The expression of myosin heavy chain isoforms in normal and hypertrophied chicken slow muscle.

Kennedy, John M.; Kamel, S.; Tambone, W W; Vrbová, Gerta; Zak, Radovan

doi:10.1083/jcb.103.3.977

Cited by 72 publications

(61 citation statements)

References 27 publications

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“…The growth of the overloaded ALD was accompanied by a shift in the relative decrease of the slow myosin isozyme SM1 while no significant changes in the relative distribution of fast isomyosins in the overloaded PLD were detected ( fig.2). These data are consistent with a previous report [6].…”

Section: Resultssupporting

confidence: 94%

“…Overload hypertrophy was induced in 5 week-old male White Leghorn chicken by the application of a weight equivalent to 10°70 of the body mass to one wing as described previously [6]. The contralateral wing served as a control.…”

Section: Methodsmentioning

confidence: 99%

“…In this model, the chicken ALD undergoes rapid enlargeCorrespondence address: J. Gagnon, Dept of Medicine, The University of Chicago, 5841 South Maryland Ave, Chicago, IL 60637, USA Abbreviations: ALD, anterior latissimus dorsi muscle; PLD, posterior latissimus dorsi muscle; SMI, SM2, slow isomyosin 1, slow isomyosin 2; FMI, FM2, FM3, fast isomyosin 1, fast isomyosin 2, fast isomyosin 3; MHC, myosin heavy chain; MLC, myosin light chain; PP-PAGE, non-denaturing pyrophosphate-polyacrylamide gel electrophoresis; SDS-PAGE, denaturing sodium dodecyl sulfate-polyacrylamide gel electrophoresis ment accompanied by a change in isomyosin composition. The SM1 myosin isoform becomes gradually replaced by the SM2 band and three fastlike myosin bands, normally not present in this muscle, become transiently expressed during the early phase of the overload [5,6]. Using this model, we have found that the nascent fast-like myosin isoforms are first present in association with the polyribosomes and only later appear in the muscle extracts.…”

Section: Introductionmentioning

confidence: 99%

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Synthesis and assembly of native myosin on muscle polyribosomes

1989

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We have used the overload-induced growth of avian muscles to study the assembly of the newly synthetized myosins which were separated by non-denaturing pyrophosphate-polyacrylamide gel electrophoresis. Using this model, we have observed the appearance of fast-like isomyosins in polyribosomes prepared from slow anterior latissimus dorsi muscle after 72 h of overload. These new isoforms comigrating with native myosifi from fast posterior latissimus dorsi musclewere not yet present in cellular extracts from the same muscle. The in vitro translation system utilizing muscle specific polyribosomes directs the synthesis of the corresponding myosin isoforms. Under denaturing conditions, myosin heavy chains and light chains dissociate to the expected subunit composition of each specific isoform. The synthesis and assembly of native myosin on polyribosomes indicate that myosin exists as a single mature protein prior to the incorporation in the thick filament.Myosin isoform; Myosin heavy chain; Myosin light chain; Overload hypertrophy; (Chicken skeletal muscle)

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Section: Resultssupporting

confidence: 94%

Section: Methodsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Synthesis and assembly of native myosin on muscle polyribosomes

1989

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“…Mutant gastrocnemius muscle demonstrated an elevation in the M isoform of LDH, but physical activity decreased this enzyme as expected in response to exercise (16,28). An increase in COX activity was also detected in mutant gastrocnemius, but this elevation was modest if one takes into account the very low absolute mitochondrial content in glycolytic muscle.…”

Section: Discussionmentioning

confidence: 81%

Voluntary physical activity alterations in endothelial nitric oxide synthase knockout mice

