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Gene Review

CKB  -  creatine kinase, brain

Gallus gallus

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Disease relevance of CKB

  • At early stages of development (days 2-5), B-CK was more or less evenly distributed over the entire retina with the exception of ganglion cells, which were stained more strongly for B-CK than other retinal precursor cells [1].

High impact information on CKB

  • M-CK molecules and translation products of chimeric cDNA molecules containing the head half of the B-CK and the tail half of the M-CK coding regions were localized in the M-band of the myofibrils [2].
  • In the case of purified acetylcholine receptor-rich membranes, antibodies specific for chicken B-CK label only one face of the isolated vesicles [3].
  • In the chicken, a high degree of heterogeneity at the protein level has been reported for the creatine kinase-type B (B-CK) [4].
  • The transcription of the single hnRNA is directed by a complex promoter region containing a stretch of sequences which is highly conserved among all the B-CK genes known to date [4].
  • Here we show that the two B-CK isoproteins, Ba- and Bb-CK, are encoded by two mRNAs, which are derived from a single copy gene by a stochastic alternative splicing mechanism [4].

Biological context of CKB

  • cDNA clones for chicken B-CK were isolated by immunoscreening from a gizzard cDNA library constructed in the expression vector lambda gtll [5].
  • COM184: a polymorphic microsatellite marker for CKB on chicken chromosome 5 [6].
  • Interestingly, in limb mesenchyme cultures, significant M-CK expression was detected during chondrogenesis (days 2-7), whereas hypertrophic cells expressed only B-CK [7].
  • Quantitation of the CK activity peak ratios of these two populations revealed the existence of a tissue-specific, post-translational mechanism regulating B-CK dimerization in neural tissues [8].
  • Phosphorylation of Bb to yield Bb* is concluded to reduce the Km of B-CK dimers for CP by about 50% [9].

Anatomical context of CKB

  • The B-CK cDNA hybridizes specifically to a 1.6-kb mRNA found in brain and gizzard but not in adult skeletal muscle tissue [10].
  • The presence of mRNA coding for creatine kinase M (Mck) and creatine kinase B (B-CK) in RNA from myogenic and fibrogenic cell cultures, embryonic muscle, and embryonic brain tissue was demonstrated by "in vitro" translation in a heterologous cell-free protein-synthesizing system from rabbit reticulocytes [11].
  • In tibial chondrocytes, an increase in B-CK expression was seen when the cells became hypertrophic [7].
  • B-CK and Mib-CK were localized along the entire sperm tail and in the mitochondria-rich midpiece, respectively [12].
  • In the growth plate, B-CK expression was highest in the most calcified regions, and M-CK was less abundant than B-CK in all regions of the growth plate [7].

Associations of CKB with chemical compounds

  • In RNA from cells grown in 5-bromo-2'-deoxyuridine (BrdUrd) for 3 days and subcultured into the same medium for another 3 days only mRNA for B-CK was found [13].
  • Expression of B-CK increased slightly over 15 days in mineralizing, retinoic acid-treated cephalic chondrocytes, but it decreased in nonmineralizing caudal chondrocytes, while there was little expression of M-CK [7].
  • In addition to the two monomer subunits of chicken brain-type creatine kinase (B-CK, EC,, termed Bb (basic) and Ba (acidic), another subspecies called Bb* was identified by chromatofocussing in the presence of 8 M urea (Quest et al., ) [9].
  • B-CK was phosphorylated after treating the cultures with 1-oleoyl-2-acetyl-sn-glycerol, dibutyryl-cAMP, okadiac acid and combinations thereof, but not with 1,2-dioleoyl-sn-glycerol [14].

Analytical, diagnostic and therapeutic context of CKB

  • Isolated chicken B-CK can be resolved by two-dimensional gel electrophoresis into a major acidic Ba-CK and a major basic Bb-CK protein species which are very likely produced from the unique chicken B-CK gene (Wirz, T., Hossle, J [15].
  • Proteolytically modified M-CK and B-CK subunits were able to refold and reassociate into dimeric structures after treatment with high concentrations of LiCl and at low pH [16].
  • The two subunits were shown by peptide mapping, amino acid analysis and partial sequencing, as well as by immunological criteria, to be distinct B-CK polypeptides [8].
  • These intestinal epithelial cell creatine kinases were indistinguishable from the cytoplasmic (B-CK) and mitochondrial (Mi-CK) creatine kinase isozymes of brain when compared by SDS-PAGE, cellulose polyacetate electrophoresis, and peptide mapping [17].
  • The expression and the cellular- as well as subcellular-distribution of brain-type B-CK and mitochondrial Mi-CK during development of the chicken retina was studied by immunoblotting, immunofluorescence and immunogold methods [1].


