Histochemical and electrophoretic analysis of the primary flight muscle of several phyllostomid bats

1998 ◽  
Vol 76 (11) ◽  
pp. 1983-1992 ◽  
Author(s):  
John W Hermanson ◽  
James M Ryan ◽  
Matthew A Cobb ◽  
Jacqueline Bentley ◽  
William A Schutts, Jr.
Keyword(s):  
Myosin Heavy Chain ◽  
Heavy Chain ◽  
Fibre Type ◽  
Electrophoretic Analysis ◽  
Fibre Types ◽  
Type I ◽  
Myosin Isoforms ◽  
Pectoralis Muscle ◽  
Pectoralis Muscles ◽  
Artibeus Lituratus

We identify a novel histochemical fibre type that is correlated with a unique myosin heavy chain isoform in the pectoralis muscle of the two bats Artibeus lituratus and Carollia perspicillata (Phyllostomidae). Pectoralis muscles sampled from four other species (Phyllostomus hastatus, Platyrrhinus helleri, Glossophaga soricina, and Diaemus youngi) exhibited myosin heavy chain isoforms with electrophoretic properties identical with those of A. lituratus andC. perspicillata. The pectoralis muscles of A. lituratus and C. perspicillata consisted mainly of the newly described type IIe fibre. Diaemus youngi differed from the other species studied by having an FM5 native myosin isoform, a feature shared with Desmodus rotundus. We hypothesize that the two-fibre-type composition of the pectoralis muscle in the phyllostomid bats may be related to a "two-gear" locomotor strategy and represents a synapomorphy. The distribution of fibre types and myosin isoforms correlated with family-level phylogenetic affinity rather than with functional characteristics. One of the fibre types was identical with type IIa of terrestrial mammals and a correlated IIa isoform pattern upon electrophoretic analysis. The IIa fibres had high oxidative and glycolytic potential. The second fibre type, which we call type IIe, had a histochemical and immunocytochemical pattern inconsistent with interpretation as a type IIb muscle fibre. Electrophoretic analysis confirmed that isoforms correlated with IIe fibres migrated at different rates from type I, IIa, IIb, and IIx isoforms. The IIe fibres had a fast oxidative metabolic pattern and were at least twice as numerous as IIa fibres. Thus, a novel type IIe fibre is predominant in the pectoralis of six phyllostomid species that exhibit highly divergent body sizes and (or) flight styles.

scholarly journals Electrophoretic analysis of proteins from single bovine muscle fibres

1981 ◽  
Vol 195 (1) ◽  
pp. 317-327 ◽  
Author(s):  
O A Young ◽  
C L Davey
Keyword(s):  
Myosin Heavy Chain ◽  
Heavy Chain ◽  
Light Chain ◽  
Myosin Light Chain ◽  
Fibre Types ◽  
Type I ◽  
Slow Fibre ◽  
Slow Myosin ◽  
Fast Myosin ◽  
Fast Myosin Heavy Chain

