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Gene Review

CKM  -  creatine kinase, muscle

Gallus gallus

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High impact information on LOC396507

  • The tail, but not the head portion of M-CK is essential for the association of M-CK with the M-band of myofibrils [1].
  • Partial protein sequences of dog muscle (M) CK and brain (B) CK subunits were determined and compared with the derived amino acid sequence of the myocardial enzyme and of M CK subunits of other species [2].
  • Immunogold localization of muscle-type MM-CK on ultrathin cryosections of muscle, after removal of soluble CK, revealed relatively strong in situ labeling of M-CK remaining bound to the M band as well as to the SR membranes [3].
  • During the first 2 days of culture of myogenic chicken cells only minute amounts of mRNA for a subunit of creatine kinase, M-CK, could be found in cultures from the 3rd and 4th day; however, a dramatic increase of mRNA for the muscle-specific M-CK was observed [4].
  • Interestingly, in limb mesenchyme cultures, significant M-CK expression was detected during chondrogenesis (days 2-7), whereas hypertrophic cells expressed only B-CK [5].

Biological context of LOC396507


Anatomical context of LOC396507

  • 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 [5].
  • 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 [5].
  • In differentiated myogenic cells, the myotubes, both M-CK and B-CK subunits are synthesized [8].
  • A competition e.l.i.s.a. (enzyme-linked immunosorbent assay) is described that enables direct measurement of the muscle-specific polypeptide of chick creatine kinase (M-CK) in extracts of differentiating muscle-cell cultures and in blood plasma samples, even in the presence of embryonic, or brain-type, creatine kinase [9].
  • The rates of degradation of creatine kinase subunits, M-CK and B-CK subunits, were measured in cultured myogenic cells and in subcultured fibroblasts [8].

Associations of LOC396507 with chemical compounds

  • The assay was shown to be reproducible and gave a linear response with increasing amounts of RNA, allowing relative quantitation of mRNA in polysomal RNA for the creatine kinases M and B. MRNA for M-CK was detected in polusomal RAN and total cellular RNA from myogenic cells [10].
  • Myofibrillar binding is mediated by major and minor lysine charge clamp motifs (K104/K115 [major] and K8/K24 [minor] in chicken M-CK) located in the N-terminal region [J. Cell Biol. 149 (2000) 1225] [11].
  • The localization of M-CK at the I-band coincided with that of adenylate kinase and aldolase [12].

Analytical, diagnostic and therapeutic context of LOC396507

  • E.l.i.s.a. measurements on 17-20-day embryonic thigh-muscle extracts, which contain almost exclusively M-CK, agree well with enzyme activity and radioimmunoassay [9].
  • 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 [13].


  1. Intracellular targeting of isoproteins in muscle cytoarchitecture. Schäfer, B.W., Perriard, J.C. J. Cell Biol. (1988) [Pubmed]
  2. Complete nucleotide sequence of dog heart creatine kinase mRNA: conservation of amino acid sequence within and among species. Roman, D., Billadello, J., Gordon, J., Grace, A., Sobel, B., Strauss, A. Proc. Natl. Acad. Sci. U.S.A. (1985) [Pubmed]
  3. Muscle-type MM creatine kinase is specifically bound to sarcoplasmic reticulum and can support Ca2+ uptake and regulate local ATP/ADP ratios. Rossi, A.M., Eppenberger, H.M., Volpe, P., Cotrufo, R., Wallimann, T. J. Biol. Chem. (1990) [Pubmed]
  4. 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]
  5. 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]
  6. Different E-box regulatory sequences are functionally distinct when placed within the context of the troponin I enhancer. Yutzey, K.E., Konieczny, S.F. Nucleic Acids Res. (1992) [Pubmed]
  7. 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]
  8. Turnover of the creatine kinase subunits in chicken myogenic cell cultures and in fibroblasts. Caravatti, M., Perriard, J.C. Biochem. J. (1981) [Pubmed]
  9. Immunoassay of muscle-specific creatine kinase with a monoclonal antibody and application to myogenesis and muscular dystrophy. Morris, G.E., Head, L.P. Biochem. J. (1983) [Pubmed]
  10. 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]
  11. Elements of the major myofibrillar binding peptide motif are present in the earliest of true muscle type creatine kinases. Uda, K., Suzuki, T., Ellington, W.R. Int. J. Biochem. Cell Biol. (2004) [Pubmed]
  12. In situ compartmentation of creatine kinase in intact sarcomeric muscle: the acto-myosin overlap zone as a molecular sieve. Wegmann, G., Zanolla, E., Eppenberger, H.M., Wallimann, T. J. Muscle Res. Cell. Motil. (1992) [Pubmed]
  13. 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]
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