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Query: UNIPROT:Q86TM3 (cage)
 29,987 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The localization of myosin was studied in rat neuronal and glial cell maintained in primary culture, using the double antibody immunofluorescent method. Antibodies were raised against myosin purified from bovine adrenal medulla. Myosin-specific immunoreactivity was found in the cell body and neurites of neuronal cells and in the cytoplasm of glial cells. In the former no typical substructure was observable, whilst in the latter myosin-rich filaments were found forming either a cage entrapping the nucleus or as long cables in cellular morphogenic expansions.
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PMID:Immunofluorescent localization of microfilaments in neuronal and glial primary cell cultures with antibody against adrenal medullary myosin. 37 14

The purpose of this study was to determine whether cardiac biochemical adaptations are induced by chronic exercise training (ET) of miniature swine. Female Yucatan miniature swine were trained on a treadmill or were cage confined (C) for 16-22 wk. After training, the ET pigs had increased exercise tolerance, lower heart rates during exercise at submaximal intensities, moderate cardiac hypertrophy, increased coronary blood flow capacity, and increased oxidative capacity of skeletal muscle. Myosin from both the C and ET hearts was 100% of the V3 isozyme, and there were no differences between the myosin adenosine triphosphatase (ATPase) or myofibrillar ATPase activities of C and ET hearts. Also, the sarcoplasmic reticulum Ca(2+)-ATPase activity and Na(+)-Ca2+ exchange activity of sarcolemmal vesicles were the same in cardiac muscle of C and ET hearts. Finally, the glycolytic and oxidative capacity of ET cardiac muscle was not different from control, since phosphofructokinase, citrate synthase, and 3-hydroxyacyl-CoA dehydrogenase activities were the same in cardiac tissue from ET and C pigs. We conclude that endurance exercise training does not provide sufficient stress on the heart of a large mammal to induce changes in any of the three major cardiac biochemical systems of the porcine myocardium: the contractile system, the Ca2+ regulatory systems, or the metabolic system.
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PMID:Biochemical characterization of exercise-trained porcine myocardium. 183 67

This study examined the time course of adult rodent soleus muscle myofibril and myosin isoform protein expression after 4, 8, 16, 28, and 56 days of hindlimb unweighting by tail suspension (S). The time course of soleus muscle recovery (R) was also examined after 28 days of hindlimb unweighting with an additional 4, 8, 16, and 28 days of unrestricted cage activity. During suspension, soleus muscle myofibril protein rapidly decreased from 34.3 +/- 3.1 (1.96SE) mg/pair in the control (C) group to 6.9 +/- 1.4 (1.96SE) mg/pair in S (t = 56 days). The calculated first-order degradation rate constant for this loss was kd = 0.17 days-1 [half time (t1/2) = 4.1 days]. The estimated slow myosin (SM) isoform content decreased from 13.4 +/- 2.0 (1.96SE) mg/pair in C to 2.1 +/- 0.2 (1.96SE) mg/pair in S (kd = 0.19 days-1, t1/2 = 3.6 days). The relative proportion of other myosin isoforms was increased at 28 and 56 days of suspension, reflecting an apparent de novo synthesis and the loss of SM. Recovery of contractile protein after 28 days of suspension was slower for both the myofibril protein and the SM isoform (kd = 0.07 days-1, t1/2 = 10 days). These data suggest that loss of weight bearing specifically affected the mechanisms of contractile protein expression reflected in soleus muscle protein degradation processes. In addition, the expression of the myosin isoforms were apparently differentially affected by the loss of weight-bearing activity.
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PMID:Time course of soleus muscle myosin expression during hindlimb suspension and recovery. 295 49

