Fast myosin heavy chains expressed in secondary mammalian muscle fibers at the time of their inception

1994 ◽  
Vol 107 (9) ◽  
pp. 2361-2371 ◽  
Author(s):  
M. Cho ◽  
S.M. Hughes ◽  
I. Karsch-Mizrachi ◽  
M. Travis ◽  
L.A. Leinwand ◽  
...  
Keyword(s):  
Muscle Development ◽  
Muscle Fibers ◽  
Fiber Formation ◽  
Mammalian Skeletal Muscle ◽  
Western Blots ◽  
Mammalian Muscle ◽  
Heavy Chains ◽  
Fast Myosin ◽  
Myhc Isoforms ◽  
Fast Myosin Heavy Chain

Mammalian skeletal muscle is generated by two waves of fiber formation, resulting in primary and secondary fibers. These fibers mature to give rise to several classes of adult muscle fibers with distinct contractile properties. Here we describe fast myosin heavy chain (MyHC) isoforms that are expressed in nascent secondary, but not primary, fibers in the early development of rat and human muscle. These fast MyHCs are distinct from previously described embryonic and neonatal fast MyHCs. To identify these MyHCs, monoclonal antibodies were used whose specificity was determined in western blots of MyHCs on denaturing gels and reactivity with muscle tissue at various stages of development. To facilitate a comparison of our results with those of others obtained using different antibodies or species, we have identified cDNAs that encode the epitopes recognized by our antibodies wherever possible. The results suggest that epitopes characteristic of adult fast MyHCs are expressed very early in muscle fiber development and distinguish newly formed secondary fibers from primary fibers. This marker of secondary fibers, which is detectable at the time of their inception, should prove useful in future studies of the derivation of primary and secondary fibers in mammalian muscle development.

scholarly journals Slow and fast myosin heavy chain content defines three types of myotubes in early muscle cell cultures.

1985 ◽  
Vol 101 (5) ◽  
pp. 1643-1650 ◽  
Author(s):  
J B Miller ◽  
M T Crow ◽  
F E Stockdale
Keyword(s):  
Myosin Heavy Chain ◽  
Heavy Chain ◽  
Pectoral Muscle ◽  
Myosin Heavy Chain Isoforms ◽  
Fiber Formation ◽  
Single Type ◽  
Fast Myosin ◽  
Slow Myosin Heavy Chain ◽  
Fast Myosin Heavy Chain ◽  
Different Populations

We prepared monoclonal antibodies specific for fast or slow classes of myosin heavy chain isoforms in the chicken and used them to probe myosin expression in cultures of myotubes derived from embryonic chicken myoblasts. Myosin heavy chain expression was assayed by gel electrophoresis and immunoblotting of extracted myosin and by immunostaining of cultures of myotubes. Myotubes that formed from embryonic day 5-6 pectoral myoblasts synthesized both a fast and a slow class of myosin heavy chain, which were electrophoretically and immunologically distinct, but only the fast class of myosin heavy chain was synthesized by myotubes that formed in cultures of embryonic day 8 or older myoblasts. Furthermore, three types of myotubes formed in cultures of embryonic day 5-6 myoblasts: one that contained only a fast myosin heavy chain, a second that contained only a slow myosin heavy chain, and a third that contained both a fast and a slow heavy chain. Myotubes that formed in cultures of embryonic day 8 or older myoblasts, however, were of a single type that synthesized only a fast class of myosin heavy chain. Regardless of whether myoblasts from embryonic day 6 pectoral muscle were cultured alone or mixed with an equal number of myoblasts from embryonic day 12 muscle, the number of myotubes that formed and contained a slow class of myosin was the same. These results demonstrate that the slow class of myosin heavy chain can be synthesized by myotubes formed in cell culture, and that three types of myotubes form in culture from pectoral muscle myoblasts that are isolated early in development, but only one type of myotube forms from older myoblasts; and they suggest that muscle fiber formation probably depends upon different populations of myoblasts that co-exist and remain distinct during myogenesis.

scholarly journals Type 2X-myosin heavy chain is coded by a muscle fiber type-specific and developmentally regulated gene.

