stabilization of bound Ca2+ ions in a cooperative pair of EF-hands through hydrogen bonding of coordinating water molecules in calbindin D(9k). Fast, J., Håkansson, M., Muranyi, A., Gippert, G.P., Thulin, E., Evenäs, J., Svensson, L.A., Linse, S. Biochemistry (2001) [Pubmed]
  4. Induction of calbindin D-28K in Madin-Darby bovine kidney cells by 1,25(OH)2D3. Gagnon, A.M., Simboli-Campbell, M., Welsh, J.E. Kidney Int. (1994) [Pubmed]
  5. Focusing of the electrostatic potential at EF-hands of calbindin D(9k): titration of acidic residues. Kesvatera, T., Jönsson, B., Thulin, E., Linse, S. Proteins (2001) [Pubmed]
  6. Kinetics of calcium binding to calbindin mutants. Forsén, S., Linse, S., Thulin, E., Lindegård, B., Martin, S.R., Bayley, P.M., Brodin, P., Grundström, T. Eur. J. Biochem. (1988) [Pubmed]
  7. Modulation and phosphorylation of calbindin-D28K correlates with protein kinase C activation1. Gagnon, A., Welsh, J. Biochem. Cell Biol. (1997) [Pubmed]
  8. Identification and primary structure of a calbindin 9K binding domain in the plasma membrane Ca2+ pump. James, P., Vorherr, T., Thulin, E., Forsen, S., Carafoli, E. FEBS Lett. (1991) [Pubmed]
  9. Ionization behavior of acidic residues in calbindin D(9k). Kesvatera, T., Jönsson, B., Thulin, E., Linse, S. Proteins (1999) [Pubmed]
  10. Effect of amino acid substitutions and deletions on the thermal stability, the pH stability and unfolding by urea of bovine calbindin D9k. Wendt, B., Hofmann, T., Martin, S.R., Bayley, P., Brodin, P., Grundström, T., Thulin, E., Linse, S., Forsén, S. Eur. J. Biochem. (1988) [Pubmed]
  11. CaBP9K levels during the luteal and follicular phases of the estrous cycle in the bovine uterus. Inpanbutr, N., Miller, E.K., Petroff, B.K., Iacopino, A.M. Biol. Reprod. (1994) [Pubmed]
 
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