A number of single fibres were isolated by dissection of four bovine masseter (ma) muscles, three rectus abdominis (ra) muscles and eight sternomandibularis (sm) muscles. By histochemical criteria these muscles contain respectively, solely slow fibres (often called type I), predominantly fast fibres (type II), and a mixture of fast and slow. The fibres were analysed by conventional sodium dodecyl sulphate/polyacrylamide-gel electrophoresis and the gels stained with Coomassie Blue. Irrespective of the muscle, every fibre could be classed into one of two broad groups based on the mobility of proteins in the range 135000-170000 daltons. When zones containing myosin heavy chain were cut from the single-fibre gel tracks and ‘mapped’ [Cleveland, Fischer, Kirschner & Laemmli (1977) J. Biol. Chem. 252, 1102-1106] with Staphylococcus proteinase, it was found that one group always contained fast myosin heavy chain, whereas the second group always contained the slow form. Moreover, a relatively fast-migrating alpha-tropomyosin was associated with the fast myosin group and a slow-migrating form with the slow myosin group. All fibres also contained beta-tropomyosin; the coexistence of alpha- and beta-tropomyosin is at variance with evidence that alpha-tropomyosin is restricted to fast fibres [Dhoot & Perry (1979) Nature (London) 278, 714-718]. Fast fibres containing the expected fast light chains and troponins I and C fast were identified in the three ra muscles, but in only four sm muscles. In three other sm muscles, all the fast fibres contained two troponins I and an additional myosin light chain that was more typical of myosin light chain 1 slow. The remaining sm muscle contained a fast fibre type that was similar to the first type, except that its myosin light chain 1 was more typical of the slow polymorph. Troponin T was bimorphic in all fast fibres from a ra muscles and in at least some fast fibres from one sm muscle. Peptide ‘mapping’ revealed two forms of fast myosin heavy chain distributed among fast fibres. Each form was associated with certain other proteins. Slow myosin heavy chain was unvarying in three slow fibre types identified. Troponin I polymorphs were the principal indicator of slow fibre types. The myofibrillar polymorphs identified presumably contribute to contraction properties, but beyond cud chewing involving ma muscle, nothing is known of the conditions that gave rise to the variable fibre composites in sm and ra muscles.

Force-velocity and force-power properties of single muscle fibers from elite master runners and sedentary men

1996 ◽  
Vol 271 (2) ◽  
pp. C676-C683 ◽  
Author(s):  
J. J. Widrick ◽  
S. W. Trappe ◽  
D. L. Costill ◽  
R. H. Fitts
Keyword(s):  
Myosin Heavy Chain ◽  
Heavy Chain ◽  
Power Output ◽  
Peak Power ◽  
Isometric Force ◽  
Peak Force ◽  
Peak Power Output ◽  
Type I ◽  
Shortening Velocity ◽  
Force Velocity

Gastrocnemius muscle fiber bundles were obtained by needle biopsy from five middle-aged sedentary men (SED group) and six age-matched endurance-trained master runners (RUN group). A single chemically permeabilized fiber segment was mounted between a force transducer and a position motor, subjected to a series of isotonic contractions at maximal Ca2+ activation (15 degrees C), and subsequently run on a 5% polyacrylamide gel to determine myosin heavy chain composition. The Hill equation was fit to the data obtained for each individual fiber (r2 > or = 0.98). For the SED group, fiber force-velocity parameters varied (P < 0.05) with fiber myosin heavy chain expression as follows: peak force, no differences: peak tension (force/fiber cross-sectional area), type IIx > type IIa > type I; maximal shortening velocity (Vmax, defined as y-intercept of force-velocity relationship), type IIx = type IIa > type I; a/Pzero (where a is a constant with dimensions of force and Pzero is peak isometric force), type IIx > type IIa > type I. Consequently, type IIx fibers produced twice as much peak power as type IIa fibers, whereas type IIa fibers produced about five times more peak power than type I fibers. RUN type I and IIa fibers were smaller in diameter and produced less peak force than SED type I and IIa fibers. The absolute peak power output of RUN type I and IIa fibers was 13 and 27% less, respectively, than peak power of similarly typed SED fibers. However, type I and IIa Vmax and a/Pzero were not different between the SED and RUN groups, and RUN type I and IIa power deficits disappeared after power was normalized for differences in fiber diameter. Thus the reduced absolute peak power output of the type I and IIa fibers from the master runners was a result of the smaller diameter of these fibers and a corresponding reduction in their peak isometric force production. This impairment in absolute peak power production at the single fiber level may be in part responsible for the reduced in vivo power output previously observed for endurance-trained athletes.

scholarly journals Myosins and pathology: genetics and biology.

