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A novel latent proteinase of which activity was induced by heating in the presence of NaCl was purified to homogeneity from threadfin-bream muscle by a combination of DEAE-cellulose, Con A-Sepharose, Arg-Sepharose, and Shim-pack HAC chromatographies. This proteinase was a glycoprotein having a monomeric subunit structure; Mr was estimated to be 77,000 on SDS-PAGE analysis. The proteinase hydrolyzed Boc-Leu-Thr-Arg-MCA as well as myosin heavy chain in the presence of 2-4% NaCl at pH 7.0 and at 60 degrees C, optimally. The proteinase was classified as serine proteinase based on the effects of soybean trypsin inhibitor, leupeptin, and antipain.
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PMID:Purification and properties of a novel latent proteinase showing myosin heavy chain-degrading activity from threadfin-bream muscle. 235 32

Mammalian skeletal muscles consist of three main fibre types, type 1,2A and 2B fibres, with different myosin heavy chain (MHC) composition. We have now identified another fibre type, called type 2X fibre, characterized by a specific MHC isoform. Type 2X fibres, which are widely distributed in rat skeletal muscles, can be distinguished from 2A and 2B fibres by histochemical ATPase activity and by their unique staining pattern with seven anti-MHC monoclonal antibodies. The existence of the 2X-MHC isoform was confirmed by immunoblotting analysis using muscles containing 2X fibres as a major component, such as the normal and hyperthyroid diaphragm, and the soleus muscle after high frequency chronic stimulation. 2X-MHC contains one determinant common to 2B-MHC and another common to all type 2-MHCs, but lacks epitopes specific for 2A- and 2B-MHCs, as well as an epitope present on all other MHCs. By SDS-polyacrylamide gel electrophoresis 2X-MHC shows a lower mobility compared to 2B-MHC and appears to comigrate with 2A-MHC. Muscles containing predominantly 2X-MHC display a velocity of shortening intermediate between that of slow muscles and that of fast muscles composed predominantly of 2B fibres.
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PMID:Three myosin heavy chain isoforms in type 2 skeletal muscle fibres. 254 31

We have utilized a key biochemical determinant of muscle fiber type, myosin isoform expression, to investigate the initial developmental program of future fast and slow skeletal muscle fibers. We examined myosin heavy chain (HC) phenotype from the onset of myogenesis in the limb bud muscle masses of the chick embryo through the differentiation of individual fast and slow muscle masses, as well as in newly formed myotubes generated in adult muscle by weight overload. Myosin HC isoform expression was analyzed by immunofluorescence localization with a battery of anti-myosin antibodies and by electrophoretic separation with SDS-PAGE. Results showed that the initial myosin phenotype in all skeletal muscle cells formed during the embryonic period (until at least 8 days in ovo) consisted of expression of a myosin HC which shares antigenic and electrophoretic migratory properties with ventricular myosin and a distinct myosin HC which shares antigenic and electrophoretic migratory properties with fast skeletal isomyosin. Similar results were observed in newly formed myotubes in adult muscle. Future fast and slow muscle fibers could only be discriminated from each other in developing limb bud muscles by the onset of expression of slow skeletal myosin HC at 6 days in ovo. Slow skeletal myosin HC was expressed only in myotubes which became slow fibers. These findings suggest that the initial commitment of skeletal muscle progenitor cells is to a common skeletal muscle lineage and that commitment to a fiber-specific lineage may not occur until after localization of myogenic cells in appropriate premuscle masses. Thus, the process of localization, or events which occur soon thereafter, may be involved in determining fiber type.
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PMID:Evidence for expression of a common myosin heavy chain phenotype in future fast and slow skeletal muscle during initial stages of avian embryogenesis. 265 4

Muscle biopsies from 20 cases of spinal muscular atrophy (SMA), mostly diagnosed as Werdnig-Hoffmann (W-H) disease, were examined for myosin heavy chain (HC) composition. The fetal, fast, and slow heavy chains were characterized in the isolated muscle myosin, and in myosin of single, chemically skinned fibers, by electrophoresis in SDS-6% polyacrylamide gels and by immunoblot techniques, using specific antibodies directed to each main type of myosin HC. The fiber distribution of myosin HC isozymes was further investigated on muscle cryostat sections by an indirect immunofluorescent technique. Fetal myosin HC was found to be expressed in a subpopulation of severely atrophic fibers, alone or together with the slow form of myosin HC. Triangulated fibers of intermediate size contained fetal and fast myosin or fast myosin alone. The hypertrophic fibers were characterized by the predominant expression of slow myosin HC; but in some of these fibers, also low amounts of HC fetal were found to be expressed. These findings are discussed in relation to developmental transitions of myosin heavy chains in human muscle.
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PMID:Myosin heavy chain composition of muscle fibers in spinal muscular atrophy. 266 3

