Myosin Heavy Chain Composition in Human Masticatory Muscles by Immunohistochemistry and Gel Electrophoresis

2003 ◽  
Vol 51 (1) ◽  
pp. 113-119 ◽  
Author(s):  
J.A.M. Korfage ◽  
T.M.G.J. Van Eijden
Keyword(s):  
Myosin Heavy Chain ◽  
Correlation Coefficient ◽  
Heavy Chain ◽  
Fiber Type ◽  
Masticatory Muscles ◽  
Digastric Muscle ◽  
Type I ◽  
Fiber Types ◽  
Hybrid Fibers ◽  
Cross Sectional

In this study we compared the immunohistochemically quantified fiber type area with the myosin heavy chain (MyHC) contents of a bundle of fibers from a human masticatory muscle. The total cross-sectional areas were determined immunohistochemically for the three major fiber types (I, IIA, and IIX) in bundles of fibers ( n = 42) taken from the anterior and posterior belly of the human digastric muscle ( n = 7). The relative MyHC contents of the same fiber bundles were determined electrophoretically (MyHC-I, -IIA, and -IIX; anterior, 32%, 35%, and 33%; posterior, 39%, 42%, and 19%) and compared with the immunohistochemical data (MyHC-I, -IIA, and -IIX; anterior, 32%, 31%, and 37%; posterior, 39%, 45%, and 15%). No significant differences were seen in the mean fiber type distribution between the two techniques; the correlation coefficient ranged from 0.71 to 0.96. The correlation coefficient was higher for MyHC type I and MyHC type IIX than for MyHC type IIA. The MyHC contents of single fibers taken from the posterior belly indicated that many fibers in this belly co-express MyHC-IIA and MyHC-IIX. Despite the presence of these hybrid fibers, the correspondence between both methods was relatively large.

Enzymatic plasticity of medial gastrocnemius fibers in the adult chronic spinal cat

1990 ◽  
Vol 259 (3) ◽  
pp. C507-C514 ◽  
Author(s):  
B. Jiang ◽  
R. R. Roy ◽  
V. R. Edgerton
Keyword(s):  
Myosin Heavy Chain ◽  
Heavy Chain ◽  
Fiber Type ◽  
Motor Units ◽  
Glycolytic Enzyme ◽  
Medial Gastrocnemius ◽  
Fiber Types ◽  
Cross Sectional ◽  
Fast Myosin ◽  
Weight Support

The metabolic plasticity of single fibers in adult cat medial gastrocnemius (MG) 6 mo after complete spinal cord transection (Sp) at T12-T13 was studied. Some Sp cats were trained to weight support (Sp-WS) 30 min/day beginning 1 mo posttransection. Cross-sectional area, succinate dehydrogenase (SDH), alpha-glycerophosphate dehydrogenase (GPD), and myofibrillar adenosinetriphosphatase (ATPase) activities were determined in fibers identified in frozen serial sections. Fibers were categorized as light or dark based on myosin ATPase staining, alkaline preincubation. The percentage of dark ATPase fibers was higher in Sp and Sp-WS (approximately 85%) than in control (approximately 60%). All dark ATPase fibers reacted positively to a fast myosin heavy chain monoclonal antibody. In both spinal groups, a higher percentage of dark ATPase fibers reacted to both fast and slow myosin heavy chain antibodies than in controls. Neither Sp nor Sp-WS cats showed fiber atrophy. Compared with control, SDH activity was decreased in both fiber types of Sp cats. Daily weight-support training ameliorated this adaptation. There were no differences among the three groups in mean GPD and ATPase activities for either fiber type. There was a slight tendency, however, for spinal cats to have higher GPD and ATPase activities (independent of type) than control, probably reflecting the larger proportion of dark ATPase fibers in these cats. These observations indicate that 6 mo after spinalization in adult cats, some of the fibers of a fast muscle became "faster" and developed oxidative and glycolytic enzyme profiles that normally are exhibited in fast fatigable motor units.(ABSTRACT TRUNCATED AT 250 WORDS)

