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Heavy Chain Isoforms (heavy + chain_isoform)
Kinds of Heavy Chain Isoforms Selected AbstractsCharacterisation of human soft palate muscles with respect to fibre types, myosins and capillary supplyJOURNAL OF ANATOMY, Issue 2 2000PER S. STÅL Four human soft palate muscles, and palatopharyngeus, the uvula, the levator and tensor veli palatini were examined using enzyme-histochemical, immunohistochemical and biochemical methods and compared with human limb and facial muscles. Our results showed that each palate muscle had a distinct morphological identity and that they generally shared more similarities with facial than limb muscles. The palatopharyngeus and uvula muscles contained 2 of the highest proportions of type II fibres ever reported for human muscles. In contrast, the levator and tensor veli palatini muscles contained predominantly type I fibres. A fetal myosin heavy chain isoform (MyHC), not usually found in normal adult limb muscles, was present in a small number of fibres in all palate muscles. The mean muscle fibre diameter was smaller than in limb muscles and the individual and intramuscular variability in diameter and shape was considerable. All palate muscles had a high capillary density and an unusually high mitochondrial enzyme activity in the type II fibres, in comparison with limb muscles. No ordinary muscle spindles were observed. The fibre type and MyHC composition indicate that the palatopharyngeus and uvula muscles are functionally involved in quick movements whereas the levator and tensor veli palatini muscles perform slower and more continuous contractions. The high aerobic capacity and the rich capillarisation suggest that the palate muscles are relatively fatigue resistant. Absence of ordinary muscle spindles indicates a special proprioceptive control system. The special morphology of the palate muscles may be partly related to the unique anatomy with only one skeletal insertion, a feature consistent with muscle work at low load and tension and which may influence the cytoarchitecture of these muscles. Other important factors determining the special morphological characteristics might be specific functional requirements, distinct embryological origin and phylogenetic factors. [source] Differences in sodium voltage-gated channel properties according to myosin heavy chain isoform expression in single muscle fibresTHE JOURNAL OF PHYSIOLOGY, Issue 21 2009F. Rannou The myosin heavy chain (MHC) isoform determines the characteristics and shortening velocity of muscle fibres. The functional properties of the muscle fibre are also conditioned by its membrane excitability through the electrophysiological properties of sodium voltage-gated channels. Macropatch-clamp is used to study sodium channels in fibres from peroneus longus (PL) and soleus (Sol) muscles (Wistar rats, n= 8). After patch-clamp recordings, single fibres are identified by SDS-PAGE electrophoresis according to their myosin heavy chain isoform (slow type I and the three fast types IIa, IIx, IIb). Characteristics of sodium currents are compared (Student's t test) between fibres exhibiting only one MHC isoform. Four MHC isoforms are identified in PL and only type I in Sol single fibres. In PL, maximal sodium current (Imax), maximal sodium conductance (gNa,max) and time constants of activation and inactivation (,m and ,h) increase according to the scheme I,IIa,IIx,IIb (P < 0.05). ,m values related to sodium channel type and/or function, are similar in Sol I and PL IIb fibres (P= 0.97) despite different contractile properties. The voltage dependence of activation (Va,1/2) shows a shift towards positive potentials from Sol type I to IIa, IIx and finally IIb fibres from PL (P < 0.05). These data are consistent with the earlier recruitment of slow fibres in a fast-mixed muscle like PL, while slow fibres of postural muscle such as soleus could be recruited in the same ways as IIb fibres in a fast muscle. [source] Special gears for full-time engines: association of dystrophin,glycoprotein complex and focal adhesion complex with myosin heavy chain isoforms in rat skeletal muscleACTA PHYSIOLOGICA, Issue 4 2009Ugo Carraro No abstract is available for this article. [source] Correlation of dystrophin,glycoprotein complex and focal adhesion complex with myosin heavy chain isoforms in rat skeletal muscleACTA PHYSIOLOGICA, Issue 4 2009S. Masuda Abstract Aim:, The dystrophin,glycoprotein complex (DGC) and focal adhesion complex (FAC) are transmembrane structures in muscle fibres that link the intracellular cytoskeleton to the extracellular matrix. DGC and FAC proteins are abundant in slow-type muscles, indicating the structural reinforcement which play a pivotal role in continuous force output to maintain posture for long periods. The aim of the present study was to examine the expression of these structures across fast-type muscles