Stimulation-induced expression of slow muscle myosin in a fast muscle of the rat

FEBS Letters ◽  
1993 ◽  
Vol 327 (3) ◽  
pp. 297-300 ◽  
Author(s):  
Caroline N. Mayne ◽  
Thomas Mokrusch ◽  
Jonathan C. Jarvis ◽  
Stephen J. Gilroy ◽  
Stanley Salmons
Keyword(s):  
Slow Muscle ◽  
Fast Muscle ◽  
Induced Expression ◽  
Muscle Myosin

scholarly journals Differences between Slow and Fast Muscle Myosin

1970 ◽  
Vol 245 (2) ◽  
pp. 219-224
Author(s):  
Frederick J. Samaha ◽  
Lloyd Guth ◽  
R. Wayne Albers
Keyword(s):  
Fast Muscle ◽  
Muscle Myosin

scholarly journals Myosin heavy-chain composition in striated muscle after tenotomy

1992 ◽  
Vol 282 (1) ◽  
pp. 237-242 ◽  
Author(s):  
A Jakubiec-Puka ◽  
C Catani ◽  
U Carraro
Keyword(s):  
Myosin Heavy Chain ◽  
Heavy Chain ◽  
Striated Muscle ◽  
Slow Muscle ◽  
Fast Muscle ◽  
Muscle Fibres ◽  
Adult Rats ◽  
Tendon Regeneration ◽  
Adult Muscle ◽  
Gastrocnemius Muscles

The myosin heavy-chain (MHC) isoform pattern was studied by biochemical methods in the slow-twitch (soleus) and fast-twitch (gastrocnemius) muscles of adult rats during atrophy after tenotomy and recovery after tendon regeneration. The tenotomized slow muscle atrophied more than the tenotomized fast muscle. During the 12 days after tenotomy the total MHC content decreased by about 85% in the slow muscle, and only by about 35% in the fast muscle. In the slow muscle the ratio of MHC-1 to MHC-2A(2S) remained almost unchanged, showing that similar diminution of both isoforms occurs. In the fast muscle the MHC-2A/MHC-2B ratio decreased, showing the loss of MHC-2A mainly. After tendon regeneration, the slow muscle recovered earlier than the fast muscle. Full recovery of the muscles was not observed until up to 4 months later. The embryonic MHC, which seems to be expressed in denervated adult muscle fibres, was not detected by immunoblotting in the tenotomized muscles during either atrophy or recovery after tendon regeneration. The influence of tenotomy and denervation on expression of the MHC isoforms is compared. The results show that: (a) MHC-1 and MHC-2A(2S) are very sensitive to tenotomy, whereas MHC-2B is much less sensitive; (b) expression of the embryonic MHC in adult muscle seems to be inhibited by the intact neuromuscular junction.

Red and white muscle development in the trout (Oncorhynchus mykiss) as shown by in situ hybridisation of fast and slow myosin heavy chain transcripts

2001 ◽  
Vol 204 (12) ◽  
pp. 2097-2101 ◽  
Author(s):  
Pierre-Yves Rescan ◽  
Bertrand Collet ◽  
Cecile Ralliere ◽  
Chantal Cauty ◽  
Jean-Marie Delalande ◽  
...  
Keyword(s):  
Myosin Heavy Chain ◽  
Heavy Chain ◽  
In Situ Hybridisation ◽  
Slow Muscle ◽  
Fast Muscle ◽  
Slow Myosin ◽  
Slow Myosin Heavy Chain ◽  
And Migration ◽  
Slow Myhc

SUMMARY The axial muscle of most teleost species consists of a deep bulk of fast-contracting white fibres and a superficial strip of slow-contracting red fibres. To investigate the embryological development of fast and slow muscle in trout embryos, we carried out single and double in situ hybridisation with fast and slow myosin heavy chain (MyHC)-isoform-specific riboprobes. This showed that the slow-MyHC-positive cells originate in a region of the somite close to the notochord. As the somite matures in a rostrocaudal progression, the slow-MyHC-positive cells appear to migrate radially away from the notochord to the lateral surface of the myotome, where they form the superficial strip of slow muscle. Surprisingly, the expression pattern of the fast MyHC showed that the differentiation of fast muscle commences in the medial domain of the somite before the differentiation and migration of the slow muscle precursors. Later, as the differentiation of fast muscle progressively spreads from the inside to the outside of the myotome, slow-MyHC-expressing cells become visible medially. Our observations that the initial differentiation of fast muscle takes place in proximity to axial structures and occurs before the differentiation and migration of slow muscle progenitors are not in accord with the pattern of muscle formation in teleosts previously described in the zebrafish Danio rerio, which is often used as the model organism in fishes.