Cellular adaptations of skeletal muscles to cyclosporine

1998 ◽  
Vol 84 (6) ◽  
pp. 1967-1975 ◽  
Author(s):  
Manmohan S. Biring ◽  
Mario Fournier ◽  
David J. Ross ◽  
Michael I. Lewis
Keyword(s):  
Myosin Heavy Chain ◽  
Heavy Chain ◽  
Cellular Response ◽  
Myosin Heavy Chain Isoforms ◽  
Male Rats ◽  
Type I ◽  
Solid Organ ◽  
Fiber Types ◽  
Cross Sectional ◽  
Final Body Weight

The aim of this study was to evaluate the cellular response of the diaphragm, extensor digitorum longus (EDL), and soleus (Sol) muscles to clinically relevant doses of cyclosporine administered to male rats over 4 wk. Control rats were provided with vehicle only. Muscle fiber types, cross-sectional areas, indexes of capillarity, and succinate dehydrogenase (SDH) activity were determined by quantitative histochemistry. Myosin heavy chain isoforms were identified by SDS-PAGE, and their proportions were measured by scanning densitometry. Serum cyclosporine level, 20–24 h after the last dose of cyclosporine, was 145 ± 81 ng/ml. Final body weight and muscle mass were similar between the cyclosporine and control groups. In the diaphragm, EDL, and Sol, no differences were observed between the groups with regard to fiber type proportions, fiber cross-sectional areas, and proportions of myosin heavy chain isoforms. In the EDL, reductions, both in SDH activity in type I, IIx, and IIb fibers (−26 to −37%) and in indexes of capillarity (−18 to −37%), were noted. In the Sol, SDH activity and capillarity were similar between the groups. In the diaphragm of cyclosporine-treated rats, there was significant reduction in the number of capillaries around individual fibers (−5%), whereas levels of SDH activity tended to be lower. This suggests that activation history may in part determine muscle-specific responses to cyclosporine. We speculate that reduced oxidative activity and capillarity of some limb muscles contribute to reduced exercise capacity and the “deconditioned state” observed in patients receiving cyclosporine after successful solid-organ transplantation.

scholarly journals Muscle Fiber Type Transitions with Exercise Training: Shifting Perspectives

Sports ◽  
2021 ◽  
Vol 9 (9) ◽  
pp. 127
Author(s):  
Daniel L. Plotkin ◽  
Michael D. Roberts ◽  
Cody T. Haun ◽  
Brad J. Schoenfeld
Keyword(s):  
Fiber Type ◽  
Significant Proportion ◽  
Current Evidence ◽  
Type I ◽  
Fiber Types ◽  
Hybrid Fibers ◽  
Long Distance ◽  
Cross Sectional ◽  
Fiber Analysis ◽  
Identification Techniques

Human muscle fibers are generally classified by myosin heavy chain (MHC) isoforms characterized by slow to fast contractile speeds. Type I, or slow-twitch fibers, are seen in high abundance in elite endurance athletes, such as long-distance runners and cyclists. Alternatively, fast-twitch IIa and IIx fibers are abundant in elite power athletes, such as weightlifters and sprinters. While cross-sectional comparisons have shown marked differences between athletes, longitudinal data have not clearly converged on patterns in fiber type shifts over time, particularly between slow and fast fibers. However, not all fiber type identification techniques are created equal and, thus, may limit interpretation. Hybrid fibers, which express more than one MHC type (I/IIa, IIa/IIx, I/IIa/IIx), may make up a significant proportion of fibers. The measurement of the distribution of fibers would necessitate the ability to identify hybrid fibers, which is best done through single fiber analysis. Current evidence using the most appropriate techniques suggests a clear ability of fibers to shift between hybrid and pure fibers as well as between slow and fast fiber types. The context and extent to which this occurs, along with the limitations of current evidence, are discussed herein.

scholarly journals The histochemical profiles of fast fiber types IIB, IID, and IIA in skeletal muscles of mouse, rat, and rabbit.

