Denervation of newborn rat muscles does not block the appearance of adult fast myosin heavy chain

Butler-Browne, Gillian; Bugaisky, Lawrence B.; Cuénoud, Sylvia; Schwartz, Ketty; Whalen, Robert G.

doi:10.1038/299830a0

Cited by 130 publications

(74 citation statements)

References 21 publications

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“…In accordance with these data, denervated slowtype soleus expressed exclusively the fast MHCIIX and IIB mRNAs in the regeneration process (Esser et al 1993;Jerkovic et al 1997). Other reports also suggest that IIB fibers develop in the absence of neural stimulation (Butler-Browne et al 1982;Schiaffino and Reggiani 1996;Fink et al 2003). Thus, the relatively small MHCIIB-expressing fibers, often located in the connective tissue-rich areas in our experiments, certainly represent denervated fibers that could not accomplish MHC transitions and growth.…”

Section: Discussionsupporting

confidence: 69%

Regeneration of Reinnervated Rat Soleus Muscle Is Accompanied by Fiber Transition Toward a Faster Phenotype

Mendler

Pintér

Kiricsi

et al. 2007

J Histochem Cytochem.

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S U M M A R Y The functional recovery of skeletal muscles after peripheral nerve transection and microsurgical repair is generally incomplete. Several reinnervation abnormalities have been described even after nerve reconstruction surgery. Less is known, however, about the regenerative capacity of reinnervated muscles. Previously, we detected remarkable morphological and motor endplate alterations after inducing muscle necrosis and subsequent regeneration in the reinnervated rat soleus muscle. In the present study, we comparatively analyzed the morphometric properties of different fiber populations, as well as the expression pattern of myosin heavy chain isoforms at both immunohistochemical and mRNA levels in reinnervated versus reinnervated-regenerated muscles. A dramatic slow-tofast fiber type transition was found in reinnervated soleus, and a further change toward the fast phenotype was observed in reinnervated-regenerated muscles. These findings suggest that the (fast) pattern of reinnervation plays a dominant role in the specification of fiber phenotype during regeneration, which can contribute to the long-lasting functional impairment of the reinnervated muscle. Moreover, because the fast II fibers (and selectively, a certain population of the fast IIB fibers) showed better recovery than did the slow type I fibers, the faster phenotype of the reinnervated-regenerated muscle seems to be actively maintained by selective yet undefined cues. (J Histochem Cytochem 56:111-123, 2008)

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Section: Discussionsupporting

confidence: 69%

Regeneration of Reinnervated Rat Soleus Muscle Is Accompanied by Fiber Transition Toward a Faster Phenotype

Mendler

Pintér

Kiricsi

et al. 2007

J Histochem Cytochem.

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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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“…Histochemical ATPase staining was performed as described [23] with preincubation at pH 4.3 carried out at room temperature for 40 min. Characterization of the neonatal myosin antibody and methods for antigen and antibody purification, solid phase enzyme immunoassay, immunoblotting and indirect immunofluorescence have already been described [15,24,25].…”

Section: Methodsmentioning

confidence: 99%

A developmentally regulated disappearance of slow myosin in fast‐type muscles of the mouse

et al. 1984

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Histochemistry and immunocytochemistry using an antibody to adult rat slow-type myosin demonstrated that about 10% of the fibers in the mouse extensor digitorum longus and semimembranosus muscles contain slow myosin during the first month after birth. In adult animals, these muscles have only t&0.8% slow myosin-containing fibers. These results demonstrate a developmentally linked disappearance of an adult-type myosin, and show that the adult phenotype of muscle fibers is not necessarily determined before birth as previously suggested. Histochemistry Immunocytochemistry

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Denervation of newborn rat muscles does not block the appearance of adult fast myosin heavy chain

Cited by 130 publications

References 21 publications

Regeneration of Reinnervated Rat Soleus Muscle Is Accompanied by Fiber Transition Toward a Faster Phenotype

Regeneration of Reinnervated Rat Soleus Muscle Is Accompanied by Fiber Transition Toward a Faster Phenotype

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

A developmentally regulated disappearance of slow myosin in fast‐type muscles of the mouse

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