Ultrastructure studies on the binding of creatine kinase and the 165,000 molecular weight component to the M-band of muscle

Herasymowych, O.Sonia; Mani, Rajam S.; Kay, Cyril M.; Bradley, R.; Scraba, Douglas G.

doi:10.1016/0022-2836(80)90313-7

Cited by 18 publications

(3 citation statements)

References 11 publications

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“…The MM-CK bound to the M-band was removed by incubation at low ionic strength [1,30,31] and could be slowly replaced by external fluorescent CK. These results are in agreement with observations obtained by electron microscopy of beef heart and rabbit muscle [35] and by measuring rebound CK activity on rat heart [36]. The observation of such a slow exchange supports the hypothesis put forward by Arrio-Dupont et al [27] to explain the presence of a very slightly mobile CK fraction in cultured muscle cells.…”

Section: M-ck Bound To the M-band Of Rabbit Psoas Myofibrils Is Exchangeablesupporting

confidence: 92%

Presence of enolase in the M-band of skeletal muscle and possible indirect interaction with the cytosolic muscle isoform of creatine kinase

FOUCAULT¹,

VACHER²,

Меркулова³

et al. 1999

Biochem. J.

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Glycerol-skinned skeletal muscle fibres retain the defined sarcomeric structure of the myofibrils. We show here that a small fraction of two enzymes important for energy metabolism, the cytosolic muscle isoform of creatine kinase (EC 2.7.3.2), MM-creatine kinase (MM-CK), and enolase (EC 4.2.1.11), remains bound to skinned fibres. CK is slowly exchangeable, whereas enolase is firmly bound. Two-dimensional gel electrophoresis followed by Western blot analyses demonstrates that both alpha (ubiquitous) and beta (muscle-specific) subunits of enolase are present in these preparations. Enolase and CK were co-localized at the M-band of the sarcomeres, as observed by indirect immunofluorescence and confocal microscopy. Cross-linking experiments were performed on skinned fibres with three bifunctional succinimidyl esters of different lengths and yielded a protein complex of 150 kDa that reacted with antibodies directed against either M-CK or beta-enolase. The cross-linking efficiency was greatest for the longest reagent and zero for the shortest one. The length of the cross-linker giving a covalent complex between the two enzymes does not support the notion of a direct interaction between M-CK and enolase. This is the first demonstration of the presence of an enzyme of energy metabolism other than CK at the M-band of myofibres.

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Section: M-ck Bound To the M-band Of Rabbit Psoas Myofibrils Is Exchangeablesupporting

confidence: 92%

Presence of enolase in the M-band of skeletal muscle and possible indirect interaction with the cytosolic muscle isoform of creatine kinase

FOUCAULT¹,

VACHER²,

Меркулова³

et al. 1999

Biochem. J.

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“…The main component of M-bridges is MM-creatine kinase (Strehler et al, 1983 and references therein). Two other M-line proteins, 165,000-mol-wt M-protein and 185,000-molwt myomesin (Grove et al, 1984(Grove et al, , 1985 are closely associated with the bare zone of myosin filaments (Herasymowych et al, 1980;Bahler et al, 1985) and can be considered integral M-disc proteins. It is not known what structures are formed by myomesin and M-protein, but it seems unlikely that they contribute to the M-bridges (Bahler et al, 1985).…”

Section: Structure Of the M-discmentioning

confidence: 99%

Skelemins: cytoskeletal proteins located at the periphery of M-discs in mammalian striated muscle.

Price¹

1987

The Journal of Cell Biology

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Abstract. The cytoskeletons of mammalian striated and smooth muscles contain a pair of high molecular weight (HMW) polypeptides of 220,000 and 200,000 mol wt, each with isoelectric points of about 5 (Price, M. G., 1984, Am. J. PhysioL, 246:H566-572) in a molar ratio of 1:1:20 with desmin. The HMW polypeptides of mammalian muscle have been named "skelemins," because they are in the insoluble cytoskeletons of striated muscle and are at the M-discs. I have used two-dimensional peptide mapping to show that the two skelemin polypeptides are closely related to each another. Polyclonal antibodies directed against skelemins were used to demonstrate that they are immunologically distinct from talin, fodrin, myosin heavy chain, synemin, microtubule-associated proteins, and numerous other proteins of similar molecular weight, and are not oligomers of other muscle proteins. Skelemins appear not to be proteolytic products of larger proteins, as shown by immunoautoradiography on 3 % polyacrylamide gels. Skelemins are predominately cytoskeletal, with little extractable from myofibrils by various salt solutions. Human, bovine, and rat cardiac, skeletal, and smooth muscles, but not chicken muscles, contain proteins cross-reacting with anti-skelemin antibodies. Skelemins are localized by immunofluorescence at the M-lines of cardiac and skeletal muscle, in 0.4-1xm-wide smooth striations. Cross sections reveal that skelemins are located at the periphery of the M-discs. Skelemins are seen in threads linking isolated myofibrils at the M-discs. There is sufficient skelemin in striated muscle to wrap around the M-disc about three times, if the skelemin molecules are laid end to end, assuming a length-to-weight ratio similar to M-line protein and other elongated proteins. The results indicate that skelemins form linked rings around the periphery of the myofibrillar M-discs. These cytoskeletal rings may play a role in the maintenance of the structural integrity of striated muscle throughout cycles of contraction and relaxation.

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“…CK is found as four isoenzymes: three cytosolic forms MM, MB and BB, named according to the tissue where they are predominantly found (MM in muscle, BB in brain), and a mitochondrial form, bound to the external face of the internal membrane [5]. A part of the MM form is firmly bound to the M line of the myofilaments [6] and can only be detached in low ionic strength medium [7].…”

Section: Introductionmentioning

confidence: 99%

An example of substrate channeling between co‐immobilized enzymes Coupled activity of myosin ATPase and creatine kinase bound to frog heart myofilaments

Arrio-Dupont

1988

FEBS Letters

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In myofilaments obtained by Triton X-100 lysis of frog heart cells in high ionic strength medium, the activity of bound creatine kinase cannot be detected by a coupled enzymatic assay. ATP is channel&d toward myosin ATPase, through the unstirred layer near myofilaments and cannot diffuse into the bulk solution. Model systems based upon the coupled kinetics of enzymes co-immobilized on the same surface may explain this behaviour. This may also account for why myofilament-bound creatine kinase is more efficient than free enzyme in the cytosol for the physiological recycling of ADP into ATP.

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Ultrastructure studies on the binding of creatine kinase and the 165,000 molecular weight component to the M-band of muscle

Cited by 18 publications

References 11 publications

Presence of enolase in the M-band of skeletal muscle and possible indirect interaction with the cytosolic muscle isoform of creatine kinase

Presence of enolase in the M-band of skeletal muscle and possible indirect interaction with the cytosolic muscle isoform of creatine kinase

Skelemins: cytoskeletal proteins located at the periphery of M-discs in mammalian striated muscle.

An example of substrate channeling between co‐immobilized enzymes Coupled activity of myosin ATPase and creatine kinase bound to frog heart myofilaments

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