This study examined the effect of stationary ground support (2 and 4 h/day) and uphill running (1.5 h/day, 20 m/min, 30% grade) activity patterns on soleus muscle atrophy and slow myosin loss during 4 wk of rodent hindlimb unweighting by tail suspension. We also examined the effect of uphill running during the last 4 wk of an 8-wk hindlimb unweighting program and during 4 wk of cage recovery after 4 wk of hindlimb unweighting. All forms of activity partially spared soleus muscle weight (mg), myofibril protein (mg/muscle pair and microgram/mg muscle), and relative and absolute slow myosin (SM) isoform content (% of total and mg/muscle pair, P less than 0.05). Relative to the normal control soleus muscle, the uphill running regimens resulted in 1) increased fast myosin isoform content and 2) diminished recovery of SM isoform content when coupled with cage activity recovery. Four weeks of cage recovery after 4 wk of hindlimb unweighting resulted in recovery of the relative SM isoform content to proportions exceeding normal control values, suggesting an apparent degradation of any normally existing fast myosin. These results indicate that, in the context of the hindlimb unweighting model, the mechanisms controlling the expression of soleus muscle SM and fast myosin genes can be affected differently by the diverse activities of stationary ground support, unrestricted cage activity, and programmed uphill running.
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PMID:Activity influences on soleus muscle myosin during rodent hindlimb suspension. 362 21

Morphometric data on left ventricular papillary muscle structures have been determined in tumor-induced malnutrition and related to the maximum activities of key enzymes for energy production in the whole myocardium. Adult, nongrowing mice with a syngeneic sarcoma were used to represent a condition of cancer associated host tissue wasting. Hearts from mice 11 days after tumor implantation showed atrophy and a significantly reduced amount of myofibrillar, soluble, and collagen proteins than hearts from control animals. The cross-sectional area of myocardial cells was 33% smaller in tumor-bearing mice (p less than 0.025), but the total number of capillaries and the residual interstitial volume were similar in the two groups. The total number of subcellular structures per cell, such as mitochondria, myofibrils, and myosin filaments per myofiber, were significantly lower in the tumor-bearing animals (p less than 0.025). Conversely, the proportion of myofibrils was higher (p less than 0.05) in tumor-bearing animals while the proportion of mitochondria was lower. Maximum activities (Vmax) of selected regulatory key enzymes for energy production (glycogenolytic, glycolytic, and mitochondrial) were not significantly altered in hearts from tumor-bearing mice. The results support the conclusion that myocardial functional capacity is better preserved than overall structural components would imply in tumor-host associated malnutrition, which is probably secondary to deprived food intake. Teleologically, this may be a means by which functional deterioration of the heart is minimized during the induction of malnutrition.
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PMID:Ultrastructural changes and enzyme activities for energy production in hearts concomitant with tumor-associated malnutrition. 382 Oct 91

Rats housed as a group per cage were centrifuged for 21 and 30 days at 1.1 and 2.0 G. The following parameters were measured: motor activity, body mass, static and dynamic endurance, acceleration (+Gz) tolerance, vestibular function, equilibrium function, skeletal muscle contractility, bone dynamics, gas exchange, blood biochemistry; weight of adrenals, thymus and thyroid gland; morphology of adrenals, thyroid gland, and cortex of the cerebellum nodulus; biochemistry of blood hormones, energy metabolism enzymes in the liver, bone phosphatases, myosin Ca-Mg-ATPase in the myocardium, protein sulfhydryl groups in the cerebellar motor cortex. The study has demonstrated that prolonged (1/50 of their life time) centrifugation of unrestrained rats causes no deterioration of many physiological functions, i.e., rotation produces no adverse effects on the animal body.
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PMID:[Primary results of rat experiments with long-term rotation in relation to the problem of artificial gravity]. 387 13