1993 ◽  
Vol 41 (5) ◽  
pp. 733-743 ◽  
Author(s):  
N Hämäläinen ◽  
D Pette
Keyword(s):  
Myosin Heavy Chain ◽  
Heavy Chain ◽  
Skeletal Muscles ◽  
Fiber Type ◽  
Vastus Lateralis ◽  
Fiber Types ◽  
Cross Sectional ◽  
Fast Fiber ◽  
Myosin Heavy Chain Composition ◽  
Biochemical Analyses

This study characterized histochemically three fast fiber types (IIB, IID, IIA) in skeletal muscles of mouse, rat, and rabbit, with special reference to fiber types IIB and IID. The results are complemented by biochemical analyses of myosin heavy chain composition in these muscles. Fiber type delineation is based on various methods for mATPase staining with pre-incubations and assays under different conditions. In rat and mouse, IIB and IID fibers can be best distinguished according to their different mATPase stabilities towards formaldehyde and alkaline pH. In rabbit, the method of Matoba and Gollnick using acid pre-incubation provided best and most reproducible results. In addition to their different mATPase stabilities, the three fast fiber types differ with regard to their oxidative capacities and cross-sectional fiber areas in the three species. In general, Type IIB fibers are the largest and least oxidative, Type IIA fibers the smallest and most oxidative, and Type IID fibers intermediate. In rabbit, Type IID fibers are the predominant fast fiber population in extensor digitorum longus, psoas, and tibialis anterior muscles. As judged from histochemistry, these muscles of rabbit do not contain pure Type IIB fibers. This is in accordance with biochemical results that show the HCIId to form the majority of the myosin heavy chain complement expressed in these muscles. On the other hand, IIB fibers are numerous in rabbit adductor magnus, gastrocnemius, and vastus lateralis muscles. Similarly, appreciable amounts of myosin heavy chain HCIIb are found in the three latter muscles of rabbit.

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.

Rostrocaudal pattern of fiber-type changes in an overloaded rat ankle extensor

1991 ◽  
Vol 71 (2) ◽  
pp. 558-564 ◽  
Author(s):  
P. F. Gardiner ◽  
B. J. Jasmin ◽  
P. Corriveau
Keyword(s):  
Fiber Type ◽  
Muscle Length ◽  
Similar Degree ◽  
Complex Nature ◽  
Type I ◽  
Fiber Types ◽  
Type Ii ◽  
Cross Sectional ◽  
Hypertrophic Response ◽  
Type I Fibers

Our aim was to quantify the overload-induced hypertrophy and conversion of fiber types (type II to I) occurring in the medial head of the gastrocnemius muscle (MG). Overload of MG was induced by a bilateral tenotomy/retraction of synergists, followed by 12–18 wk of regular treadmill locomotion (2 h of walking/running per day on 3 of 4 days). We counted all type I fibers and determined type I and II mean fiber areas in eight equidistant sections taken along the length of control and overloaded MG. Increase in muscle weights (31%), as well as in total muscle cross-sectional areas (37%) and fiber areas (type I, 57%; type II, 34%), attested to a significant hypertrophic response in overloaded MG. An increase in type I fiber composition of MG from 7.0 to 11.5% occurred as a result of overload, with the greatest and only statistically significant changes (approximately 70–100%) being found in sections taken from the most rostral 45% of the muscle length. Results of analysis of sections taken from the largest muscle girth showed that it significantly underestimated the extent of fiber conversion that occurred throughout the muscle as a whole. These data obtained on the MG, which possesses a compartmentalization of fiber types, support the notion that all fiber types respond to this model with a similar degree of hypertrophy. Also, they emphasize the complex nature of the adaptive changes that occur in these types of muscles as a result of overload.

