Denervated skeletal muscle displays discoordinate regulation for the synthesis of several myofibrillar proteins.

Matsuda, Ryoichi; Spector, Dennis; Strohman, Richard C.

doi:10.1073/pnas.81.4.1122

Cited by 46 publications

(27 citation statements)

References 36 publications

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“…This suggests a potential role for innervation in regulation of MHC isoform protein expression. However, previous studies have suggested that innervation is not a requirement for the ultimate expression of adult fast MHC protein isoforms (6,8,27,32). Furthermore, during postnatal development of the rat Dia m , removal of innervation with unilateral denervation only delayed expression of fast MHC protein isoforms and prolonged expression of the MHC Neo protein isoform (39).…”

Section: Discussionmentioning

confidence: 99%

Mechanisms underlying myosin heavy chain expression during development of the rat diaphragm muscle

Geiger¹,

Bailey²,

Mantilla³

et al. 2006

Journal of Applied Physiology

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real-time reverse transcriptase-polymerase chain reaction; electrophoresis; myosin heavy chain gene regulation; muscle plasticity IN THE RAT DIAPHRAGM MUSCLE (Dia m ), significant changes in myosin heavy chain (MHC) isoform expression occur during the first 4 wk of postnatal development (22-24, 38, 39, 41). Most fibers express protein for the MHC Neo isoform at birth (P-0), but the relative expression of this isoform gradually decreases until it disappears by postnatal day 28 (P-28). In contrast, MHC 2X and MHC 2B protein isoforms are not expressed in the rat Dia m until at least the second postnatal week. Postnatal development of the rat Dia m is also characterized by changes in muscle contractile properties and by significant growth of muscle fibers, most notably those expressing MHC 2X and MHC 2B (15,22,36,38,42,43,45,47). Thus the relative MHC isoform composition changes during postnatal development of the Dia m , and ultimately it determines Dia m function. At the present time, very little is known about the underlying mechanisms regulating MHC phenotype expression.Previous studies of postnatal development, both in limb muscles and the Dia m , have focused exclusively on changes in the relative protein expression of the different MHC isoforms in the whole muscle (9, 11, 22-24, 30, 31, 33, 38, 39, 45). However, during postnatal development of the rat Dia m , MHC content (measured by MHC mass per half-sarcomere volume and fiber cross-sectional area) increases markedly (15). This increase varies across fiber types (classified based on MHC isoform expression). At single Dia m fibers, the developmental increase in MHC content is greater in fibers expressing MHC 2X and/or MHC 2B isoforms than in those expressing MHC Slow or MHC 2A . Thus, during postnatal development, not only do Dia m fibers increase in size but also they increase their MHC protein content. This substantial increase in total MHC protein expression across Dia m fiber types is not evident if only the relative expression of MHC isoform is examined.The period from birth to adulthood provides a unique and significant opportunity to examine the mechanisms underlying rapid muscle growth and phenotype transitions. In rat limb muscles, postnatal muscle phenotype is regulated by MHC gene expression either as a result from mechanical stretch induced by skeletal growth and/or increased muscle activity (18). At present, there is no direct information regarding the transcriptional regulation of MHC isoform expression during postnatal development of the rat Dia m .An increase in MHC protein of the rat Dia m during postnatal development could be due to transcriptional, translational, and/or posttranslational mechanisms, which may vary depending on fiber type (10). Assuming transcriptional rate remains constant, an increase in mRNA expression would result in increased protein expression. For example, patterns of MHC isoform-specific mRNA and protein expression are very similar during postnatal development in pigs (25). We hypothesized that postnatal transitions ...

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Section: Discussionmentioning

confidence: 99%

Mechanisms underlying myosin heavy chain expression during development of the rat diaphragm muscle

Geiger¹,

Bailey²,

Mantilla³

et al. 2006

Journal of Applied Physiology

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“…Sur le plan métabolique, on observe, après dénervation, une diminution de la synthèse et une augmentation de la dégradation de la majeure partie des protéines intracellulaires (Padieu, 1959 ;Schapira et Dreyfus, 1959 ;Gutmann, 1962 (Gauthier et Carraro etal., 1985), tropomyosine, troponine et chaînes légères de la myosine évoluent vers des configurations embryonnaires (Dhoot et Perry, 1982 ;Matsuda et al, 1984a ;Obinata et al, 1984 ;Shimizu et Shimada, 1985).…”

Section: A) Propriétés Des Fibres Musculairesunclassified

Propriétés des fibres musculaires squelettiques. 1. Influence de l'innervation motrice

Bacou¹,

Vigneron²

1988

Reprod. Nutr. Dévelop.

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“…MHC isoform transitions have also been described during myogenesis in mouse (Weydert et al, 1983(Weydert et al, , 1987 and chicken (Bandman et al, 1982). Developing avian muscles exhibit isoform transitions in the MLCl gene family (Barton et al, 1988), the actin gene family (Hayward and Schwartz, 1986), and the tropomyosin (Tm) and troponin T (TnT) gene families (Matsuda et al, 1981(Matsuda et al, , 1984. Similarly, in mammals, embryonic isoform profiles differ from those of adult skeletal muscles for MLCl (Periasamy et al, 1984;Barton et al, 1988Barton et al, , 1989Lyons et al, 1990), actin (Buckingham, 1985), and TnT (Briggs et al, 1990;Saggin et al, 1990).…”

Section: Introductionmentioning

confidence: 99%

Identification of a program of contractile protein gene expression initiated upon skeletal muscle differentiation

Sutherland

Esser

Elsom

et al. 1993

Developmental Dynamics

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The functional diversity of skeletal muscle is largely determined by the combinations of contractile protein isoforms that are expressed in different fibers. Just how the developmental expression of this large array of genes is regulated to give functional phenotypes is thus of great interest. In the present study, we perform a comprehensive analysis of contractile protein isoform mRNA profiles in skeletal muscle systems representing each generation of fiber formed: primary, secondary, and regenerating fibers. We find that in each system examined there is a common pattern of isoform gene expression during early differentiation for 5 of the 6 gene families we have investigated: myosin light chain (MLCI1, MLC2, tropomyosin, troponin (Tn)C, and TnI. We suggest that the common isoform patterns observed together represent a genetic program of skeletal muscle differentiation that is independent of the mature fiber phenotype and is found in all newly formed myotubes. Within each of these contractile protein gene families the program is independent of the isoforms of myosin heavy chain (MHC) expressed. The maintenance of such a program may reflect a specific requirement of the initial differentiation process. 0 1993 Wiley-Liss, Inc.

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Denervated skeletal muscle displays discoordinate regulation for the synthesis of several myofibrillar proteins.

Cited by 46 publications

References 36 publications

Mechanisms underlying myosin heavy chain expression during development of the rat diaphragm muscle

Mechanisms underlying myosin heavy chain expression during development of the rat diaphragm muscle

Propriétés des fibres musculaires squelettiques. 1. Influence de l'innervation motrice

Identification of a program of contractile protein gene expression initiated upon skeletal muscle differentiation

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