Kinetic properties of myosin heavy chain isoforms in mouse skeletal muscle: comparison with rat, rabbit, and human and correlation with amino acid sequence

2004 ◽  
Vol 287 (6) ◽  
pp. C1725-C1732 ◽  
Author(s):  
Oleg Andruchov ◽  
Olena Andruchova ◽  
Yishu Wang ◽  
Stefan Galler
Keyword(s):  
Skeletal Muscle ◽  
Amino Acid ◽  
Myosin Heavy Chain ◽  
Heavy Chain ◽  
Actin Binding ◽  
Kinetic Properties ◽  
Fiber Types ◽  
Mouse Skeletal Muscle ◽  
Structural Variability ◽  
Kinetics Of

Stretch activation kinetics were investigated in skinned mouse skeletal muscle fibers of known myosin heavy chain (MHC) isoform content to assess kinetic properties of different myosin heads while generating force. The time to peak of stretch-induced delayed force increase ( t3) was strongly correlated with MHC isoforms [ t3 given in ms for fiber types containing specified isoforms; means ± SD with n in parentheses: MHCI 680 ± 108 ( 13 ), MHCIIa 110.5 ± 10.7 ( 23 ), MHCIIx(d) 46.2 ± 5.2 ( 20 ), MHCIIb 23.5 ± 3.3 (76)]. This strong correlation suggests different kinetics of force generation of different MHC isoforms in the following order:MHCIIb > MHCIIx(d) > MHCIIa ≫ MHCI. For rat, rabbit, and human skeletal muscles the same type of correlation was found previously. The kinetics decreases slightly with increasing body mass. Available amino acid sequences were aligned to quantify the structural variability of MHC isoforms of different animal species. The variation in t3 showed a correlation with the structural variability of specific actin-binding loops (so-called loop 2 and loop 3) of myosin heads ( r = 0.74). This suggests that alterations of amino acids in these loops contribute to the different kinetics of myosin heads of various MHC isoforms.

scholarly journals Mutation of the IIB myosin heavy chain gene results in muscle fiber loss and compensatory hypertrophy

2001 ◽  
Vol 280 (3) ◽  
pp. C637-C645 ◽  
Author(s):  
David L. Allen ◽  
Brooke C. Harrison ◽  
Carol Sartorius ◽  
William C. Byrnes ◽  
Leslie A. Leinwand
Keyword(s):  
Skeletal Muscle ◽  
Myosin Heavy Chain ◽  
Body Mass ◽  
Heavy Chain ◽  
Compensatory Hypertrophy ◽  
Muscle Disease ◽  
Chain Gene ◽  
Fiber Types ◽  
Mouse Skeletal Muscle ◽  
Ultrastructural Studies

The fast skeletal IIb gene is the source of most myosin heavy chain (MyHC) in adult mouse skeletal muscle. We have examined the effects of a null mutation in the IIb MyHC gene on the growth and morphology of mouse skeletal muscle. Loss in muscle mass of several head and hindlimb muscles correlated with amounts of IIb MyHC expressed in that muscle in wild types. Decreased mass was accompanied by decreases in mean fiber number, and immunological and ultrastructural studies revealed fiber pathology. However, mean cross-sectional area was increased in all fiber types, suggesting compensatory hypertrophy. Loss of muscle and body mass was not attributable to impaired chewing, and decreased food intake as a softer diet did not prevent the decrease in body mass. Thus loss of the major MyHC isoform produces fiber loss and fiber pathology reminiscent of muscle disease.

scholarly journals Kinetic properties of myosin heavy chain isoforms in single fibers from human skeletal muscle

FEBS Letters ◽  
1999 ◽  
Vol 455 (3) ◽  
pp. 267-270 ◽  
Author(s):  
Karlheinz Hilber ◽  
Stefan Galler ◽  
Bärbel Gohlsch ◽  
Dirk Pette
Keyword(s):  
Skeletal Muscle ◽  
Myosin Heavy Chain ◽  
Heavy Chain ◽  
Human Skeletal Muscle ◽  
Myosin Heavy Chain Isoforms ◽  
Kinetic Properties ◽  
Single Fibers

The homoeobox geneSIX1alters myosin heavy chain isoform expression in mouse skeletal muscle

2013 ◽  
Vol 210 (2) ◽  
pp. 415-428 ◽  
Author(s):  
K. L. Hetzler ◽  
B. C. Collins ◽  
R. A. Shanely ◽  
H. Sue ◽  
M. C. Kostek
Keyword(s):  
Skeletal Muscle ◽  
Myosin Heavy Chain ◽  
Heavy Chain ◽  
Myosin Heavy Chain Isoform ◽  
Mouse Skeletal Muscle ◽  
Isoform Expression

scholarly journals Thin-filament length correlates with fiber type in human skeletal muscle

2012 ◽  
Vol 302 (3) ◽  
pp. C555-C565 ◽  
Author(s):  
David S. Gokhin ◽  
Nancy E. Kim ◽  
Sarah A. Lewis ◽  
Heinz R. Hoenecke ◽  
Darryl D. D'Lima ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Myosin Heavy Chain ◽  
Heavy Chain ◽  
Thin Filament ◽  
Fiber Type ◽  
Pectoralis Major Muscle ◽  
Thick Filament ◽  
Fiber Types ◽  
Filament Length ◽  
Orthopedic Rehabilitation