1993 ◽  
Vol 123 (4) ◽  
pp. 823-835 ◽  
Author(s):  
C DeNardi ◽  
S Ausoni ◽  
P Moretti ◽  
L Gorza ◽  
M Velleca ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Myosin Heavy Chain ◽  
Heavy Chain ◽  
Muscle Development ◽  
Fiber Type ◽  
Muscle Fibers ◽  
Hindlimb Muscles ◽  
Isolation And Characterization ◽  
Skeletal Muscle Fibers ◽  
Myhc Isoforms

We have previously reported the identification of a distinct myosin heavy chain (MyHC) isoform in a major subpopulation of rat skeletal muscle fibers, referred to as 2X fibers (Schiaffino, S., L. Gorza, S. Sartore, L. Saggin, M. Vianello, K. Gundersen, and T. Lømo. 1989. J. Muscle Res. Cell Motil. 10:197-205). However, it was not known whether 2X-MyHC is the product of posttranslational modification of other MyHCs or is coded by a distinct mRNA. We report here the isolation and characterization of cDNAs coding a MyHC isoform that is expressed in type 2X skeletal muscle fibers. 2X-MyHC transcripts differ from other MyHC transcripts in their restriction map and 3' end sequence and are thus derived from a distinct gene. In situ hybridization analyses show that 2X-MyHC transcripts are expressed at high levels in the diaphragm and fast hindlimb muscles and can be coexpressed either with 2B- or 2A-MyHC transcripts in a number of fibers. At the single fiber level the distribution of each MyHC mRNA closely matches that of the corresponding protein, determined by specific antibodies on serial sections. In hindlimb muscles 2X-, 2A-, and 2B-MyHC transcripts are first detected by postnatal day 2-5 and display from the earliest stages a distinct pattern of distribution in different muscles and different fibers. The emergence of type 2 MyHC isoforms thus defines a distinct neonatal phase of fiber type differentiation during muscle development. The functional significance of MyHC isoforms is discussed with particular reference to the velocity of shortening of skeletal muscle fibers.

Evidence for three adult fast myosin heavy chain isoforms in type II skeletal muscle fibers in pigs.

1998 ◽  
Vol 76 (6) ◽  
pp. 1584 ◽  
Author(s):  
L Lefaucheur ◽  
R K Hoffman ◽  
D E Gerrard ◽  
C S Okamura ◽  
N Rubinstein ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Myosin Heavy Chain ◽  
Heavy Chain ◽  
Muscle Fibers ◽  
Myosin Heavy Chain Isoforms ◽  
Type Ii ◽  
Fast Myosin ◽  
Skeletal Muscle Fibers ◽  
Fast Myosin Heavy Chain

Adaptation of fibers in fast-twitch muscles of rats to spaceflight and hindlimb suspension

1992 ◽  
Vol 73 (2) ◽  
pp. S58-S65 ◽  
Author(s):  
B. Jiang ◽  
Y. Ohira ◽  
R. R. Roy ◽  
Q. Nguyen ◽  
E. I. Ilyina-Kakueva ◽  
...  
Keyword(s):  
Cross Sections ◽  
Medial Gastrocnemius ◽  
Hindlimb Suspension ◽  
Cross Sectional ◽  
Heavy Chains ◽  
Fast Myosin ◽  
Glycerophosphate Dehydrogenase ◽  
Close Relationship ◽  
Fast Myosin Heavy Chain ◽  
Fast Twitch

The adaptation of single fibers in medial gastrocnemius (MG), a fast-twitch extensor, and tibialis anterior (TA), a fast-twitch flexor, was studied after 14 days of spaceflight (COSMOS 2044) or hindlimb suspension. Cross-sectional area (CSA) and succinate dehydrogenase (SDH), alpha-glycerophosphate dehydrogenase (GPD), and myofibrillar adenosinetriphosphatase (ATPase) activities were determined in fibers identified in frozen serial cross sections. Fibers were categorized as light, dark, or intermediate on the basis of myosin ATPase staining and alkaline preincubation and immunohistochemically as reacting with slow, fast, or both slow and fast myosin heavy chain monoclonal antibodies. Because there was a close relationship between these two means of categorizing fibers, all fibers were categorized on the basis of the immunohistochemical reaction. The percentage of slow- and fast-twitch fibers of the MG and TA were unchanged in either group. Mean fiber size of all fibers, irrespective of type, was unaffected in either muscle after flight or suspension. The fibers that expressed both fast and slow myosin heavy chains were smaller than control in the MG of both experimental groups. Compared with control, the SDH and total SDH activities in the MG were significantly less in suspended rats, with the fast-twitch fibers showing the largest difference. The ATPase activity in the MG was higher in flight than in control or suspended rats. There were no significant effects of flight on fibers of the TA. In contrast, the TA in suspended rats had higher GPD activities than either control or flight rats.(ABSTRACT TRUNCATED AT 250 WORDS)