containing different myosin heavy chain (MHC) isoform patterns which reflect the fatigue-resistant characteristics of skeletal muscle. Methods:, We measured the expression of dystrophin and ,1 integrin (representative proteins of DGC and FAC respectively) in plantaris, extensor digitorum longus, tibialis anterior, red and white portions of gastrocnemius, superficial portion of vastus lateralis and diaphragm, in comparison with soleus (SOL) and cardiac muscle from rats. Results:, The expression of dystrophin and ,1 integrin correlated positively with the percentage of type I, IIa and IIx MHC isoforms and negatively with that of type IIb MHC isoform in fast-type skeletal muscles, and their expression was abundant in SOL and cardiac muscle. Conclusion:, Our results support the idea that DGC and FAC are among the factors that explain the fatigue-resistant property not only of slow-type but also of fast-type skeletal muscles. [source] Electrophoretic variants of cardiac myosin heavy chain-, in Sprague Dawley ratsELECTROPHORESIS, Issue 3 2004Peter J. Reiser Abstract Analysis of cardiac myosin revealed differences in gel electrophoretic migration patterns of the ,-isoform of myosin heavy chain, but not the ,-isoform, in Sprague Dawley rats. No differences in the migration patterns of the ,-or ,-isoforms were observed in other rat strains. Three electrophoretic migration patterns of the ,-isoforms were observed in individual rats: a slower migrating isoform alone (4% of all rats tested), a faster migrating isoform alone (55%), and both isoforms (41%). The isoform expression pattern was identical in all myocardial regions in each rat. Frequency of expression patterns suggests multiple gene sequences for ,-cardiac myosin heavy chain in Sprague Dawley rats. Sequence analysis of amplified regions of the Sprague Dawley and Brown Norway rat ,-myosin genes, specifically the 5'-untranslated region, exons 1,3, and associated introns, showed numerous single nucleotide polymorphisms in coding and noncoding regions, including putative regulatory sites in Sprague Dawley rats, but not in Brown Norway rats. All Sprague Dawley rats varied from Brown Norway rats and no heterogeneity was observed in Brown Norway rats. Several deletions and dimorphic positions were also observed. Dimorphic positions were evident on automated sequencing comparisons. The data indicate that at least two ,-myosin heavy chain isoforms exist in Sprague Dawley rats and these rats exhibit sequence diversity within that portion of the ,-myosin heavy chain gene reported in this study. [source] Regional specialization of rat quadriceps myosin heavy chain isoforms occurring in distal to proximal parts of middle and deep regions is not mirrored by citrate synthase activityJOURNAL OF ANATOMY, Issue 1 2007Tertius Abraham Kohn Abstract Myosin heavy chain (MHC) isoform content and citrate synthase (CS) activities were measured in the Quadriceps femoris (QF) muscle of 18 female rats. The muscle group was divided into superficial, middle and deep, distal, central and proximal parts. MHC IIb and IIx were more abundant in superficial regions (P < 0.05) with low CS activities compared with deeper parts. The deeper parts expressed all four isoforms (MHC IIb, MHC IIx, MHC IIa and MHC I), with a concomitantly higher CS activity. MHC I, MHC IIa and MHC IIb isoform content varied significantly along the length of the deep regions. Only MHC IIb and CS activity in the proximal middle part correlated (negatively) with each other. This study showed that the QF has regional specialization and that standardization of sampling site is important. Furthermore, CS activity and MHC isoforms are only loosely associated, or not at all. [source] Muscular design in the equine interosseus muscleJOURNAL OF MORPHOLOGY, Issue 6 2006Carl Soffler Abstract We studied the forelimb interosseus muscle in horses, Equus caballus, to determine the muscular properties inherent in its function. Some authors have speculated that the equine interosseus contains muscle fibers at birth only to undergo loss of these fibers through postnatal ontogeny. We describe the muscle fibers in eight interosseus specimens from adult horses. These fibers were studied histochemically using myosin ATPase studies and immunocytochemically using several antibodies directed against type I and type II myosin heavy chain antibodies. We determined that 95% of the fibers were type I, presumed slow-twitch fibers. All fibers exhibited normal morphological appearance in terms of fiber diameter and cross-sectional area, suggesting that the muscles are undergoing normal cycles of recruitment. SDS-PAGE studies of myosin heavy chain isoforms were consistent with these observations of primarily slow-twitch muscle. Fibers were determined to be ,800 ,m long when studied using nitric acid digestion protocols. Short fiber length combined with high pinnation angles suggest that the