Exercise-induced cellular alterations in the diaphragm

1992 ◽  
Vol 263 (5) ◽  
pp. R1093-R1098 ◽  
Author(s):  
S. K. Powers ◽  
D. Criswell ◽  
F. K. Lieu ◽  
S. Dodd ◽  
H. Silverman
Keyword(s):  
Exercise Training ◽  
Endurance Training ◽  
Fiber Type ◽  
Capillary Density ◽  
Oxidative Capacity ◽  
Control Group ◽  
Type I ◽  
Fiber Types ◽  
Image Analysis System ◽  
Cross Sectional

Limited data exist concerning the effects of exercise training on cellular oxidative capacity in the diaphragm of senescent animals. In this study we examined the changes in cellular oxidative capacity, muscle cell cross-sectional area (CSA), and capillarity within the costal diaphragm of senescent animals after a 10-wk endurance-training program. Twelve 24-mo-old female Fischer 344 rats were divided into either a sedentary control group (n = 6) or exercise training group (n = 6). The trained animals exercised on a motor-driven treadmill (60 min/day, 5 days/wk) at a work rate equal to approximately 55-65% VO2max. Capillaries were identified histologically and fiber types determined using adenosinetriphosphatase (ATPase) histochemistry. Succinate dehydrogenase (SDH) activity and CSA in individual fibers were measured using a computerized image analysis system. Exercise training did not increase (P > 0.05) the capillary-to-fiber ratio for any fiber type. However, training significantly decreased CSA (P < 0.05) and increased capillary density (capillary number/CSA) (P < 0.05) in type I, type IIa, and type IIb fibers. Furthermore, exercise training resulted in small but significant increase in SDH activity (P < 0.05) in type I and IIa fibers, whereas training did not alter SDH activity (P > 0.05) in type IIb fibers. These data demonstrate that endurance training in senescent animals results in small relative improvements in both oxidative capacity and capillary density in costal diaphragmatic type I and IIa muscle fibers. The increase in both capillary density and fiber SDH activity was largely due to a reduction in fiber CSA.

Muscle-specific and inducible expression of 293-base pair beta-myosin heavy chain promoter in transgenic mice

1996 ◽  
Vol 271 (3) ◽  
pp. R688-R695 ◽  
Author(s):  
J. L. Wiedenman ◽  
G. L. Tsika ◽  
L. Gao ◽  
J. J. McCarthy ◽  
I. D. Rivera-Rivera ◽  
...  
Keyword(s):  
Myosin Heavy Chain ◽  
Heavy Chain ◽  
Specific Activity ◽  
Fiber Type ◽  
Regulatory Element ◽  
Histochemical Staining ◽  
Regulatory Sequences ◽  
Type I ◽  
Adult Mice ◽  
Mechanical Overload

The DNA regulatory element(s) involved in beta-myosin heavy chain (beta-MHC) induction by the physiological stimulus of mechanical overload have not been identified as yet. To delineate regulatory sequences that are required for mechanical overload induction of the beta-MHC gene, transgenic mouse lines were generated that harbor transgenes containing serial deletions of the human beta-MHC promoter to nucleotides -293 (beta 293), -201 (beta 201), and -141 (beta 141) from the transcription start site (+1). Mechanically overloaded adult plantaris and soleus muscles contained 11- and 1.9-fold increases, respectively, in endogenous beta-MHC-specific mRNA transcripts (Northern blot) compared with sham-operated controls. Expression assays (chloramphenicol acetyltransferase specific activity) revealed that only transgene beta 293 expression was muscle specific in both fetal and adult mice and was induced in the plantaris (10- to 27-fold) and soleus (2- to 2.5-fold) muscles by mechanical overload. Histochemical staining for myosin adenosinetriphosphatase activity revealed a fiber-type transition of type II to type I in the overloaded plantaris and soleus muscles. These transgenic data suggest that sequences located between nucleotides -293 and +120 may be sufficient to regulate the endogenous beta-MHC gene in response to developmental signals and to the physiological signals generated by mechanical overload in fast- and slow-twitch muscles.

scholarly journals Calcineurin plays a modulatory role in loading-induced regulation of type I myosin heavy chain gene expression in slow skeletal muscle

