Reinnervation of denervated extensor digitorum longus of the rat by the nerve of the soleus does not induce the type I myosin synthesis directly but through a sequential transition of type II myosin isoforms

Mira, Jean‐Claude; Janmot, Chantal; Couteaux, R; d’Albis, Anne

doi:10.1016/0304-3940(92)90899-i

Cited by 24 publications

(21 citation statements)

References 14 publications

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“…A sequential exchange of fast myosin heavy chain isoforms has previously been shown in low-frequency-stimulated fast-twitch muscle of the rat [5]. A similar sequential transition of fast myosin isoforms was observed in rat fast-twitch extensor digitorum longus muscle after denervation and reinnervation by the nerve of the soleus muscle [23]. In the present study, the changes in myosin heavy chain isoforms follow the order HCIId+HCIIa+HCI.…”

Section: Discussionsupporting

confidence: 62%

Coordinate changes in the expression of troponin subunit and myosin heavy‐chain isoforms during fast‐to‐slow transition of low‐frequency‐stimulated rabbit muscle

Leeuw

Pette

1993

European Journal of Biochemistry

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The purpose of this study was to follow the time course of changes in the expression of myosin heavy chain (HC) and troponin (Tn) subunit isoforms during fast-to-slow transition as induced in rabbit fast-twitch muscle by low-frequency stimulation. The evaluation of changes in the relative concentrations of myosin and troponin subunit isoforms were supplemented by measurements of relative protein synthesis rates using an in situ labeling technique. Changes in the amounts of mRNA encoding fast troponin C (TnC) were followed by Northern blot analysis, those for fast and slow troponin I (TnI) by in vitro translation of total RNA. The various fast myosin heavy chain (HC) and fast troponin T (TnT) isoforms were exchanged sequentially. Myosin HCIId which is the predominant fast isoform in rabbit tibialis anterior, was exchanged with HCIIa and, finally, the latter was replaced by the slow myosin HCI. The replacement of HCIId by HCIIa was accompanied by an exchange of TnT,, and TnT,, with TnT,,. The expression of HCI was accompanied by an exchange of TnT,, with the slow TnT isoforms, TnT,, and TnT,,. The changes in the relative concentrations of the TnT isoforms were preceded by similar changes of their relative synthesis rates. Pronounced decreases in the fast TnI and TnC isoforms occurred only with prolonged stimulation and were preceded by changes of the specific mRNAs and decreases in relative synthesis rates. The parallel time courses of the sequential transitions in both the myosin heavy chain and troponin T isoforms suggest the existence of coordinate programs of expression serving specific functional requirements.Numerous studies have shown that mammalian fasttwitch muscles can be converted into slow-twitch muscles by low-frequency stimulation. The stimulation-induced transformation affects all elements of the muscle fiber studied to date (for review see [l, 21). At the level of the myofibrillar apparatus, chronic low-frequency stimulation induces fast-toslow transitions in the expression of thick and thin filament proteins. Studies on rabbit muscle showed changes in the myosin heavy chain pattern, such that long-term-stimulated fast-twitch muscles ultimately expressed the slow myosin heavy chain, HCI [3,4]. Time course studies including single fiber analyses on muscles of rat and rabbit revealed that the fast-to-slow fiber type transition was preceded by sequential exchanges of the various fast myosin heavy chain isoforms [4, 51. Fast-to-slow transitions were also observed for the three troponin (Tn) subunits, i.e., troponin T (TnT), troponin I (TnI), and troponin C (TnC). In the case of TnT, the changes consisted of sequential transitions in the expression of the major fast TnT isoforms, TnT,, TnTzh TnT,, and TnT,, Correspondence to D. Pette, Fakultat fur Biologie, UniversitatFax: +49 753188 39 40. Abbreviations. HC, heavy chain; Tn, troponin; TnC, troponin C; TnC,, fast troponin C; TnC,, slow troponin C ; TnI, troponin I; TnI,, fast troponin I; TnI,, slow troponin I; TnT, troponin T ; TnT,, TnT,, TnT3f, TnT,,,...

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Section: Discussionsupporting

confidence: 62%

Coordinate changes in the expression of troponin subunit and myosin heavy‐chain isoforms during fast‐to‐slow transition of low‐frequency‐stimulated rabbit muscle

Leeuw

Pette

1993

European Journal of Biochemistry

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“…These changes especially concern their metabolic properties (Buchegger et al, 1984;Gundersen et al, 1988;Pette and Tyler, 1983) and their contractile characteristics (Eccles, 1967;Lemo et al, 1974;Salmons and SrCter, 1976;Westgaard and Lemo, 1988). The latter are associated with transformations of the myosin isoform spectrum (Ausoni et al, 1990;Brown et al, 1983;Mabuchi et al, 1982;Mira et al, 1992;SrCter et al, 1975;Srihari et al, 1981 ;Termin and Pette, 1992;Weeds et al, 1974) as well as of the regulatory proteins of myofilaments (for review, see Pette and Vrbovi, 1992).…”

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confidence: 99%

Expression of Myosin Isoforms in Denervated, Cross‐Reinnervated, and Electrically Stimulated Rabbit Muscles