  1. Differential expression and localization of brain-type and mitochondrial creatine kinase isoenzymes during development of the chicken retina: Mi-CK as a marker for differentiation of photoreceptor cells. Wegmann, G., Huber, R., Zanolla, E., Eppenberger, H.M., Wallimann, T. Differentiation (1991) [Pubmed]
  2. Intracellular targeting of isoproteins in muscle cytoarchitecture. Schäfer, B.W., Perriard, J.C. J. Cell Biol. (1988) [Pubmed]
  3. Subcellular localization of creatine kinase in Torpedo electrocytes: association with acetylcholine receptor-rich membranes. Wallimann, T., Walzthöny, D., Wegmann, G., Moser, H., Eppenberger, H.M., Barrantes, F.J. J. Cell Biol. (1985) [Pubmed]
  4. A unique chicken B-creatine kinase gene gives rise to two B-creatine kinase isoproteins with distinct N termini by alternative splicing. Wirz, T., Brändle, U., Soldati, T., Hossle, J.P., Perriard, J.C. J. Biol. Chem. (1990) [Pubmed]
  5. The primary structure of chicken B-creatine kinase and evidence for heterogeneity of its mRNA. Hossle, J.P., Rosenberg, U.B., Schäfer, B., Eppenberger, H.M., Perriard, J.C. Nucleic Acids Res. (1986) [Pubmed]
  6. COM184: a polymorphic microsatellite marker for CKB on chicken chromosome 5. Clendenning, M., Bumstead, N. Anim. Genet. (2001) [Pubmed]
  7. Developmental expression of creatine kinase isoenzymes in chicken growth cartilage. Hobson, G.M., Funanage, V.L., Elsemore, J., Yagami, M., Rajpurohit, R., Perriard, J.C., Hickok, N.J., Shapiro, I.M., Tuan, R.S. J. Bone Miner. Res. (1999) [Pubmed]
  8. Two different B-type creatine kinase subunits dimerize in a tissue-specific manner. Quest, A.F., Eppenberger, H.M., Wallimann, T. FEBS Lett. (1990) [Pubmed]
  9. Phosphorylation of chicken brain-type creatine kinase affects a physiologically important kinetic parameter and gives rise to protein microheterogeneity in vivo. Quest, A.F., Soldati, T., Hemmer, W., Perriard, J.C., Eppenberger, H.M., Wallimann, T. FEBS Lett. (1990) [Pubmed]
  10. Accumulation of creatine kinase mRNA during myogenesis: molecular cloning of a B-creatine kinase cDNA. Kwiatkowski, R.W., Ehrismann, R., Schweinfest, C.W., Dottin, R.P. Dev. Biol. (1985) [Pubmed]
  11. Detection and relative quantitation of mRNA for creatine kinase isoenzymes in mRNA from myogenic cell cultures and embryonic chicken tissues. Perriard, J.C., Perriard, E.R., Eppenberger, H.M. J. Biol. Chem. (1978) [Pubmed]
  12. Identification of two distinctly localized mitochondrial creatine kinase isoenzymes in spermatozoa. Kaldis, P., Stolz, M., Wyss, M., Zanolla, E., Rothen-Rutishauser, B., Vorherr, T., Wallimann, T. J. Cell. Sci. (1996) [Pubmed]
  13. Developmental regulation of creatine kinase isoenzymes in myogenic cell cultures from chicken. Levels of mRNA for creatine kinase subunits M and B. Perriard, J.C. J. Biol. Chem. (1979) [Pubmed]
  14. Effect of okadaic acid on protein phosphorylation patterns of chicken myogenic cells with special reference to creatine kinase. Hemmer, W., Skarli, M., Perriard, J.C., Wallimann, T. FEBS Lett. (1993) [Pubmed]
  15. Alternative ribosomal initiation gives rise to chicken brain-type creatine kinase isoproteins with heterogeneous amino termini. Soldati, T., Schäfer, B.W., Perriard, J.C. J. Biol. Chem. (1990) [Pubmed]
  16. Specific proteolytic modification of creatine kinase isoenzymes. Implication of C-terminal involvement in enzymic activity but not in subunit-subunit recognition. Lebherz, H.G., Burke, T., Shackelford, J.E., Strickler, J.E., Wilson, K.J. Biochem. J. (1986) [Pubmed]
  17. Discrete subcellular localization of a cytoplasmic and a mitochondrial isozyme of creatine kinase in intestinal epithelial cells. Keller, T.C., Gordon, P.V. Cell Motil. Cytoskeleton (1991) [Pubmed]
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