Autoantibodies in Canine Masticatory Muscle Myositis Recognize a Novel Myosin Binding Protein-C Family Member

Wu, Xiaohua; Li, Zhifang; Brooks, R. L.; Komives, Elizabeth A.; Torpey, Justin W.; Engvall, Eva; Gonias, Steven L.; Shelton, G. Diane

doi:10.4049/jimmunol.179.7.4939

Cited by 37 publications

(35 citation statements)

References 27 publications

(39 reference statements)

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“…In those species that have specialized fiber types in masticatory muscles, MyHC isoforms are not the only distinctive molecular sign of specialization. Other myofibrillar proteins such as myosin light chain 2 (630), tropomyosin (393,666) and myosin-binding protein C (MyBP-C) (393,882,891) are present in those fibers with isoforms specific for masticatory muscles.…”

Section: Head and Neck Musclesmentioning

confidence: 99%

Fiber Types in Mammalian Skeletal Muscles

Schiaffino

Reggiani

2011

Physiological Reviews

2,257

2,465

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Mammalian skeletal muscle comprises different fiber types, whose identity is first established during embryonic development by intrinsic myogenic control mechanisms and is later modulated by neural and hormonal factors. The relative proportion of the different fiber types varies strikingly between species, and in humans shows significant variability between individuals. Myosin heavy chain isoforms, whose complete inventory and expression pattern are now available, provide a useful marker for fiber types, both for the four major forms present in trunk and limb muscles and the minor forms present in head and neck muscles. However, muscle fiber diversity involves all functional muscle cell compartments, including membrane excitation, excitation-contraction coupling, contractile machinery, cytoskeleton scaffold, and energy supply systems. Variations within each compartment are limited by the need of matching fiber type properties between different compartments. Nerve activity is a major control mechanism of the fiber type profile, and multiple signaling pathways are implicated in activity-dependent changes of muscle fibers. The characterization of these pathways is raising increasing interest in clinical medicine, given the potentially beneficial effects of muscle fiber type switching in the prevention and treatment of metabolic diseases.

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Section: Head and Neck Musclesmentioning

confidence: 99%

Fiber Types in Mammalian Skeletal Muscles

Schiaffino

Reggiani

2011

Physiological Reviews

2,257

2,465

View full text Add to dashboard Cite

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“…There are indications that M MyHC combines with specific masticatory myosin light subunits (MyLC) (18) and integrates in the sarcomeric structure together with other specific masticatory isoforms as masticatory ␣-tropomyosin (22) and masticatory myosin-binding protein C (10,31,33). Although ATPase activity has been measured and found high both in M fibers (24) and in M myosin preparations (23), more limited information is available on the mechanical properties.…”

mentioning

confidence: 99%

Masticatory myosin unveiled: first determination of contractile parameters of muscle fibers from carnivore jaw muscles

Toniolo

Cancellara²,

Maccatrozzo³

et al. 2008

American Journal of Physiology-Cell Physiology

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Toniolo L, Cancellara P, Maccatrozzo L, Patruno M, Mascarello F, Reggiani C. Masticatory myosin unveiled: first determination of contractile parameters of muscle fibers from carnivore jaw muscles. Am J Physiol Cell Physiol 295: C1535-C1542, 2008. First published October 8, 2008 doi:10.1152/ajpcell.00093.2008.-Masticatory myosin heavy chain (M MyHC) is a myosin subunit isoform with expression restricted to muscles derived from the first branchial arch, such as jaw-closer muscles, with pronounced interspecies variability. Only sparse information is available on the contractile properties of muscle fibers expressing M MyHC (M fibers). In this study, we characterized M fibers isolated from the jaw-closer muscles (temporalis and masseter) of two species of domestic carnivores, the cat and the dog, compared with fibers expressing slow or fast (2A, 2X, and 2B) isoforms. In each fiber, during maximally calcium-activated contractions at 12°C, we determined isometric-specific tension (Po), unloaded shortening velocity (v o) with the slack test protocol, and the rate constant of tension redevelopment (KTR) after a fast shorteningrelengthening cycle. At the end of the mechanical experiment, we identified MyHC isoform composition of each fiber with gel electrophoresis. Electrophoretic migration rate of M MyHC was similar in both species. We found that in both species the kinetic parameters v o and KTR of M fibers were similar to those of 2A fibers, whereas Po values were significantly greater than in any other fiber types. The similarity between 2A and M fibers and the greater tension development of M fibers were confirmed also in mechanical experiments performed at 24°C. Myosin concentration was determined in single fibers and found not different in M fibers compared with slow and fast fibers, suggesting that the higher tension developed by M fibers does not find an explanation in a greater number of force generators. The specific mechanical characteristics of M fibers might be attributed to a diversity in cross-bridge kinetics.

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“…Due to their unique embryologic origin, these muscles contain type 2 M fibers and a type 1 fiber variant, which are not present in any other muscles in the body . The autoantigen in the masticatory myofibers has been determined to be the myosin heavy and light chains and a recently identified protein, myositigen, or masticatory myosin binding protein‐C (mMyBPC) . The pathogenesis of the disease remains unknown, but one theory for the initiation of autoimmunity includes molecular mimicry, whereby antibodies against an infectious agent cross‐react with the type 2 M myofibers of the masticatory muscles .…”

Section: Discussionmentioning

confidence: 99%