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Edizione italiana della "NOMENCLATURA ANATOMICA VETERINARIA ILLUSTRATA" di O. SCHALLER
No full textANTONIO DELFINO EDITORE; EDIZIONE ITALIANA A CURA DI MASCARELLO F. E COZZI B
Effects of clenbuterol on rabbit growth, nitrogen balance and skeletal muscle fibres
No full text27 male N.Z.W. rabbits (1953 +/- 32 g initial live weight) were housed in individual metabolic cages in a controlled environment maintainedat a temperature of 18-degrees-C, illuminated between 8 AM and 8 PM. The animals were divided into 3 homogenous groups fed ad libitum (from6 PM to 9 AM) diets containing different levels of clenbuterol (CB) (C: control diet, T-0.5: control diet plus 0.5 mg/kg CB, T-1: control diet plus 1 mg/kg CB). Two N-balance trials were performed:days 4 through 8 and days 27 through 31 from the beginning of administration of experimental diet. CB treatment significantly improved final live weight (about + 8.9%), with no dose-effect. Treatment did not affect feed intake, while a better feed efficiency was observed for groups receiving CB. During the N-balance study no treatment-effects wereobserved on N intake nor on fecal N. The beta-adrenergic agonist increased N-retained (P < 0.01) and reduced N-urinary excretion (P < 0.01). The effects of CB treatment on reducing urea, OH-proline and alpha-amino-N excretion were initially greater. Our data indicate that the beta-agonist reduces amino acid oxidation, collagen protein degradation and spares amino acids, thus contributing to enhanced efficiency of N deposition. Creatinine-N excretion was significantly increased only during second period of N-balance (P < 0.001). Treatment with CB significantly improved the dressing percentage. The semimembranosus muscle was significantly heavier in the treated group (T-1) than in the controls, due to muscle hypertrophy. The muscle hypertrophy caused by CB included a general effect on the cross-sectional area of all fibre types and a transformation of fibre types, especially type IIA to IIB
INFLUENCE OF BREEDING SYSTEMS ON PH AND HISTOCHEMICAL PROPERTIES OF MUSCLE-FIBERS IN PORCINE MUSCULUS-SEMIMEMBRANOSUS
No full textThe characteristic fibre-type composition and fast myosin present in the striated oesophageal muscle of the carnivores
No full textExpression of myosin heavy chain isoforms in laryngeal muscles in comparison with skeletal and special muscles
No full textLarynx in mammals is characterized by five intrinsic laryngeal muscles with complex movements involved in respiration, airway protection and phonation. These muscles, differently from limb and trunk muscles that derived from somites, originate from the branchial arches. In all species the laryngeal muscles have the capacity to express the transitional embryonic and perinatal isoforms in adult but at low level ([1-4]). In same species of mammals (horse and cow) the laryngeal muscles express only the three skeletal MyHC isoforms (type 1, 2A and 2X) ([3], [5]); other species (dog, cat and tiger) express also a faster isoform, not detectable in skeletal muscles, the 2B isoform [4,6,7]. Furthermore, in species where the 2B isoform is present in skeletal muscles (rat and rabbit), another isoform presumably faster is present, the EO MyHC ([8], [9]). In rat and human laryngeal muscles a different isoform (IIL MyHC) was described [10,11], but it is unclear if this new isoform correspond to EO in rat or to 2B in human or to the two novel isoforms identified by Rossi et al. [12] in EO muscles (codified by MYH 14 and 15 genes). Combining RNA expression, electrophoresis and immunoblot we demonstrated that the IIL isoform in human does not correspond to type 2 isoforms (2A, 2X, 2B, EO, embryonic and perinatal cluster), to cardiac isoforms (beta and alfa), to M isoform and to isoforms codified by MYH 14 and 15 gene, and therefore is probably a new isoform.
[1] Jung HH, Han SH, Choi JO. Expression of myosin heavy chain mRNA in rat laryngeal muscles. Acta Otolaryngol. 1999; 119(3):396-402.
[2] Malmgren LT, Lovice DB, Kaufman MR. Age-related changes in muscle fiber regeneration in the human thyroarytenoid muscle. Arch Otolaryngol Head Neck Surg. 2000; 126(7):851-6.