Regenerated rat fast muscle transplanted to the slow muscle bed and innervated by the slow nerve, exhibits an identical myosin heavy chain repertoire to that of the slow muscle

1996 ◽  
Vol 106 (5) ◽  
pp. 473-479 ◽  
Author(s):  
Erika Snoj-Cvetko ◽  
Janez Sketelj ◽  
Igor Dolenc ◽  
Slavko Obreza ◽  
Chantal Janmot ◽  
...  
Keyword(s):  
Myosin Heavy Chain ◽  
Heavy Chain ◽  
Slow Muscle ◽  
Fast Muscle

scholarly journals Desensitizing mouse cardiac troponin C to calcium converts slow muscle towards a fast muscle phenotype

2018 ◽  
Vol 596 (19) ◽  
pp. 4651-4663 ◽  
Author(s):  
Svetlana Tikunova ◽  
Natalya Belevych ◽  
Kelly Doan ◽  
Peter J. Reiser
Keyword(s):  
Cardiac Troponin ◽  
Troponin C ◽  
Slow Muscle ◽  
Fast Muscle ◽  
Cardiac Troponin C

scholarly journals Polymorphism of sarcoplasmic-reticulum adenosine triphosphatase of rabbit skeletal muscle

1981 ◽  
Vol 197 (1) ◽  
pp. 245-248 ◽  
Author(s):  
E Damiani ◽  
R Betto ◽  
S Salvatori ◽  
P Volpe ◽  
G Salviati ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Sarcoplasmic Reticulum ◽  
Immunosorbent Assay ◽  
Adenosine Triphosphatase ◽  
Slow Muscle ◽  
Fast Muscle ◽  
Enzyme Linked Immunosorbent Assay ◽  
Immunological Relationship ◽  
One Step ◽  
Membrane Bound

Antibody was raised in chickens against purified sarcoplasmic-reticulum Ca2+-activated ATPase (Ca2+-ATPase). The immunological relationship between the Ca2+-ATPase of fast-muscle and slow-muscle sarcoplasmic reticulum was investigated by a one-step and a two-step competitive enzyme-linked immunosorbent assay (ELISA). The results show marked antigenic differences between the membrane-bound Ca2+-ATPase of the sarcoplasmic-reticulum vesicles from fast muscle and slow muscle, beside differences in the membrane content of ATPase protein.

scholarly journals Force-velocity characteristics and metabolism of carp muscle fibres following temperature acclimation

1985 ◽  
Vol 119 (1) ◽  
pp. 239-249 ◽  
Author(s):  
I. A. Johnston ◽  
B. D. Sidell ◽  
W. R. Driedzic
Keyword(s):  
Cytochrome Oxidase ◽  
Citrate Synthase ◽  
Temperature Acclimation ◽  
Slow Muscle ◽  
Fast Muscle ◽  
Acclimation Temperature ◽  
Muscle Fibres ◽  
Mechanical Power Output ◽  
Slow Muscle Fibres ◽  
Force Velocity

Common carp (Cyprinus carpio L.), 1 kg body weight, were acclimated for 1–2 months to water temperatures of either 7–8 degrees C (cold-acclimated group) or 23–24 degrees C (warm-acclimated group). Single fast fibres and small bundles of slow fibres were isolated from the myotomal muscles and chemically skinned. Force-velocity (P-V) characteristics were determined at 7 degrees C and 23 degrees C. The contractile properties of carp muscle fibres are dependent on acclimation temperature. In the warm-acclimated group maximum isometric tensions (P0, kN m-2) are 47 +/− 6 and 64 +/− 5 for slow muscle fibres and 76 +/− 10 and 209 +/− 21 for fast muscle fibres at 7 degrees C and 23 degrees C, respectively. Maximum contraction velocities (Vmax, muscle lengths-1), are 0.4 +/− 0.05 and 1.5 +/− 0.1 at 7 degrees C (slow fibres) and 0.6 +/− 0.04 and 1.9 +/− 0.4 at 23 degrees C (fast fibres). All values represent mean +/− S.E. P0 and Vmax at 7 degrees C are around 1.5-2.0 times higher for slow and fast muscle fibres isolated from the cold-acclimated group. Fibres from 7 degrees C-acclimated carp fail to relax completely following maximal activations at 23 degrees C. The resulting Ca-insensitive force component (50–70% P0) is associated with the development of abnormal crossbridge linkages and very slow contraction velocities. Activities of enzymes associated with energy metabolism were determined at a common temperature of 15 degrees C. Marker enzymes of the electron transport system (cytochrome oxidase), citric acid cycle (citrate synthase), fatty acid metabolism (carnitine palmitoyl transferase, beta-hydroxyacyl CoA dehydrogenase) and aerobic glucose utilization (hexokinase) have 30–60% higher activities in slow muscle from cold-acclimated than from warm-acclimated fish. Activities of cytochrome oxidase and citrate synthase in fast muscle are also elevated following acclimation to low temperature. It is concluded that thermal compensation of mechanical power output by carp skeletal muscle is matched by a concomitant increase in the potential to supply aerobically-generated ATP at low temperatures.

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