Force production in skeletal muscle is proportional to the amount of overlap between the thin and thick filaments, which, in turn, depends on their lengths. Both thin- and thick-filament lengths are precisely regulated and uniform within a myofibril. While thick-filament lengths are essentially constant across muscles and species (∼1.65 μm), thin-filament lengths are highly variable both across species and across muscles of a single species. Here, we used a high-resolution immunofluorescence and image analysis technique (distributed deconvolution) to directly test the hypothesis that thin-filament lengths vary across human muscles. Using deltoid and pectoralis major muscle biopsies, we identified thin-filament lengths that ranged from 1.19 ± 0.08 to 1.37 ± 0.04 μm, based on tropomodulin localization with respect to the Z-line. Tropomodulin localized from 0.28 to 0.47 μm further from the Z-line than the NH2-terminus of nebulin in the various biopsies, indicating that human thin filaments have nebulin-free, pointed-end extensions that comprise up to 34% of total thin-filament length. Furthermore, thin-filament length was negatively correlated with the percentage of type 2X myosin heavy chain within the biopsy and shorter in type 2X myosin heavy chain-positive fibers, establishing the existence of a relationship between thin-filament lengths and fiber types in human muscle. Together, these data challenge the widely held assumption that human thin-filament lengths are constant. Our results also have broad relevance to musculoskeletal modeling, surgical reattachment of muscles, and orthopedic rehabilitation.

scholarly journals Skeletal muscle myosin heavy chain composition and resistance training

1993 ◽  
Vol 74 (2) ◽  
pp. 911-915 ◽  
Author(s):  
G. R. Adams ◽  
B. M. Hather ◽  
K. M. Baldwin ◽  
G. A. Dudley
Keyword(s):  
Skeletal Muscle ◽  
Resistance Training ◽  
Myosin Heavy Chain ◽  
Heavy Chain ◽  
Fiber Type ◽  
Type I ◽  
Fiber Types ◽  
Type Distribution ◽  
Heavy Resistance Training ◽  
Fiber Type Distribution

We recently reported that 19 wk of heavy resistance training caused a decrease in the percentage of type IIb and an increase in the percentage of type IIa fibers as determined by qualitative histochemical analyses of myofibrillar adenosinetriphosphatase activity of biopsies of musculus vastus lateralis (Hather et al. Acta Physiol. Scand. 143: 177–185, 1991). These data were interpreted to suggest that resistance training had caused transformation among the fast-twitch fiber subtypes. To more clearly establish the influence of resistance training on muscle fiber composition, biopsies from the original study were analyzed biochemically for myosin heavy chain (MHC) composition by use of sodium dodecyl sulfate-polyacrylamide gel electrophoresis and histochemically for fiber types by use of myofibrillar adenosinetriphosphatase activity. The results show that after training (n = 13), IIb MHC composition decreased (P < 0.05) from 19 +/- 4 to 7 +/- 1%. IIa MHC, in contrast, increased (P < 0.05) from 48 +/- 3 to 60 +/- 2%. These responses were essentially mirrored by alterations in fiber type distribution. The percentage of type IIb fibers decreased (P < 0.05) from 18 +/- 3 to 1 +/- 1%, whereas the percentage of type IIa fibers increased from 46 +/- 4 to 60 +/- 3% (P < 0.05). Neither I MHC composition nor type I fiber percentage changed with training. The control group (n = 4) showed no changes in MHC composition or fiber type distribution. These results suggest that heavy resistance training alters MHC composition in human skeletal muscle, presumably reflecting a change in genetic expression.

scholarly journals Identification in skeletal muscle of a distinct extracellular pool of amino acids, and its role in protein synthesis

1971 ◽  
Vol 121 (5) ◽  
pp. 817-827 ◽  
Author(s):  
R. C. Hider ◽  
E. B. Fern ◽  
D. R. London
Keyword(s):  
Skeletal Muscle ◽  
Amino Acids ◽  
Protein Synthesis ◽  
Amino Acid ◽  
Incubation Medium ◽  
Extensor Digitorum Longus ◽  
Extensor Digitorum ◽  
Longus Muscle ◽  
Kinetics Of

1. The kinetics of radioactive labelling of extra- and intra-cellular amino acid pools and protein of the extensor digitorum longus muscle were studied after incubations with radioactive amino acids in vitro. 2. The results indicated that an extracellular pool could be defined, the contents of which were different from those of the incubation medium. 3. It was concluded that amino acids from the extracellular pool, as defined in this study, were incorporated directly into protein.

Myosin Heavy Chain Expression in Skeletal Muscle Autografts under Neural or Aneural Conditions

1998 ◽  
Vol 75 (2) ◽  
pp. 135-147 ◽  
Author(s):  
Kotaro Yoshimura ◽  
William M. Kuzon ◽  
Kiyonori Harii
Keyword(s):  
Skeletal Muscle ◽  
Myosin Heavy Chain ◽  
Heavy Chain
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