Bacou¹,

Rouanet

Barjot³

et al. 1996

European Journal of Biochemistry

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The expression of myosin heavy (MyHC) and light (MyLC) chain isoforms was analyzed after denervation and cross-reinnervation by a fast nerve of the slow-twitch Semimembranosus proprius (SMp) muscle, and after denervation and electrical stimulation at low frequency of the fast-twitch Semimembranosus accessorius (SMa) muscle of the rabbit. The control SMp (100% type I fibers) expressed 100% type I MyHC and 100% slow-type (lS', 1s and 2s) MyLC isoforms. Five month denervation did not alter significantly the MyHC expression of the muscle, but induced the expression of a new type 1 MyLC corresponding most probably to an embryonic MyLC. Five-month cross-reinnervation of the SMp by the fast SMa nerve induced a large change of its fiber type properties. As shown by immunocytochemistry, almost all fibers were stained by fast myosin antibody, but a high proportion of them co-expressed slow myosin. This result was in agreement with biochemical data showing that fast MyHC and MyLC isoforms became predominant. The control SMa (nearly 100% type 11 fibers) expressed almost 100% type I1 MyHC (70% type IIb and 22% IIx/d) and 100% fast-type (IF, 2F and 3F) MyLC isoforms. Five month denervation of the SMa induced a shift in its MyHC, with 98 % type 1Idd and 2 % type IIb isoforms, and no change in the proportions of its MyLC. Three month electrical stimulation at 10 Hz of the SMa transformed its fiber type composition. All fibers reacted with the slow myosin antibody and a minor proportion of them were stained by the fast myosin antibody. These observations were in agreement with the biochemical analysis showing a large predominance of the slow-type MyHC and MyLC isoforms. Taken together, these results obtained from rabbit muscles which are normally homogeneous in either fast-twitch or slow-twitch fiber types, further support the idea that the different myosin isoforms, particularly the MyHC, are differentially regulated by motor innervation. Type I MyHC is maintained in denervated SMp muscle, but is not expressed in denervated SMa. Type IIb isoform is the most sensitive to neural influence, as it disappears rapidly in denervated and electrically stimulated fast-twitch SMa muscle, and is barely expressed in cross-reinnervated slow-twitch SMp muscle. In contrast, type IIa and type IIdd are less dependent upon motor innervation. In addition to the previous studies of d'Albis et al.[d'Albis, A., Gouble, F., Couteaux, R., Jannot, C. & Mira, J. C. (1994) Eur. J. Biochem. 223, 241-2581, analysis of these results leads us to conclude that, in the rabbit, sensitivity to motor innervation increases from the glycolytic to the oxydative types of fibers, in the order IIB > IIX/IID > IIA > I.

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“…MHC separated electrophoretically ference in the expression of MLC isoforms appeared from EDL using 5-8% SDS-PAGE displayed two isoin the ''standard'' and the ''nerve-intact'' grafts. 23 and principally by Jakubiec-Puka et 4A), while in the ''nerve-intact'' grafts the results al.…”

Section: Resultsmentioning

confidence: 89%

“…They suggested that tively. 23,27 The composition of MHC as well as MLC isoforms determines the shortening velocity of musthe induction of slow myosin phenotype in regenerating soleus muscle is dependent on the positive influcle fibers.…”

Section: Resultsmentioning

confidence: 99%

The effect of autografting on the myosin composition in skeletal muscle fibers

1997

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The purpose of the study was to investigate the changes in myosin heavy chain (MHC) and myosin light chain (MLC) isoforms following autotransplantation of extensor digitorum longus muscles. Muscles were grafted in “standard” and “nerve‐intact” conditions. MHC and MLC isoforms were analyzed by sodium dodecyl sulphate gel electrophoresis. Changes in MHC isoforms 10, 30, and 60 days after grafting were similar in the “standard” and the “nerve‐intact” grafts. In contrast to MHC, changes in MLC were different in the 10th day groups, but the same in the 30th day groups. Sixty days after grafting the content of MLC isoforms was the same as the control muscles. These data indicate that transient loss of functional innervation, even for a short time, has permanent effect on the composition of MHC but not MLC isoforms in regenerating skeletal muscle fibers. © 1997 John Wiley & Sons, Inc. Muscle Nerve, 20, 718–727, 1997.

show abstract

Reinnervation of denervated extensor digitorum longus of the rat by the nerve of the soleus does not induce the type I myosin synthesis directly but through a sequential transition of type II myosin isoforms

Cited by 24 publications

References 14 publications

Coordinate changes in the expression of troponin subunit and myosin heavy‐chain isoforms during fast‐to‐slow transition of low‐frequency‐stimulated rabbit muscle

Coordinate changes in the expression of troponin subunit and myosin heavy‐chain isoforms during fast‐to‐slow transition of low‐frequency‐stimulated rabbit muscle

Expression of Myosin Isoforms in Denervated, Cross‐Reinnervated, and Electrically Stimulated Rabbit Muscles

The effect of autografting on the myosin composition in skeletal muscle fibers

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