Differential distribution of tropomyosin subunits in fast and slow rat muscles and its changes in long‐term denervated hemidiaphragm

Carraro, Ugo; Catani, Claudia; Libera, Luciano Dalla; Vascon, M.; Zanella, G.

doi:10.1016/0014-5793(81)80088-9

Cited by 24 publications

(10 citation statements)

References 22 publications

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“…The discrepancy is possibly due to the use of different methods (2D gel vs. MS) and there might also be a difference in the age and strain used. Nevertheless, our results show an increasing percentage of Tpm1.1: Tpm2.2 ratio in rat diaphragm compared to soleus, which agrees with the trend in the study by Carraro et al (Carraro et al 1981). The ratio of Tpm1.1:Tpm2.2 in rat soleus muscle is also evaluated by 1D SDS-PAGE.…”

Section: Resultssupporting

confidence: 94%

“…The ratio of Tpm1.1:Tpm2.2 appears to be muscle-type dependent based on our results and previous studies (Carraro et al 1981; Lees-Miller and Helfman 1991; Peng et al 2013a). Previous studies have demonstrated that Tpm1.1 isoform is dominant in cardiac and fast twitch skeletal muscles whereas Tpm2.2 isoform is prominent in slow twitch muscles (Lees-Miller and Helfman 1991).…”

Section: Resultssupporting

confidence: 88%

“…In previous study of rat skeletal muscles, Carraro et al used two-dimensional gel electrophoresis to quantify the relative abundances of Tpm1.1 and Tpm2.2 in rat soleus and diaphragm (Carraro et al 1981). Their results showed that the ratio of Tpm1.1: Tpm2.2 in rat soleus is 0.26:1 and that in rat diaphragm is 0.99:1.…”

Section: Resultsmentioning

confidence: 99%

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Comprehensive analysis of tropomyosin isoforms in skeletal muscles by top-down proteomics

Jin

Peng

Lin

et al. 2016

J Muscle Res Cell Motil

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Mammalian skeletal muscles are heterogeneous in nature and are capable of performing various functions. Tropomyosin (Tpm) is a major component of the thin filament in skeletal muscles and plays an important role in controlling muscle contraction and relaxation. Tpm is known to consist of multiple isoforms resulting from different encoding genes and alternative splicing, along with post-translational modifications. However, a systematic characterization of Tpm isoforms in skeletal muscles is still lacking. Therefore, we employed top-down mass spectrometry (MS) to identify and characterize Tpm isoforms present in different skeletal muscles from multiple species, including swine, rat, and human. Our study revealed that Tpm1.1 and Tpm2.2 are the two major Tpm isoforms in swine and rat skeletal muscles, whereas Tpm1.1, Tpm2.2, and Tpm3.12 are present in human skeletal muscles. Tandem MS was utilized to identify the sequences of the major Tpm isoforms. Furthermore, quantitative analysis revealed muscle-type specific differences in the abundance of un-modified and modified Tpm isoforms in rat and human skeletal muscles. This study represents the first systematic investigation of Tpm isoforms in skeletal muscles, which not only demonstrates the capabilities of top-down MS for the comprehensive characterization of skeletal myofilament proteins but also provides the basis for further studies on these Tpm isoforms in muscle-related diseases.

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Section: Resultssupporting

confidence: 94%

Section: Resultssupporting

confidence: 88%

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Comprehensive analysis of tropomyosin isoforms in skeletal muscles by top-down proteomics

Jin

Peng

Lin

et al. 2016

J Muscle Res Cell Motil

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“…There are two main isoforms of tropomyosin in mammalian skeletal muscle. Fast-twitch fibres contain predominantly a-tropomyosin while slow-twitch fibres contain more fl-tropomyosin (Cummins & Perry, 1974;Carraro et al 1981;Smillie, 1982). /f-Tropomyosin contains a higher proportion of cysteine (Cummins & Perry, 1974) and could therefore be more likely to be functionally affected by DTNB.…”

Section: Discussionmentioning

confidence: 99%

“…Since the number and properties of the sulphydryls on different isotypes of the contractile proteins are known to vary (Cummins & Perry, 1974;Carraro, Catani, Dalla Libera, Vascon & Zanella, 1981;Smillie, 1982;Wagner, 1982) it was of interest MYOFIBRILLAR SLULPHYDR YL MODIFICATION to compare the effects of DTNB upon different muscle fibre types. The rat soleus and the rat extensor digitorum longus (EDL) muscles were therefore used to obtain slowtwitch and fast-twitch skeletal muscle fibres respectively (Stephenson & Williams, 1981).…”

Section: Introductionmentioning

confidence: 99%

Effects of sulphydryl modification on skinned rat skeletal muscle fibres using 5,5'‐dithiobis(2‐nitrobenzoic acid).