Relationship between calpastatin activity and the slow and fast myosin heavy chain content of ovine skeletal muscles

2002 ◽  
Vol 2002 ◽  
pp. 173-173
Author(s):  
A.Q. Sazili ◽  
P.L. Sensky ◽  
T. Parr ◽  
R.G. Bardsley ◽  
P.J. Buttery
Keyword(s):  
Atpase Activity ◽  
Myosin Heavy Chain ◽  
Heavy Chain ◽  
Skeletal Muscles ◽  
Myofibrillar Atpase ◽  
Heavy Chains ◽  
Fast Myosin ◽  
Myofibrillar Atpase Activity ◽  
Fast Myosin Heavy Chain ◽  
The Relationship

Calpastatin, the specific endogenous inhibitor of the calpain system, is considered to be a principle contributor to variations in meat tenderisation (Parr et al., 1999). Previous studies have suggested that the differences in calpastatin activity in different ovine skeletal muscles could be influenced by muscle metabolic and contractile characteristics according to myofibrillar ATPase activity (Ouali and Talmant, 1990). The type of myofibrillar ATPase activity is largely determined by the content of slow or fast myosin heavy chains (Rivero et al., 1999). The present study was designed to investigate the relationship between calpastatin inhibitory activity and slow myosin heavy chain (MHC-s) and fast myosin heavy chain (MHC-f) expression.

Two Types of Neonatal-to-Adult Fast Myosin Heavy Chain Transitions in Rat Hindlimb Muscle Fibers

1993 ◽  
Vol 157 (2) ◽  
pp. 359-370 ◽  
Author(s):  
Steven D. Russell ◽  
Natalie A. Cambon ◽  
Robert G. Whalen
Keyword(s):  
Myosin Heavy Chain ◽  
Heavy Chain ◽  
Muscle Fibers ◽  
Fast Myosin ◽  
Hindlimb Muscle ◽  
Fast Myosin Heavy Chain

scholarly journals Myofibrillar ATPase activity of feline muscle fibers expressing slow and fast myosin heavy chains.

1995 ◽  
Vol 43 (8) ◽  
pp. 811-819 ◽  
Author(s):  
R J Talmadge ◽  
R R Roy ◽  
B Jiang ◽  
V R Edgerton
Keyword(s):  
Atpase Activity ◽  
Linear Relationship ◽  
Muscle Fibers ◽  
Medial Gastrocnemius ◽  
Myofibrillar Atpase ◽  
Heavy Chains ◽  
Fast Myosin ◽  
Myofibrillar Atpase Activity ◽  
Acid Acid ◽  
Highly Correlated

The interrelationships among myofibrillar ATPase activity (Quant-mATPase), qualitative myofibrillar ATPase staining after acid (Acid-mATPase) and alkaline (Alk-mATPase) preincubations, and myosin heavy chain (MHC) composition were determined in frozen sections of soleus (Sol) and medial gastrocnemius (MG) muscle fibers from adult control cats and cats 6 months after complete spinal cord transection (Sp). Fibers were categorized as either fast, slow, or fast and slow (Fast-Slow) based on monoclonal antibody labeling. Slow fibers had low Quant-mATPase activity and stained lightly with Alk-mATPase and darkly with Acid-mATPase. Fast fibers had high Quant-mATPase activity (approximately twice that of slow fibers) and stained darkly with Alk-mATPase and lightly with Acid-mATPase. Fast-Slow fibers had intermediate Quant-mATPase activity and stained intermediately for Acid-mATPase and darkly for Alk-mATPase. There was a positive linear relationship between Alk-mATPase and Quant-mATPase for all fibers of Sol and MG from control and Sp cats. There was a negative linear relationship between Acid-mATPase and Quant-mATPase for all fibers of Sol and MG. However, within the fast fiber population of the MG there was a positive relationship between these two measures of mATPase. In summary, quantitative and qualitative measures of mATPase are highly correlated with the types of MHC expressed by single fibers from control and Sp cat muscles.

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