Journal ArticleDOI
Collagen of slow twitch and fast twitch muscle fibres in different types of rat skeletal muscle
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TLDR
Investigation of skeletal muscles with different contractile properties using endurance trained and untrained rats as experimental animals found biochemical evidence that MS and the slow twitch area of MG are more collagenous than MRF and the fast twitch Area of MG both at the level of perimysium and endomysium.Abstract:
The appearance of collagen around individual fast twitch (FT) and slow twitch (ST) muscle fibres was investigated in skeletal muscles with different contractile properties using endurance trained and untrained rats as experimental animals. The collagenous connective tissue was analyzed by measuring hydroxyproline biochemically and by staining collagenous material histochemically in M. soleus (MS), M. rectus femoris (MRF), and M. gastrocnemius (MG). The concentration of hydroxyproline in the ST fibres dissected from MS (2.72±0.35 Μg·mg−1 d.w.) was significantly higher than that of the FT fibres dissected from MRF (1.52±0.33 Μg·mg−1 d.w.). Similarly, the concentration of hydroxyproline was higher in ST (2.54±0.51 ⧎g·mg−1 d.w.) than in FT fibres (1.60±0.43 Μg·mg−1 d.w.), when the fibres were dissected from the same muscle, MG. Histochemical staining of collagenous material agreed with the biochemical evidence that MS and the slow twitch area of MG are more collagenous than MRF and the fast twitch area of MG both at the level of perimysium and endomysium. The variables were not affected by endurance training. When discussing the role of collagen in the function of skeletal muscle it is suggested that the different functional demands of different skeletal muscles are also reflected in the structure of intramuscular connective tissue, even at the level of endomysial collagen. It is supposed that the known differences in the elastic properties of fast tetanic muscle compared to slow tonic muscle as, e.g., the higher compliance of fast muscle could at least partly be explained in terms of the amount, type, and structure of intramuscular collagen.read more
Citations
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Fiber types in mammalian skeletal muscles.
TL;DR: Mammalian skeletal muscle comprises different fiber types, whose identity is first established during embryonic development by intrinsic myogenic control mechanisms and is later modulated by neural and hormonal factors.
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Role of Extracellular Matrix in Adaptation of Tendon and Skeletal Muscle to Mechanical Loading
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Coordinated collagen and muscle protein synthesis in human patella tendon and quadriceps muscle after exercise
Benjamin F. Miller,Jens Lykkegaard Olesen,Mette Hansen,Simon Døssing,Regina M. Crameri,Rasmus J. Welling,Henning Langberg,Allan Flyvbjerg,Michael Kjaer,John A. Babraj,Kenneth Smith,Kenneth Smith,Michael J. Rennie,Michael J. Rennie +13 more
TL;DR: There is a rapid increase in collagen synthesis after strenuous exercise in human tendon and muscle, and the similar time course of changes of protein synthetic rates in different cell types supports the idea of coordinated musculotendinous adaptation.
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Muscle strength and its development. New perspectives.
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A second look into fibre typing--relation to meat quality.
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References
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Journal ArticleDOI
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P. R. Cavanagh,Paavo V. Komi +1 more
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Journal ArticleDOI
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Helen A. Padykula,Edith Herman +1 more
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