2002 ◽  
Vol 49 (4) ◽  
pp. 789-804 ◽  
Author(s):  
Maria Jolanta Redowicz
Keyword(s):  
Hypertrophic Cardiomyopathy ◽  
Myosin Heavy Chain ◽  
Inner Ear ◽  
Heavy Chain ◽  
Hair Cells ◽  
Familial Hypertrophic Cardiomyopathy ◽  
Light Chains ◽  
Myosin Isoforms ◽  
Cardiac Myosin ◽  
Genes Encoding

This article summarizes current knowledge on the genetics and possible molecular mechanisms of Human pathologies resulted from mutations within the genes encoding several myosin isoforms. Mutations within the genes encoding some myosin isoforms have been found to be responsible for blindness (myosins III and VIIA), deafness (myosins I, IIA, IIIA, VI, VIIA and XV) and familial hypertrophic cardiomyopathy (beta cardiac myosin heavy chain and both the regulatory and essential light chains). Myosin III localizes predominantly to photoreceptor cells and is proved to be engaged in the vision process in Drosophila. In the inner ear, myosin I is postulated to play a role as an adaptive motor in the tip links of stereocilia of hair cells, myosin IIA seems to be responsible for stabilizing the contacts between adjacent inner ear hair cells, myosin VI plays a role as an intracellular motor transporting membrane structures within the hair cells while myosin VIIA most probably participates in forming links between neighbouring stereocilia and myosin XV probably stabilizes the stereocilia structure. About 30% of patients with familial hypertrophic cardiomyopathy have mutations within the genes encoding the beta cardiac myosin heavy chain and both light chains that are grouped within the regions of myosin head crucial for its functions. The alterations lead to the destabilization of sarcomeres and to a decrease of the myosin ATPase activity and its ability to move actin filaments.

Distribution of myosin heavy chain isoforms in non-weight-bearing rat soleus muscle fibers

1996 ◽  
Vol 81 (6) ◽  
pp. 2540-2546 ◽  
Author(s):  
Robert J. Talmadge ◽  
Roland R. Roy ◽  
V. Reggie Edgerton
Keyword(s):  
Myosin Heavy Chain ◽  
Soleus Muscle ◽  
Heavy Chain ◽  
De Novo ◽  
Weight Bearing ◽  
Muscle Fibers ◽  
Myosin Heavy Chain Isoforms ◽  
Hindlimb Suspension ◽  
Type I ◽  
Rat Soleus Muscle

Talmadge, Robert J., Roland R. Roy, and V. Reggie Edgerton.Distribution of myosin heavy chain isoforms in non-weight-bearing rat soleus muscle fibers. J. Appl. Physiol. 81(6): 2540–2546, 1996.—The effects of 14 days of spaceflight (SF) or hindlimb suspension (HS) (Cosmos 2044) on myosin heavy chain (MHC) isoform content of the rat soleus muscle and single muscle fibers were determined. On the basis of electrophoretic analyses, there was a de novo synthesis of type IIx MHC but no change in either type I or IIa MHC isoform proportions after either SF or HS compared with controls. The percentage of fibers containing only type I MHC decreased by 26 and 23%, and the percentage of fibers with multiple MHCs increased from 6% in controls to 32% in HS and 34% in SF rats. Type IIx MHC was always found in combination with another MHC or combination of MHCs; i.e., no fibers contained type IIx MHC exclusively. These data suggest that the expression of the normal complement of MHC isoforms in the adult rat soleus muscle is dependent, in part, on normal weight bearing and that the absence of weight bearing induces a shift toward type IIx MHC protein expression in the preexisting type I and IIa fibers of the soleus.