The fiber type composition of two fast muscles of the chicken, namely, adductor superficialis (AS) and pectoralis major (PM) was examined by the histochemical myosin ATPase staining and immunochemical techniques using monoclonal antibodies (McAbs). Two new McAbs produced against the myosin of the anterior latissimus dorsi (ALD) muscle of the chicken and named ALD-122 and ALD-83 were characterized to be specific for myosin heavy chain (MHC) and for myosin light chain-1 respectively. They were used in conjunction with previously reported McAbs specific for slow MHC (ALD-47), fast MHC (MF-14) and fast light chain-2 (MF-5). By the histochemical ATPase test most muscle fibers of AS and PM muscles reacted as IIA and IIB respectively. By immunofluorescent staining with the anti-MHC McAbs, ALD-122 and MF-14, the fibers of AS muscle showed remarkable heterogeneity whereas PM muscle fibers reacted uniformly. Differences in the myosin light chain composition of AS and PM muscles were also found by SDS-gel electrophoresis and immunoblot analysis with the anti-light chain McAb, ALD-83. The study clearly indicated that the histochemically homogenous (type IIA) AS muscle is composed of several subpopulations of fibers which differ in their myosin composition and that this heterogeneity of the muscle is not simply due to presence of variable amounts of slow myosin in its fibers.
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PMID:Heterogeneity of fast-oxidative muscle fibers of chicken demonstrated by anti-myosin monoclonal antibodies. 273 24

Changes in the expression of heavy chains of myosin during development determine the functional characteristics of striated muscles. The distribution of heavy-chain isoforms of smooth-muscle myosin was determined in the airways of adult and infant humans to see whether it might underlie the hyperreactivity of human airways. The protein bands corresponding to myosin were separated using SDS/polyacrylamide-gel electrophoresis (4% gels) and identified by immunoblotting using both monoclonal and polyclonal antibodies against smooth-muscle myosin and non-muscle myosin. The relative proportion of each heavy chain stained by Coomassie Blue was measured by densitometric scanning. Three major bands corresponding to myosin heavy-chain isoforms were found; the two slower migrating bands (MHC1 and MHC2) were smooth-muscle myosin, and the third band was non-muscle myosin. The MHC1/MHC2 ratio was 0.69:1 in adult bronchus, and in infant bronchus and trachea. This contrasted with the airway smooth muscle in pigs, which was run concurrently, where the smooth-muscle heavy-chain ratio changed with development [Mohammad & Sparrow (1988) FEBS Lett. 228, 109-112]. The non-muscle myosin heavy chain comprised 63% of the smooth-muscle myosin. In both adult and infant lungs an additional putative myosin heavy chain which migrated slightly more rapidly than non-muscle myosin heavy chain was identified using the monoclonal smooth-muscle myosin antibody BF 48. This was unique to the human species.
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PMID:The distribution of heavy-chain isoforms of myosin in airways smooth muscle from adult and neonate humans. 276 80

Fluorescence spectra of ANM-labeled, glycerinated rabbit psoas muscle fibers were recorded in relaxed, contracted, and rigor states. SDS polyacrylamide gel electrophoresis of the ANM-labeled muscle fibers indicated that proteins labeled with ANM were myosin heavy chain, C protein, and actin. In a relaxed state in the presence of ATP, myosin heavy chain was mainly labeled. During the transition from rigor to the relaxed or contracted state, there was a blue shift (about 5 nm) of the ANM emission spectrum. Similar experiments with FAM (N-(3-fluoranthyl)-maleimide)-labeled muscle fibers showed that these fluorescence changes were not artifacts due to the movement of muscle fibers. The fibers labeled in the ATP relaxing solution showed a marked decrease in both isometric force and unloaded shortening velocity (Vo), while in the fibers labeled in the rigor solution isometric tension was not markedly suppressed, though Vo decreased to the same extent as in the fibers labeled in the ATP relaxing solution. Fluorescence spectra of ANM-labeled HMM in different states were also measured. A fluorescence enhancement and a blue shift (about 5 nm) of the emission maximum were observed in HMM + MgATP or HMM + MgATP + F-actin in comparison with HMM + F-actin. These results suggest that the fluorescence spectra of the ANM-labeled muscle fibers reflect their conformational changes between the rigor state (in the absence of MgATP) and the relaxed or contracted state (in the presence of MgATP).
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PMID:Fluorescence properties and contraction characteristics of ANM (N-(1-anilinonaphthyl-4)maleimide)-labeled rabbit psoas muscle fibers. 293 82