Wilson

Remedios

Stephenson

et al. 1991

The Journal of Physiology

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SUMMARY1. The sulphydryl groups of skinned skeletal muscle fibres have been reacted with 5,5'-dithiobis(2-nitrobenzoic acid) (DTNB) in order to determine whether the effects of modifications to the contractile proteins are reflected in changes in the physiological properties of the contractile apparatus and Ca2+-regulatory system. 2. Results obtained from fast-twitch and slow-twitch rat fibres which were treated with DTNB (10 mm, pH 8-6, 5 C) for various periods of time under relaxing conditions showed that a major effect of the modification was to reduce the level of maximally Ca2+-activated force and fibre stiffness. Force and fibre stiffness were found to decline in proportion. Treatment with DTNB under these conditions did not cause a rise in force or fibre stiffness in relaxed fibres of either type.3. The effects induced by DTNB under relaxing conditions were substantially reversed by exposure to the reducing agent dithiothreitol (DTT) (10 mM, pH 741, 23°C). Force abolished by 30-35 s treatment with DTNB recovered after subsequent DTT treatment to 67+3 % (mean + S.E.M., n = 4) in fast-twitch fibres and to 91 + 2 % (n = 7) in slow-twitch fibres. These results were significantly different (t test, P < 0f001) indicating that the level of force recovery depended upon the fibre type.4. DTNB was found to affect not only the maximal Ca2+-activated force, but also the force-pCa (pCa = -logl0[Ca2+]) relationships of the fibres in a complex, fibretype specific way. DTT treatment partially reversed these DTNB effects. 5. The skinned fibre preparations reacted differently with DTNB under rigor conditions than under relaxing conditions, indicating that rigor modifies the reactivity of the functional sulphydryl groups to the thiol-targeted agents.6. When superprecipitation assays (an in vitro analogue of fibre contraction) were

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Long‐term reiention of regenerative capability after denervation of skeletal muscle, and dependency of late differentiation on innervation

Gulati

1988

Anat. Rec.

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The present study examines the influence of denervation on the regenerative ability of skeletal muscle in rats. Muscle denervation was achieved by transecting and ligating the cut ends of the sciatic nerve. Four to 48 weeks after denervation, the extensor digitorum longus (EDL) muscle was autotransplanted to induce muscle regeneration. The transplanted EDL muscles were examined at 1-12 weeks. Normal (i.e., no prior denervation) EDL muscle autotransplants were also examined for comparison. Denervation resulted in progressive atrophy of muscle, marked by a reduction in the size of myofibers and an increase in endomysialperimysial connective tissue. In spite of these alterations, typical events of muscle regeneration were invariably observed after transplantation. Initial myofiber degeneration and subsequent regeneration of myotubes occurred in a manner similar to normal muscle transplants. However, only a partial maturation of myotubes was observed in denervated muscles. These results show that extended denervation does not abolish the capability for muscle regeneration. The precursor myosatellite cells, proposed to be responsible for muscle regeneration, retain their regenerative potential after denervation. It is concluded, however, that the presence of intact innervation is crucial for the terminal differentiation and maturation of regenerating muscle.

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Differential distribution of tropomyosin subunits in fast and slow rat muscles and its changes in long‐term denervated hemidiaphragm

Cited by 24 publications

References 22 publications

Comprehensive analysis of tropomyosin isoforms in skeletal muscles by top-down proteomics

Comprehensive analysis of tropomyosin isoforms in skeletal muscles by top-down proteomics

Effects of sulphydryl modification on skinned rat skeletal muscle fibres using 5,5'‐dithiobis(2‐nitrobenzoic acid).

Long‐term reiention of regenerative capability after denervation of skeletal muscle, and dependency of late differentiation on innervation

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