Rat diaphragm during postnatal development. I. Changes in distribution of muscle fibre type and in oxidative potential

1996 ◽  
Vol 8 (3) ◽  
pp. 391 ◽  
Author(s):  
MD Fratacci ◽  
M Levame ◽  
A Rauss ◽  
H Bousbaa ◽  
G Atlan
Keyword(s):  
Muscle Fibre ◽  
Fibre Type ◽  
Oxidative Capacity ◽  
Cross Sectional Area ◽  
Fibre Types ◽  
Type I ◽  
Sectional Area ◽  
Rat Diaphragm ◽  
Oxidative Potential ◽  
Cross Sectional

The changes occurring in the histochemical characteristics of the rat diaphragm during the postnatal period were examined. Fibre-type distribution, fibre oxidative capacity, i.e. succinate-dehydrogenase (SDH) activity, and cross-sectional area were compared in the costal (COS) and crural (CRU) regions, and across their abdominal and thoracic surfaces. The proportions of type I and IIb fibres in both COS and CRU increased with age, while the proportion of type IIa fibres progressively decreased. For COS, fibre distribution was homogeneous over the entire muscle and did not change after 4 weeks. For CRU, it was heterogeneous with a higher proportion of type I fibres on the thoracic surface as from the first week. All fibre types significantly increased in cross-sectional area between 1 and 8 weeks, with no significant differences in COS and CRU. Mean SDH activity did not differ between COS and CRU or across the muscles. Mean SDH activities-were low and identical in all fibre types at birth, and then increased, peaking at the 6th week in type I and IIa fibres. When total muscle fibre oxidative capacity was calculated from an index including fibre-type proportion, cross-sectional area and mean SDH activity, it was significantly higher at 1 than at 8 weeks after birth; this might have functional implications for the newborn.

Myosin heavy chain composition of skeletal muscles in young rats growing under hypobaric hypoxia conditions

2000 ◽  
Vol 88 (2) ◽  
pp. 479-486 ◽  
Author(s):  
A. X. Bigard ◽  
H. Sanchez ◽  
O. Birot ◽  
B. Serrurier
Keyword(s):  
Myosin Heavy Chain ◽  
Heavy Chain ◽  
Wheel Running ◽  
Barometric Pressure ◽  
Major Influence ◽  
Type I ◽  
Running Activity ◽  
Equivalent Quantity ◽  
Chain Composition ◽  
Myosin Heavy Chain Composition

This study investigated the effects of voluntary wheel running on the myosin heavy chain (MHC) composition of the soleus (Sol) and plantaris muscles (Pla) in rats developing under hypobaric choronic hypoxia (CH) conditions during 4 wk in comparison with those of control rats maintained under local barometric pressure conditions (C) or rats pair-fed an equivalent quantity of food to that consumed by CH animals (PF). Compared with C animals, sedentary rats subjected to CH conditions showed a significant decrease in type I MHC in Sol (−12%, P < 0.01). Although strongly decreased under hypoxia, spontaneous running activity increased the expression of type I MHC ( P < 0.01) so that no difference in the MHC profile of Sol was shown between CH active and C active rats. The MHC distribution in Sol of PF rats was not significantly different from that found in C animals. CH resulted in a significant decrease in type I ( P < 0.01) and type IIA ( P < 0.005) MHC, concomitant with an increase in type IIB MHC in Pla ( P < 0.001), compared with C and PF animals. In contrast to results in Sol muscle, this slow-to-fast shift in the MHC profile was unaffected by spontaneous running activity. These results suggest that running exercise suppresses the hypoxia-induced slow-to-fast transition in the MHC expression in Sol muscles only. The hypoxia-induced decrease in food intake has no major influence on MHC expression in developing rats.

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.

Type I Myosin Heavy Chain Expression Influences Motor Unit Behavior of the Vastus Lateralis

2016 ◽  
Vol 48 ◽  
pp. 406
Author(s):  
Michael A. Trevino ◽  
Eric M. Mosier ◽  
Jonathan D. Miller ◽  
Andrew C. Fry ◽  
Philip M. Gallagher ◽  
...  
Keyword(s):  
Myosin Heavy Chain ◽  
Motor Unit ◽  
Heavy Chain ◽  
Vastus Lateralis ◽  
Type I
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