[3] Toniolo L, Maccatrozzo L, Patruno M, Caliaro F, Mascarello F, Reggiani C. Expression of eight distinct MHC isoforms in bovine striated muscles: evidence for MHC-2B presence only in extraocular muscles. J Exp Biol. 2005; 208:4243-53.
[4] Toniolo L, Maccatrozzo L, Patruno M, Pavan E, Caliaro F, Rossi R, Rinaldi C, Canepari M, Reggiani C, Mascarello F. Fiber types in canine muscles: myosin isoform expression and functional characterization. Am J Physiol Cell Physiol. 2007; 292(5):C1915-26.
[5] Rhee HS, Steel CM, Derksen FJ, Robinson NE, Hoh JF. Immunohistochemical analysis of laryngeal muscles in normal horses and horses with subclinical recurrent laryngeal neuropathy. J Histochem Cytochem. 2009; 57(8):787-800.
[6] Wu YZ, Baker MJ, Crumley RL, Blanks RH, Caiozzo VJ. A new concept in laryngeal muscle: multiple myosin isoform types in single muscle fibers of the lateral cricoarytenoid. Otolaryngol Head Neck Surg. 1998; 118(1):86-94.
[7] Bergrin M, Bicer S, Lucas CA, Reiser PJ. Three-dimensional compartmentalization of myosin heavy chain and myosin light chain isoforms in dog thyroarytenoid muscle. Am J Physiol Cell Physiol. 2006; 290(5):C1446-58.
[8] Lucas CA, Rughani A, Hoh JF. Expression of extraocular myosin heavy chain in rabbit laryngeal muscle. J Muscle Res Cell Motil. 1995; 16(4):368-78.
[9] Briggs MM, Schachat F. Early specialization of the superfast myosin in extraocular and laryngeal muscles. J Exp Biol. 2000; 203:2485-94.
[10] DelGaudio JM, Sciote JJ, Carroll WR, Escalmado RM. Atypical myosin heavy chain in rat laryngeal muscle. Ann Otol Rhinol Laryngol. 1995; 104(3):237-45.
[11] Toniolo L, Macchi V, Porzionato A, Paoli A, Marchese-Ragona R, De Caro R, Reggiani C. Myosin heavy chain isoforms in human laryngeal muscles: an expression study based on gel electrophoresis. Int J Mol Med. 2008; 22(3):375-9.
[12] Rossi AC, Mammucari C, Argentini C, Reggiani C, Schiaffino S. Two novel/ancient myosins in mammalian skeletal muscles: MYH14/7b and MYH15 are expressed in extraocular muscles and muscle spindles. J Physiol. 2010; 588:353-64
The fibre type composition of the striated muscle of the oesophagus in ruminants and carnivores
No full text
Different putative neuromodulators are present in the nerves which distribute to the teleost skeletal muscle.
No full textThe presence of putative neuromodulators in the nerve fibres was investigated in white skeletal muscle of two teleost fish not taxonomically correlated and showing different patterns of innervation (multiple versus focal innervation). Cryostat sections of epaxial, hypaxial and adductor mandibulae (AM) muscles of Sparus aurata and Anguilla anguilla were stained histochemically for reduced nicotinamide adenine dinucleotide phosphate (NADPH)-diaphorase. Other sections were used for indirect immunohistochemistry (streptavidin-biotin and rhodamine immunofluorescence methods), employing antibodies specific for putative excitatory or inhibitory peptides, including CGRP, substance P, met-enkephalin, bombesin, and VIP. In addition, ultrastructural observations were performed in order to describe the morphology of the motor endplates. A strong immunoreactivity for CGRP and substance P was found in many nerve terminals. Met-enkephalin, bombesin and VIP immunoreactivities were less frequently observed. No immunoreactivity was observed to CCK, NPY or 5-HT. NADPH-diaphorase was identified in nerve fibres of the AM complex only of A. anguilla. Electron microscopy observations evidenced more than one type of synaptic vesicle in motor endplates. Some differences in putative neuromodulator distributions were observed in the two species and muscle complexes, which may be related to the different taxonomical position as well as the different pattern of innervation of white muscle fibres
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