2009 ◽  
Vol 297 (4) ◽  
pp. R1037-R1048 ◽  
Author(s):  
Clay E. Pandorf ◽  
Weihua H. Jiang ◽  
Anqi X. Qin ◽  
Paul W. Bodell ◽  
Kenneth M. Baldwin ◽  
...  
Keyword(s):  
Gene Expression ◽  
Skeletal Muscle ◽  
Myosin Heavy Chain ◽  
Heavy Chain ◽  
Fiber Type ◽  
Hindlimb Suspension ◽  
Chain Gene ◽  
Type I ◽  
Thyroid State

The role of calcineurin (Cn) in skeletal muscle fiber-type expression has been a subject of great interest because of reports indicating that it controls the slow muscle phenotype. To delineate the role of Cn in phenotype remodeling, particularly its role in driving expression of the type I myosin heavy chain (MHC) gene, we used a novel strategy whereby a profound transition from fast to slow fiber type is induced and examined in the absence and presence of cyclosporin A (CsA), a Cn inhibitor. To induce the fast-to-slow transition, we first subjected rats to 7 days of hindlimb suspension (HS) + thyroid hormone [triiodothyronine (T3)] to suppress nearly all expression of type I MHC mRNA in the soleus muscle. HS + T3 was then withdrawn, and rats resumed normal ambulation and thyroid state, during which vehicle or CsA (30 mg·kg−1·day−1) was administered for 7 or 14 days. The findings demonstrate that, despite significant inhibition of Cn, pre-mRNA, mRNA, and protein abundance of type I MHC increased markedly during reloading relative to HS + T3 ( P < 0.05). Type I MHC expression was, however, attenuated by CsA compared with vehicle treatment. In addition, type IIa and IIx MHC pre-mRNA, mRNA, and relative protein levels were increased in Cn-treated compared with vehicle-treated rats. These findings indicate that Cn has a modulatory role in MHC transcription, rather than a role as a primary regulator of slow MHC gene expression.

Capillarity and fiber types in the cremaster muscle of rat and hamster

1983 ◽  
Vol 245 (2) ◽  
pp. H368-H374 ◽  
Author(s):  
I. H. Sarelius ◽  
L. C. Maxwell ◽  
S. D. Gray ◽  
B. R. Duling
Keyword(s):  
Muscle Fiber ◽  
Fiber Type ◽  
Succinic Dehydrogenase ◽  
Capillary Density ◽  
Type I ◽  
Fiber Types ◽  
Cremaster Muscle ◽  
Muscle Area ◽  
Cross Sectional

We determined muscle fiber type and capillarity in cremaster muscle samples from rats and hamsters of different ages. Histochemical estimation of oxidative capacity was made from the activity of either nicotinamide dinucleotide tetrazolium reductase (NADH-TR) or succinic dehydrogenase (SDH), and fibers were termed fast or slow from myofibrillar ATPase activity. Fibers were classified as type I (low ATPase, high NADH-TR/SDH), type IIa (high ATPase, high SDH/NADH-TR), type IIb (high ATPase, low SDH/NADH-TR), or type IIc (no acid reversal of ATPase, high NADH-TR). Type IIb fibers accounted for 60-80% of the muscle area in both species at all ages. The principal change with maturation was muscle fiber hypertrophy. Mean cross-sectional fiber area increased from 488 +/- 70 (SE) and 453 +/- 19 micron2 in young hamsters and rats, respectively, to 1,255 +/- 99 and 1,540 +/- 101 micron2 in adults. Capillary density (no. of capillaries/mm2 tissue) paralleled fiber hypertrophy; it decreased significantly with maturation from 684 +/- 60 (SE) to 228 +/- 26/mm2 in hamsters and from 341 +/- 15 to 213 +/- 15/mm2 in rats. In vitro estimates of capillary density are compared with previously obtained in vivo data (31), and sources of error are identified. We conclude that reported differences in microvascular function in the cremaster muscle in vivo during maturation or between species cannot be ascribed to changes in muscle composition.

Sign in / Sign up

Export Citation Format

Share Document