scholarly journals Ultrastructural remodelling of slow skeletal muscle fibres in creatine kinase deficient mice: a quantitative study

2016 ◽  
Vol 35 (04) ◽  
pp. 477-486 ◽  
Author(s):  
Marta Novotová ◽  
Bohumila Tarabová ◽  
Lucia Tylková ◽  
Renée Ventura-Clapier ◽  
Ivan Zahradník
Keyword(s):  
Skeletal Muscle ◽  
Creatine Kinase ◽  
Quantitative Study ◽  
Muscle Fibres ◽  
Slow Skeletal Muscle ◽  
Skeletal Muscle Fibres ◽  
Deficient Mice

scholarly journals Properties of the ‘slow’ skeletal muscle fibres of the frog*

1953 ◽  
Vol 121 (2) ◽  
pp. 318-340 ◽  
Author(s):  
Stephen W. Kuffler ◽  
E. M. Vaughan Williams
Keyword(s):  
Skeletal Muscle ◽  
Muscle Fibres ◽  
Slow Skeletal Muscle ◽  
Skeletal Muscle Fibres

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

1999 ◽  
Vol 338 (1) ◽  
pp. 115-121 ◽  
Author(s):  
Georges FOUCAULT ◽  
Monique VACHER ◽  
Tatyana MERKULOVA ◽  
Angelica KELLER ◽  
Martine ARRIO-DUPONT
Keyword(s):  
Skeletal Muscle ◽  
Creatine Kinase ◽  
Energy Metabolism ◽  
Direct Interaction ◽  
Cross Linking ◽  
Muscle Fibres ◽  
Skinned Fibres ◽  
Two Dimensional Gel Electrophoresis ◽  
The Cross ◽  
Skeletal Muscle Fibres

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 α (ubiquitous) and β (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 β-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.

Two functionally distinct myosin heavy chain isoforms in slow skeletal muscle fibres

FEBS Letters ◽  
1997 ◽  
Vol 410 (2-3) ◽  
pp. 150-152 ◽  
Author(s):  
Stefan Galler ◽  
Karlheinz Hilber ◽  
Bärbel Gohlsch ◽  
Dirk Pette
Keyword(s):  
Skeletal Muscle ◽  
Myosin Heavy Chain ◽  
Heavy Chain ◽  
Myosin Heavy Chain Isoforms ◽  
Muscle Fibres ◽  
Slow Skeletal Muscle ◽  
Skeletal Muscle Fibres
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