Quantitation of creatine kinase isoenzyme transitions in differentiating chicken embryonic breast muscle and myogenic cell cultures by immunoadsorption

Perriard, Jean‐Claude; Caravatti, M; Perriard, Evelyne; Eppenberger, Hans M.

doi:10.1016/0003-9861(78)90070-x

Cited by 72 publications

(38 citation statements)

References 25 publications

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“…Therefore, untreated lysates had to be used for cotranslational phosphorylation and incorporation of 32P yielded only very faint signals due to the high endogenous phosphate pools. Incubation was followed by immunoprecipitation [23,27] and extensive washing before preparation of the samples for 2D gel analysis.…”

Section: Cotranslational Phosphotylation Assaysmentioning

confidence: 99%

Phosphorylation of chicken brain‐type creatine kinase affects a physiologically important kinetic parameter and gives rise to protein microheterogeneity in vivo

Quest¹,

Soldati²,

Hemmer³

et al. 1990

FEBS Letters

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Section: Cotranslational Phosphotylation Assaysmentioning

confidence: 99%

Phosphorylation of chicken brain‐type creatine kinase affects a physiologically important kinetic parameter and gives rise to protein microheterogeneity in vivo

Quest¹,

Soldati²,

Hemmer³

et al. 1990

FEBS Letters

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“…Heart cells derived from 8-10-d-old chicken embryos were cultured for 48-96 hours and subjected to double-immunofluorescence staining using monoclonal antibody B4 against the M-band protein myomesin (21,22) and polyclonal antibody against chicken nonmuscle specific BB-CK or the skeletal muscle-specific MM-CK (40). The results are shown in Fig.…”

Section: Chicken Heart Cells Do Not Express Mm-ckmentioning

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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“…Selected plasmid DNA (5)(6)(7)(8)(9)(10) gg) was linearized by digestion with EcoRI and bound to 1-cm2 membrane pieces (Gene-Screen) (25) …”

Section: Methodsmentioning

confidence: 99%

“…In the course of differentiation, these proteins replace the cytoplasmic contractile isoproteins, which are expressed in nonmuscle cells and in the nonterminally differentiated myogenic progenitor cells. Hence, isoprotein "switches" occur in differentiating myogenic cells and have been described for some contractile proteins (1, 2) as well as for enzymes such as creatine kinase (CK) (3)(4)(5) that have an important role in energy metabolism in muscle.…”

mentioning

confidence: 99%

“…In early stages of differentiation of cultured-myogenic cells as well as in embryonic muscle, BB-CK is accumulated but, as differentiation reaches its terminal phases, isoenzymes containing the muscle-specific CK subunit (M-CK) progressively appear (3)(4)(5) until, in adult muscle, the latter subunit replaces the type B CK subunit (B-CK) previously present (5). In an early transitory phase of terminal differentiation the synthesis of B-CK is enhanced and the synthesis of M-CK is initiated; finally differentiated cells that synthesize predominantly M-CK and only traces of B-CK are produced (6).…”

mentioning

confidence: 99%

See 1 more Smart Citation

Molecular cloning and expression during myogenesis of sequences coding for M-creatine kinase.

Rosenberg¹,

Kunz²,

Frischauf³

et al. 1982

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

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Sequences complementary to muscle poly(A)+RNA were cloned in the plasmid pBR322 and the resulting colonies were screened by colony hybridization with labeled cDNA derived from skeletal muscle and smooth muscle (gizzard). The skeletal musclespecific clones were further screened by RNA blotting hybridization for a muscle mRNA having the size expected for a putative type M creatine kinase (M-CK) mRNA. The remaining clones with the expected hybridization properties were finally characterized by hybrid-selected translation, and a cloned sequence was shown to contain DNA hybridizing to mRNA that could be translated into M-CK. This plasmid, pMCKI, was further characterized by restriction mapping. Blot analysis of total cell RNA from differentiating myogenic cell cultures showed accumulation of M-CK mRNA in cultures older than 42 hr but not in young little-differentiated cultures.During the development of myogenic cells, mononucleated cells fuse to form myotubes which become contractile at the time when well-organized myofibrils, the characteristic organelles of cross-striated muscle, appear in the cytoplasm of fully differentiated cells. The myofibrils are composed of a set of myofibrillar contractile proteins that are produced only in terminally differentiated muscle cells. In the course of differentiation, these proteins replace the cytoplasmic contractile isoproteins, which are expressed in nonmuscle cells and in the nonterminally differentiated myogenic progenitor cells. Hence, isoprotein "switches" occur in differentiating myogenic cells and have been described for some contractile proteins (1, 2) as well as for enzymes such as creatine kinase (CK) (3-5) that have an important role in energy metabolism in muscle.In early stages of differentiation of cultured-myogenic cells as well as in embryonic muscle, BB-CK is accumulated but, as differentiation reaches its terminal phases, isoenzymes containing the muscle-specific CK subunit (M-CK) progressively appear (3-5) until, in adult muscle, the latter subunit replaces the type B CK subunit (B-CK) previously present (5). In (Feldbach, Switzerland), and "Gene-Screen" membranes were obtained from New England Nuclear (Dreieich,

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Quantitation of creatine kinase isoenzyme transitions in differentiating chicken embryonic breast muscle and myogenic cell cultures by immunoadsorption

Cited by 72 publications

References 25 publications

Phosphorylation of chicken brain‐type creatine kinase affects a physiologically important kinetic parameter and gives rise to protein microheterogeneity in vivo

Phosphorylation of chicken brain‐type creatine kinase affects a physiologically important kinetic parameter and gives rise to protein microheterogeneity in vivo

Intracellular targeting of isoproteins in muscle cytoarchitecture.

Molecular cloning and expression during myogenesis of sequences coding for M-creatine kinase.

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