Masticatory (;superfast') myosin heavy chain and embryonic/atrial myosin light chain 1 in rodent jaw-closing muscles.
نویسندگان
چکیده
Masticatory myosin is widely expressed among several vertebrate classes. Generally, the expression of masticatory myosin has been associated with high bite force for a carnivorous feeding style (including capturing/restraining live prey), breaking down tough plant material and defensive biting in different species. Masticatory myosin expression in the largest mammalian order, Rodentia, has not been reported. Several members of Rodentia consume large numbers of tree nuts that are encased in very hard shells, presumably requiring large forces to access the nutmeat. We, therefore, tested whether some rodent species express masticatory myosin in jaw-closing muscles. Myosin isoform expression in six Sciuridae species was examined, using protein gel electrophoresis, immunoblotting, mass spectrometry and RNA analysis. The results indicate that masticatory myosin is expressed in some Sciuridae species but not in other closely related species with similar diets but having different nut-opening strategies. We also discovered that the myosin light chain 1 isoform associated with masticatory myosin heavy chain, in the same four Sciuridae species, is the embryonic/atrial isoform. We conclude that rodent speciation did not completely eliminate masticatory myosin and that its persistent expression in some rodent species might be related to not only diet but also to feeding style.
منابع مشابه
The myosin light chain 1 isoform associated with masticatory myosin heavy chain in mammals and reptiles is embryonic/atrial MLC1.
We recently reported that masticatory myosin heavy chain (MHC-M) is expressed as the exclusive or predominant MHC isoform in masseter and temporalis muscles of several rodent species, contrary to the prevailing dogma that rodents express almost exclusively MHC isoforms that are typically found in fast limb muscles and not masticatory myosin. We also reported that the same rodent species express...
متن کامل'Superfast' or masticatory myosin and the evolution of jaw-closing muscles of vertebrates.
There are four fibre types in mammalian limb muscles, each expressing a different myosin isoform that finely tunes fibre mechanics and energetics for locomotion. Functional demands on jaw-closer muscles are complex and varied, and jaw muscles show considerable phylogenetic plasticity, with a repertoire for myosin expression that includes limb, developmental, alpha-cardiac and masticatory myosin...
متن کاملPatterns of tropomyosin and troponin-T isoform expression in jaw-closing muscles of mammals and reptiles that express masticatory myosin.
We recently reported that masticatory ('superfast') myosin is expressed in jaw-closing muscles of some rodent species. Most mammalian limb muscle fibers express tropomyosin-β (Tm-β), along with fast-type or slow-type tropomyosin-β (Tm-β), but jaw-closing muscle fibers in members of Carnivora express a unique isoform of Tm [Tm-masticatory (Tm-M)] and little or no Tm-β. The goal of this study was...
متن کاملRegulation of jaw-specific isoforms of myosin-binding protein-C and tropomyosin in regenerating cat temporalis muscle innervated by limb fast and slow motor nerves.
Cat jaw-closing muscles are a distinct muscle allotype characterized by the expression of masticatory-specific myofibrillar proteins. Transplantation studies showed that expression of masticatory myosin heavy chain (m-MyHC) is promoted by fast motor nerves, but suppressed by slow motor nerves. We investigated whether masticatory myosin-binding protein-C (m-MBP-C) and masticatory tropomyosin (m-...
متن کاملThe masticatory system under varying functional load. Part 1: Structural adaptation of rabbit jaw muscles to reduced masticatory load.
Skeletal muscle fibres can change their myosin heavy-chain (MyHC) isoform and cross-sectional area, which determine their contraction velocity and maximum force generation, respectively, to adapt to varying functional loads. In general, reduced muscle activity induces transition towards faster fibres and a decrease in fibre cross-sectional area. In order to investigate the effect of a reduction...
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ورودعنوان ژورنال:
- The Journal of experimental biology
دوره 212 Pt 16 شماره
صفحات -
تاریخ انتشار 2009