interosseus muscle is able to generate large amounts of force but can produce little work (measured as pulling the distal tendon proximally). While the equine interosseus muscle has undergone a general reduction of muscle content during its evolution, it remains composed of a significant muscular component that likely contributes to forelimb stability and elastic storage of energy during locomotion. J. Morphol. © 2006 Wiley-Liss, Inc. [source] Myogenic precursor cells in craniofacial musclesORAL DISEASES, Issue 2 2007LK McLoon Craniofacial skeletal muscles (CskM), including the masticatory (MM), extraocular (EOM) and laryngeal muscles (LM), have a number of properties that set them apart from the majority of skeletal muscles (SkM). They have embryological origins that are distinct from musculature elsewhere in the body, they express a number of immature myosin heavy chain isoforms and maintain increased and distinct expression of a number of myogenic growth factors and their receptors from other adult SkMs. Furthermore, it has recently been demonstrated that unlike limb SkM, normal adult EOM and LM retain a population of activated satellite cells, the regenerative cell in adult SkM. In order to maintain this proliferative pool throughout life, CSkM may contain more satellite cells and/or more multipotent precursor cells that may be more resistant to apoptosis than those found in limb muscle. A further exciting question is whether this potentially more active muscle precursor cell population could be utilized not only for SkM repair, but be harnessed for repair or reconstruction of other tissues, such as nervous tissue or bone. This is a highly attractive speculation as the innate regenerative capacity of craniofacial muscles would ensure the donor tissue would not have compromised future function. [source] Correlation of tracheal smooth muscle function with structure and protein expression during early development,PEDIATRIC PULMONOLOGY, Issue 5 2007Aaron B. Cullen MD Abstract With increased survival of premature infants, understanding the impact of development on airway function and structure is imperative. Airway smooth muscle plays a primary role in the modulation of airway function. The purpose of this study is to correlate the functional maturation of airway smooth muscle during the perinatal period with structural alterations at the cellular, ultrastructural, and molecular levels. Length-tension and dose-response analyses were performed on tracheal rings acquired from preterm and term newborn lambs. Subsequent structural analyses included isolated airway smooth muscle cell length, electron microscopy, and myosin heavy chain isoform expression measurements. Functionally the compliance, contractility, and agonist sensitivity of the tracheal rings matured during preterm to term development. Structurally, isolated cell lengths and electron microscopic ultrastructure were not significantly altered during perinatal development. However, expression of myosin heavy chain isoforms increased significantly across the age range analyzed, correlating with the maturational increase in smooth muscle contractility. In conclusion, the developmental alterations in tracheal function appear due, in part, to enhanced smooth muscle myosin heavy chain expression. Pediatr Pulmonol. 2007; 42:421,432. © 2007 Wiley-Liss, Inc. [source] Relationships between tropomyosin and myosin heavy chain isoforms in bovine skeletal muscleANIMAL SCIENCE JOURNAL, Issue 2 2009Mika OE ABSTRACT The composition of tropomyosin (TPM) and myosin heavy chain (MyHC) isoforms was analyzed in 10 physiologically different bovine muscles (masseter, diaphragm, tongue, semispinalis, pectoralis profundus, biceps femoris, psoas major, semimembranosus, longissimus thoracis and semitendinosus) to clarify the relationships between TPM and MyHC isoforms in different muscle fiber types. The content of TPM1 and TPM3 was different in muscles according to their function in muscle contraction, although the content of TPM2 was constantly about 50% of the total TPM in all muscles. The content of TPM1 was higher in semimembranosus, longissimus thoracis and semitendinosus, while that of TPM3 was higher in masseter and diaphragm. The high positive correlation between MyHC-slow content and TPM3 content (r = 0.92) suggested a coexpression of TPM3 and MyHC-slow isoforms in a muscle fiber. MyHC-slow and TPM3 were expressed at the same level in masseter and diaphragm, whereas there was more TPM3 than MyHC-slow in tongue and semispinalis, so it appears that the excess TPM3 in tongue and semispinalis is expressed with other MyHC isoforms. MyHC-2a was the only fast type isoform expressed in tongue and semispinalis. Therefore, the excess TPM3 was composed of myofibrils with MyHC-2a. The results suggested that a fiber expressing MyHC-2a would be regulated delicately by changing the TPM isoform types. [source] | |||||||||||||