The human tongue muscle hyoglossus (HG) muscle is active in oro-motor behaviors encompassing a wide range of tongue movement speeds. Here we test the hypothesis that the human HG is composed of “uncommon” myosin heavy chain (MHC) isoforms MHCembryonic, MHCneonatal and MHCslow tonic as has been reported for other head and neck muscles active during kinematically diverse behaviors. Following reaction of human HG with antibodies specific for MHCI, MHCIIA, MHCII, MHCembryonic, MHCextraocular, MHCneonatal and MHCslow tonic only antibodies to MHCI, MHCIIA and MHCIIA-X label more than occasional muscle fibers. These antibodies describe five phenotypes with prevalence MHCIIA>MHCI>MHCI-IIX>MHCI-IIA>MHCIIX. In MHC composition, the human HG is thus similar to human appendicular muscles, the human tongue muscle styloglossus and many human head and neck muscles but different from human masseter and extraocular muscles which contain five or more MHC isoforms.
Background The human tongue muscle genioglossus (GG) is active in speech, swallowing, respiration and oral transport, behaviors encompassing a wide range of tongue shapes and movement speeds. Studies demonstrate substantial diversity in patterns of human GG motor unit activation but whether this is accompanied by complex expression of muscle contractile proteins is not known. Purpose We tested for conventional myosin heavy chain MHCI, MHCIIA, MHCIIX, developmental MHCembryonic and MHCneonatal and unconventional MHCαcardiac, MHCextraocular and MHCslow tonic in antero-superior (GG-A) and posterior (GG-P) adult human GG. Method SDS-PAGE, Western blot and immunohistochemistry were used to describe MHC composition of GG-A and GG-P and the prevalence of muscle fiber MHC phenotypes in GG-A. Results: By SDS-PAGE, only conventional MHC are present with ranking from most to least prevalent MHCIIA>MHCI>MHCIIX in GG-A and MHCI>MHCIIA>MHCIIX in GG-P. By immunohistochemistry many muscle fibers contain MHCI, MHCIIA and MHCIIX but few contain developmental or unconventional MHC. GG-A is composed of five phenotypes (MHCIIA>MHCI-IIX>MHCI>MHCI-IIA>MHCIIX). Phenotypes MHCI, MHCIIA and MHCI-IIX account for 96% of muscle fibers. Conclusions Despite activation of GG during kinematically diverse behaviors and complex patterns of GG motor unit activity, the human GG is composed of conventional MHC isoforms and three primary MHC phenotypes.
Monensin in ruminant diets increases production of propionic acid. We have tested the hypothesis that propionic acid may be elevated to such an extent by monensin that it cannot be optimally metabolized by the methyl malonyl-CoA pathway requiring vitamin B12 (B12) in the liver. Thus, the effects of weekly B12 injections (10 mg X head-1 X wk-1, intramuscularly) with and without dietary monensin (25 mg/kg diet) on average daily gain (ADG), dry matter intake (DMI), feed to gain ration (F/G), liver and serum B12 concentrations and liver activity of propionate metabolizing enzymes were examined in an 84-d trial. Sixteen lambs (27.5 kg average initial wt) were assigned randomly to one of four treatments in a factorial arrangement: monensin plus B12, monensin without B12, no monensin plus B12 and no monensin without B12. Lambs were fed an 80% concentrate diet and slaughtered at the end of the trial. Liver samples were obtained by biopsy on d 0 and at slaughter on d 84 to determine activity of propionate metabolizing enzymes and B12 concentrations. Serum samples were taken on d 0, 28, 56 and 84 to determine serum B12 concentration. Neither monensin nor B12 affected (P greater than .10) ADG, DMI or F/G. Lambs receiving B12 had higher (P less than .01) serum B12 concentrations, but this was not reflected (P greater than .10) in higher liver B12 concentrations. No difference (P greater than .10) in liver propionate metabolizing activity among treatments was detected; however, monensin decreased (P less than .05) fumarate and malate formation by liver homogenates. Liver B12 concentrations were highly correlated with endogenous propionate metabolizing activity at d 0 (r = .73, P less than .01) and d 84 (r = .51, P less than .05). Results suggest no advantage to providing supplemental B12 to lambs fed monensin-supplemented, high-concentrate diets.
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