Comparative studies on creatine kinase isozymes from skeletal‐muscle and stomach of trout

Perriard, Jean‐Claude; Scholl, A.; Eppenberger, Hans M.

doi:10.1002/jez.1401820110

Cited by 28 publications

(10 citation statements)

References 19 publications

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“…This is not the first time that a heterogeneity of different creatine kinases has been found. It has been described in several reports on creatine kinases of various vertebrate species including human [28-301, rabbit [31,32] chick [33] and also trout [34,35]. As many separation techniques as studies have been carried out (starch gels, urea-starch gels, agarose gels, sodium dodecylsulphate/polyacrylamide gels and preparative isoelectric focusing) so that it is difficult to compare the different results with ours.…”

Section: Discussionmentioning

confidence: 91%

Occurrence of Heterogenous Forms of the Subunits of Creatine Kinase in Various Muscle and Nonmuscle Tissues and Their Behaviour during Myogenesis

Rosenberg

Eppenberger

Perriard

1981

European Journal of Biochemistry

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Purified, homodimeric creatine kinases from chicken were subjected to two-dimensional gel analysis under dissociating conditions. Each of the subunits M-creatine kinase and B-creatine kinase was resolved into a basic and an acidic subspecies with very similar mobilities in the sodium dodecylsulfate dimension. The M-creatine kinase subspecies were found in myogenic cells, fast muscle, slow muscle and the B-creatine kinase subspecies were present in heart, gizzard and brain. The creatine kinase subunits were identified in these tissues by a variety of methods like immunoreplicas of two-dimensional gels, immunoprecipitations, or coelectrophoresis with purified creatinc kinasc and all gave the same results. In the course of myogcnic development in vitro the subspecies were synthesized coordinately and no indication was found for a differential regulation of any of the subspecies of the creatine kinase subunits. No radioactive phosphorus was incorporated into either one of thc subspecies, hence phosphorylation could be ruled out as the source of heterogeneity. Furthermore, peptide mapping analysis of partial proteolytic digests did not reveal differences among the subspecies of the same subunit. Not only chicken but also rat creatine kinase displayed this type of heterogeneity. All subspecies were observed after translation of chicken RNA in a cell-free protein-synthesizing system. The heterogeneity probably might best be explained by the existence of multiple, but closely related genes for the creatine kinase subunits.Creatine kinase is a dimeric enzyme that plays a crucial role in the energy metabolism. It is especially characteristic of muscle tissue, but also occurs in other tissues [1,2]. The cytoplasmic nonmitochondrial enzymes are made up from two different kinds of subunits with a M , of 40000, the M-creatine kinase subunit and the B-creatine kinase subunit. MM-creatine kinase is found in appreciable amounts only in adult muscle, whereas BB-creatine kinase is more widely distributed in smooth muscle, chicken heart, brain and a variety of other tissues. During the differentiation of chicken myogenic cells in cultures as well as in embryonic muscle, an isoenzyme transition is observed from BB-creatine kinase to MM-creatine kinase, the form typical for the differentiated state. During this transition the subunits combine at random to yield homodimers and also active heterodimers MBcreatine kinase [3 -51. The subunits forming the active isoenzymes are very likely the products of at least two different genes as indicated by the differences of amino acid composition [6], the lack of immunological cross-reactivity [4,6,7] and differences in the metabolism of the corresponding mRNAs coding for thc two different subunits [S]. In addition M-creatine kinase is found in the M-line of adult skeletal myofibrils as well as in the myofibrils of cultured cells, suggesting a specific property of the MM-creatine kinase dimer whichAhhreviutions. M-creatine kinase and B-creatine kinase. subunit types of creatine kinase; MM-creati...

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Section: Discussionmentioning

confidence: 91%

Occurrence of Heterogenous Forms of the Subunits of Creatine Kinase in Various Muscle and Nonmuscle Tissues and Their Behaviour during Myogenesis

Rosenberg

Eppenberger

Perriard

1981

European Journal of Biochemistry

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“…USA 81 (1984) the brain (BB) isozyme in the electric organ has also been claimed (11). Furthermore, an additional species of CK exists in the trout (28). Two-dimensional gel electrophoresis unambiguously shows that the pCK-1 translation product comigrates with Torpedo muscle-specific CK subunit.…”

Section: Discussionmentioning

confidence: 99%

Complete nucleotide sequence of Torpedo marmorata mRNA coding for the 43,000-dalton nu 2 protein: muscle-specific creatine kinase.

Giraudat¹,

Devillers‐Thiéry²,

Perriard³

et al. 1984

Proc. Natl. Acad. Sci. U.S.A.

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DNA sequences coding for the muscle-specific subunit of creatine kinase have been isolated from cDNA libraries constructed from Torpedo marmorata electric organ. Clones were screened by differential in situ hybridization and hybrid-selected translation. The in vitro translation product of the selected mRNA was immunoprecipitated by anti-chicken creatine kinase antibodies and comigrated with Torpedo muscle creatine kinase on two-dimensional gels at the same position as the cytosolic 43,000-dalton protein referred to as v2. The cDNA inserts hybridized to a mRNA species present in adult Torpedo muscle but not in brain. The complete sequence of the mRNA was determined on one of the clones except for the 78 nucleotides of the mRNA 5' terminal sequence, which were identified by the primer extension method. The amino acid sequence of muscle-specific creatine kinase from T. marmorata was deduced and analyzed. It includes the known sequence of a peptide from the active site of rabbit muscle-specific creatine kinase.

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“…Osteoglossidae and Cyprinidae), and all of the advanced teleosts, the B2 isozyme was restricted to the eye and brain. Previous work on fish creatine kinase isozymes had also indicated that at least three CK loci are present in diploid species (Champion & Whirr, 1976;Eppenberger et al, 1971;Perriard et al, 1972;SchoU & Eppenberger, 1971;Whitt et al, 1977).…”

Section: Creatine Kinase Lsozyme Evolutionmentioning

confidence: 99%

Evolution of five multilocus isozyme systems in the chordates

et al. 1980

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Comparative studies on creatine kinase isozymes from skeletal‐muscle and stomach of trout

Cited by 28 publications

References 19 publications

Occurrence of Heterogenous Forms of the Subunits of Creatine Kinase in Various Muscle and Nonmuscle Tissues and Their Behaviour during Myogenesis

Occurrence of Heterogenous Forms of the Subunits of Creatine Kinase in Various Muscle and Nonmuscle Tissues and Their Behaviour during Myogenesis

Complete nucleotide sequence of Torpedo marmorata mRNA coding for the 43,000-dalton nu 2 protein: muscle-specific creatine kinase.

Evolution of five multilocus isozyme systems in the chordates

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