Differentiation in cultures derived from embryonic chicken muscle

Turner, David C.; Gmür, Rudolf; Siegrist, Marianne; Burckhardt, Elisabeth; Eppenberger, Hans M.

doi:10.1016/0012-1606(76)90090-7

Cited by 74 publications

(7 citation statements)

References 47 publications

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“…Similarly, it was found that the appea'rance of AChR and CPK in fetal calf muscle,cultures are coupled and furthermore that their elaboration did not depend on cell fusion [10]. The recent reports [6][7][8]11,12], that cytoplasmic proteins accumulated in fusion-arrested chicken myoblasts, further support the conclusion that cell fusion is not a prerequisite forPthese manifestations of skeletal muscle differentiation. On the other hand, close association between cell fusion and the synthesis of muscle specific proteins in rat cultures was claimed [ 19 ].…”

Section: Discussionsupporting

confidence: 55%

“…The correlation between cell fusion and the appearance of muscle-specific proteins has led some authors to hypothesize that the fusion process might be a prerequisite for the protein formation [1][2][3]. Recently, however, some authors have suggested that myogenesis, as manifested by the appearance of muscle proteins, is independent of the cell fusion process [4][5][6][7][8][9][10][11][12][13].…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

The appearance of acetylcholine receptors triggered by fusion of myoblasts in vitro

Shainberg

Brik

1978

FEBS Letters

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Section: Discussionsupporting

confidence: 55%

Section: Introductionmentioning

confidence: 99%

The appearance of acetylcholine receptors triggered by fusion of myoblasts in vitro

Shainberg

Brik

1978

FEBS Letters

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“…The enzyme is a dimer of two subunits which exist as a nonskeletal muscle form, brain creatine kinase (BB-CK), in embryonic muscle and in nonmuscle cells like brain. Upon muscle differentiation the synthesis of the M-CK subunit is induced and BB-CK is gradually replaced by the skeletal muscle-specific enzyme MM-CK (8,14,40,41,51). Although myofibers that differentiate in culture have been shown to contain all three isoenzymes, MM-CK, MB-CK and BB-CK (40,51) only MM-CK appears to be localized and specifically bound to the M-band of the myofibril (53).…”

mentioning

confidence: 99%

Intracellular targeting of isoproteins in muscle cytoarchitecture.

Schäfer

Perriard

1988

The Journal of Cell Biology

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Abstract. Part of the muscle creatine kinase (MM-CK) in skeletal muscle of chicken is localized in the M-band of myofibrils, while chicken heart cells containing myofibrils and BB-CK, but not expressing MM-CK, do not show this association. The specificity of the MM-CK interaction was tested using cultured chicken heart cells as "living test tubes" by microinjection of in vitro generated MM-CK and hybrid M-CK/B-CK mRNA with SP6 RNA polymerase. The resulting translation products were detected in injected cells with isoprotein-specific antibodies. 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. The tail, but not the head portion of M-CK is essential for the association of M-CK with the M-band of myofibrils. We conclude that gross biochemical properties do not always coincide with a molecule's specific functions like the participation in cell cytoarchitecture which may depend on molecular targeting even within the same cellular compartment. IN most cells of higher organisms isoforms, representing closely related proteins with conserved amino acid sequences and often similar functional properties are the products of multigene families. Distinct isoforms may exist as related proteins in different tissues, be developmentally regulated within a single tissue or even coexist within a single cytoplasmic compartment. In part divergence in protein sequence among isoforms may serve to target a given isoprotein to its appropriate compartment within the cell. Specific sequences, often located at the amino terminus, have been found to be responsible for the extracellular export of many secretory proteins (5) or the intracellular targeting of proteins destined for intracellular compartments like mitochondria, chloroplasts or the nucleus (11,17,26).Here we examine the molecular basis for the localization of muscle creatine kinase (MM-CK) ~ within the M-band of the muscle myofibril (50,54,55,56). Creatine kinase is the major enzyme ensuring energy production in the muscle cell. The enzyme is a dimer of two subunits which exist as a nonskeletal muscle form, brain creatine kinase (BB-CK), in embryonic muscle and in nonmuscle cells like brain. Upon muscle differentiation the synthesis of the M-CK subunit is induced and BB-CK is gradually replaced by the skeletal muscle-specific enzyme 14,40,41,51). Although myofibers that differentiate in culture have been shown to contain all three isoenzymes, MM-CK, MB-CK and BB-CK (40, 51) only MM-CK appears to be localized Beat W. Sch~ifer's present address is Department of Pharmacology, Stanford University, Stanford, CA 94305. Abbreviations used in this paper:B-CK, creatine kinase subunit; BB-CK, brain creatine kinase; CMF, calcium-and magnesium-free; MB-CK heterodimeric creatine kinase; M-CK, creatine kinase subunit; MM-CK, muscle creatine kinase. and specifically bound to the M-band of the myofibril (53). This result can be explained in two ways. ...

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“…It is not surprising that our monoclonal antibody did not cross-react with chick BB-CK, since the two isoenzymes differ considerably in amino acid composition and polyclonal rabbit antisera against the two isoenzymes do not cross-react with each other (4,5,13]. The lack of cross-reaction with rabbit CK is rather less predictable, since amino acid differences between species are generally less than between MM and BB [14].…”

Section: Discussionmentioning

confidence: 99%

“…Immunological assays of CK can be made specific for any one of the CK isoenzymes and polyclonal rabbit antisera have been used for the study of muscle-specific CK (MM-CK) accumulation and distribution in differentiating myoblast cultures [4,5]. A monoclonal antibody (McAb) for these assays would have the added advantages of providing an unlimited supply of antibody with defined properties which can be selected for during McAb preparation.…”

Section: Introductionmentioning

confidence: 99%