Momken

Lechêne

Ventura‐Clapier

et al. 2004

American Journal of Physiology-Heart and Circulatory Physiology

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Momken, Iman, Patrick Lechêne, Renée Ventura-Clapier, and Vladimir Veksler. Voluntary physical activity alterations in endothelial nitric oxide synthase knockout mice. Am J Physiol Heart Circ Physiol 287: H914 -H920, 2004; 10.1152/ajpheart.00651.2003.-One of the main factors that control vasoreactivity and angiogenesis is nitric oxide produced by endothelial nitric oxide synthase (eNOS). We recently showed that knocking out eNOS induces an important reduction of mitochondrial oxidative capacity in slow-twitch skeletal muscle. Here we investigated eNOS's role in physical activity and contribution to adaptation of muscle energy metabolism to exercise conditions. Physical capacity of mice null for the eNOS isoform (eNOSϪ/Ϫ) was estimated for 8 wk with a voluntary wheel-running protocol. In parallel, we studied energy metabolism enzyme profiles and their response to voluntary exercise in cardiac and slow-twitch soleus (Sol) and fast-twitch gastrocnemius (Gast) skeletal muscles. Weekly averaged running distance was two times lower for eNOSϪ/Ϫ (4.09 Ϯ 0.42 km/day) than for wild-type (WT; 7.74 Ϯ 0.42 km/day; P Ͻ 0.01) mice. Average maximal speed of running was also lower in eNOSϪ/Ϫ (17.2 Ϯ 1.4 m/min) than WT (21.2 Ϯ 0.9 m/min; P Ͻ 0.01) mice. Voluntary exercise influenced adaptation to exercise specifically in Sol muscle. Physical activity significantly increased Sol weight by 22% (P Ͻ 0.05) in WT but not eNOSϪ/Ϫ mice. WT Sol muscle did not change its metabolic profile in response to exercise, in contrast to eNOSϪ/Ϫ muscle, in which physical activity decreased cytochrome-c oxidase (COX; Ϫ36%; P Ͻ 0.05), citrate synthase (Ϫ37%; P Ͻ 0.06), and creatine kinase (Ϫ24%, P Ͻ 0.01) activities. Voluntary exercise did not change energy enzyme profile in heart (except for 39% increase in COX activity in WT) or Gast muscle. These results suggest that eNOS is necessary for maintaining a suitable physical capacity and that when eNOS is downregulated, even moderate exercise could worsen energy metabolism specifically in oxidative skeletal muscle. muscles; exercise; mitochondria; energy metabolism MANY VASOREACTIVE FACTORS contribute to maintain adequate blood flow in muscles under different physiological conditions. One of the main factors that control vasoreactivity and angiogenesis is endothelium-derived NO (1,14,42). This substance is produced in a reaction catalyzed by NO synthase (NOS), transforming L-arginine to L-citrulline. Among the NOS isoenzymes-neuronal (nNOS), inducible (iNOS), and endothelial (eNOS)-the latter is the major isoform expressed in endothelial cells throughout the vascular bed. Mice lacking eNOS show reduced angiogenic ability (41), and inhibition of NOS has been shown to inhibit vascular remodeling in rabbits (51). In turn, it has been demonstrated that the microcirculation is a determinant of oxidative capacity in skeletal muscles (22,27), and severe reductions in blood flow have been shown to deleteriously affect muscle oxidative capacity and related enzyme activities (3, 4). Recent data directly showed a...

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“…A change in MHC isoform distribution has been seen in the rodent ventricle with hypothyroidism and in skeletal muscle after hypertroph y of chicken slow muscle from repeated use (19,27).…”

Section: Newborn Fundusmentioning

confidence: 99%

Characterization of Actin and Myosin in the Developing Stomach

1995

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During growth and development, dietary intake changes from being predominantly liquid in the newborn period to mixed solid liquid meals. These alterations in diet vary the functional demands placed on the stomach. It has been shown that, during development, smooth muscle of the stomach undergoes changes in the mechanism responsible for the contractile process. In this study, we have investigated the possibility that there are structural changes in two of the major proteins that are responsible for generation of force during smooth muscle contraction: actin and myosin. Actin and myosin were identified in newborn kittens (1 wk old) and adult gastric smooth muscle using one-dimensional SDS-PAGE. Although both the antrum and fundus of the kitten have significantly smaller total amounts of actin and myosin per mg protein than the adult, the ratio of actin to myosin is not significantly different between the age groups. Two different The changes in diet ary constitu ents during growth and development from predominantl y liquid to mixed solid liquid meals places an increasing burd en on the stomach that is required to triturate these solids and empty them from the stoma ch. The fundus or proxim al portion of the stomach is respon sibl e for the storage and empty ing of gastric food stuffs, whereas the antrum redu ces the size of ing ested solids and faci litates emptying (1). Th ere is a growing bod y of experiment al ev ide nce suggesting that functional characteristics of smoo th muscle in the sto mac h und ergo changes that parallel these alte rations in dietary mili eu. Th e frequ enc y and amplitude of contractions in the ca nine stoma ch increase during the newborn period (2). Th e in vitro force-generating capacit y of smoo th mu scle from the stomach of newborn rabbit s is less than that of adult gastri c muscl e, and this reduction in forcegeneratin g capacity did not appear to be accounted for by changes in receptor function (3,4). In addition to these quantitative differences in ability to ge nerate force, we have recentl y repo rted that isolated muscle ce lls from the antrum of the adult cat use intr acellular Ca 2 + stores that are not available for kitten antral cells (5). We observed an increase in the amount of MHC2 in the adult, which resulted in a decreased ratio of MHC1 to MHC2 in the adult. We postulate that the decreased quantity of actin and myosin in the kitten stomach and the observed changes in the ratio of the MHC isoforms are related to changes in the gastric motor that occur during growth and development. (Pediatr Res 37: 202-206, 1995) Abbreviations PMSF , phenylmethyl sulfanyl fluoride f3ME, f3-mercaptoethanol MHC , myosin heavy chain Actin and myo sin are two of the major structural proteins involved in the contractil e machinery of the cell. Th e generation of tension during muscle contraction is the result of the interaction between myos in heads and adjacent actin filaments (6). Previous studies have suggested that changes in the absolute amount and relative abundance of isoforms ...

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The expression of myosin heavy chain isoforms in normal and hypertrophied chicken slow muscle.

Cited by 72 publications

References 27 publications

Synthesis and assembly of native myosin on muscle polyribosomes

Synthesis and assembly of native myosin on muscle polyribosomes

Voluntary physical activity alterations in endothelial nitric oxide synthase knockout mice

Characterization of Actin and Myosin in the Developing Stomach

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