Distinct myosin isoforms were identified from the ventricles and atria of foetal, normal and hypertrophied human hearts. Ventricle and atrium myosins cannot be differentiated by their sedimentation behaviour in the analytical ultracentrifuge, they vary, however, with regard to the Ca2+-dependent ATPase and also the activation parameters in measurements of the enzyme activity in dependence on temperature. In agreement with other authors we observed a foetal light chain in the ventricular tissue of the latter half of gestation, when myosin was characterized by SDS-polyacrylamide gel electrophoresis and isoelectric focusing. Using pyrophosphate gel electrophoresis an additional foetal isomyosin was observed besides the typical ventricular myosin HV-3, which migrates faster. Two distinct myosin isoforms designated as HA-3 and HA-1 occur in the atrium of the normal human heart. It was found that besides their own isoenzymes normal atria also contain ventricular isomyosin, whose relative proportion is markedly increased in the hypertrophic atrium. In contrast, we usually observed only one isoenzyme in the normal ventricle. Moreover, in case of myocardial infarction a dramatic transformation of myosin heavy chain composition with a shift to an atrial myosin type took place in the ventricle.
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PMID:Myosin isoenzymes in normal and hypertrophied human hearts. 294 91

Isomyosin analyses by biochemical, immunochemical, and histochemical investigations have been carried out in five sheep following unilateral recurrent laryngeal nerve paralysis and direct functional electrostimulation of the denervated cricoarytenoid posterior muscle. Myosin light chains were identified by two-dimensional gel electrophoresis. Myosin heavy chains were analyzed by one-dimensional SDS-polyacrylamide gel electrophoresis. Slow myosin heavy chain was identified by orthogonal peptide mapping and immunochemistry. The stimulation effect at cellular level was determined using adenosine triphosphatase (ATPase) histochemistry. A dramatic increase of the type 1 fiber area (slow, fatigue-resistant fibers) could be seen after many weeks of an increasing regime of low-frequency direct electrical stimulation. Biochemically, the amount of slow myosin was always higher than in normal muscles. Some muscles were transformed almost completely to the slow type. At the time they were studied and with the methods employed, the expression of embryonic isomyosin was not observed. In conclusion, after numerous weeks of maintained functional activity, elicited by direct electrostimulation, the denervated muscle regionally showed areas of hypertrophy or at least lack of atrophy of slow myofibers without major signs of muscle damage.
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PMID:Isomyosin changes after functional electrostimulation of denervated sheep muscle. 297 27

Myosin is identified and purified from three different established Drosophila melanogaster cell lines (Schneider's lines 2 and 3 and Kc). Purification entails lysis in a low salt, sucrose buffer that contains ATP, chromatography on DEAE-cellulose, precipitation with actin in the absence of ATP, gel filtration in a discontinuous KI-KCl buffer system, and hydroxylapatite chromatography. Yield of pure cytoplasmic myosin is 5-10%. This protein is identified as myosin by its cross-reactivity with two monoclonal antibodies against human platelet myosin, the molecular weight of its heavy chain, its two light chains, its behavior on gel filtration, its ATP-dependent affinity for actin, its characteristic ATPase activity, its molecular morphology as demonstrated by platinum shadowing, and its ability to form bipolar filaments. The molecular weight of the cytoplasmic myosin's light chains and peptide mapping and immunochemical analysis of its heavy chains demonstrate that this myosin, purified from Drosophila cell lines, is distinct from Drosophila muscle myosin. Two-dimensional thin layer maps of complete proteolytic digests of iodinated muscle and cytoplasmic myosin heavy chains demonstrate that, while the two myosins have some tryptic and alpha-chymotryptic peptides in common, most peptides migrate with unique mobility. One-dimensional peptide maps of SDS PAGE purified myosin heavy chain confirm these structural data. Polyclonal antiserum raised and reacted against Drosophila myosin isolated from cell lines cross-reacts only weakly with Drosophila muscle myosin isolated from the thoraces of adult Drosophila. Polyclonal antiserum raised against Drosophila muscle myosin behaves in a reciprocal fashion. Taken together our data suggest that the myosin purified from Drosophila cell lines is a bona fide cytoplasmic myosin and is very likely the product of a different myosin gene than the muscle myosin heavy chain gene that has been previously identified and characterized.
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PMID:Cytoplasmic myosin from Drosophila melanogaster. 309 37


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