The basal body cage is a fibrillar chamber which surrounds each basal body in the ciliate cytoskeleton. The function of this chamber is unknown. In Tetrahymena, the cage contains actin filaments which connect the cage to triplet microtubules. In this study, we have examined the cage for the presence of myosin. Skeletal muscle myosin-II heavy and light chains were used to affinity-purify anti-MHC and anti-MLC antibodies, respectively, from an antiserum raised against Tetrahymena oral apparatus proteins. On western immunoblots of ATP-solubilized Tetrahymena proteins, the anti-MHC antibody detected a putative myosin heavy (180 kDa) chain, and the anti-MLC antibody detected a putative myosin light (18 kDa) chain. The anti-MHC antibody specifically labeled the AI zone of sarcomeres. In cosedimentation assays with an ATP-solubilized protein fraction, the 180 kDa polypeptide associated with skeletal muscle actin filaments in an ATP-dependent manner. The sedimented actin filaments appeared to be organized into bundles. Immunodepletion of the 180 kDa rendered the ATP-solubilized protein fraction ineffective in bundling actin filaments in a cosedimentation assay. ATP-solubilized Tetrahymena proteins, which included the 180 kDa polypeptide, exhibited F-actin-stimulated, Mg2+ ATPase activity and K+, EDTA ATPase activity which are characteristic of myosin ATPases. Immunodepletion of the 180 kDa polypeptide reduced the F-actin, Mg2+ ATPase activity of the ATP-solubilized protein fraction by more than 80%. Based on these various observations, we conclude that the 180 kDa polypeptide is a putative myosin heavy chain, probably a myosin-II and that the 18 kDa polypeptide is probably a myosin-II light chain. We have used the affinity-purified, anti-myosin antibodies with immunofluorescence microscopy and immunogold electron microscopy to map the location of the putative myosin heavy and light chains in Tetrahymena. Immunofluorescence microscopy showed that the anti-myosin antibodies localized to Tetrahymena somatic and oral region basal bodies. At the ultrastructural level, the anti-myosin antibodies localized to filaments in the basal body-cage complex. The labeling patterns with both anti-myosin antibodies were identical to the labeling pattern observed with an anti-actin antibody reported in a previous study. The co-localization of myosin and actin argue for a motility system within the basal body-cage complex.
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PMID:Putative myosin heavy and light chains in Tetrahymena: co-localization to the basal body-cage complex and association of the heavy chain with skeletal muscle actin filaments in vitro. 762 16

We have determined intersite distances from Cys374 of actin to Cys707 (SH1) and Cys697 (SH2) of myosin subfragment 1 (S1) in actosubfragment 1 (A.S1) by fluorescence resonance energy transfer for rigor complex A.S1 and complexes containing bound ADP and ADP plus orthovanadate (Vi), A.S1.ADP, and A.S1.ADP.Vi. A single energy acceptor (4-dimethylaminophenylazophenyl-4'-maleimide, DABMI) was attached to Cys374, and two different energy donors [(5-(iodoacetamideothyl)aminonaphthalene-1-sulfonic acid (IAEDANS) and 2-(4'-maleimidylanilino)naphthalene-6-sulfonic acid (MIANS)] were each attached to SH1 and SH2 for the distance determination. The two sites SH1 and SH2 of S1 were approximately equidistant (ca. 45 A) from actin Cys374 in rigor A.S1 when MIANS was the energy donor attached to the two thiols. The Cys374-SH1 distance decreased by 7-8 A in the presence of ADP plus Vi, but the distance Cys374-SH2 was essentially unaltered under identical conditions. Slightly different but similar distance results were obtained with AEDANS as energy donor. If the structure of actin monomer in A.S1 is assumed to be rigid [Miki, M. (1991) Biochemistry 30, 10878-10884], the present results indicate that MgADP plus Vi induced a movement of SH1 toward the actin site and that SH2 was insensitive to saturation of the active site pocket of S1 and relatively immobile. These results suggest that during the steady-state hydrolysis of ATP or in the weak-binding state of actomyosin, the short helical segment of S1 heavy chain containing SH1 moves closer to the COOH-terminal end of actin, while the adjacent helical segment containing SH2 remains stationary. The emission spectrum of MIANS attached to SH2 experienced a large red spectral shift (6-10 nm) in the presence of MgADP, MgADP + Vi, MgADP + beryllium fluoride, and ATP. A crude model of S1 based on the C alpha coordinates suggests that SH2 is located in a hydrophobic cage surrounded by three hydrophobic residues. Reorientation of one of these side chains could expose SH2 to the solvent. The observed red spectral shift of MIANS attached to SH2 could be explained by such a nucleotide-induced exposure, and this explanation would be consistent with the interpretation that SH2 is stationary.
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PMID:Internal movement in myosin subfragment 1 detected by fluorescence resonance energy transfer. 775 79

An understanding of the molecular mechanism of muscle contraction will require a complete description of the kinetics of the myosin motor in vitro and in vivo. To this end chemical relaxation studies employing light-directed generation of ATP from caged ATP have provided detailed kinetic information in muscle fibers. A more direct approach would be to trigger the actin-activated ATPase activity from a caged myosin, i.e., myosin whose activity is blocked upon derivatization with a photolabile protection group. Herein we report that a new type of caged reagent can be used to prepare a caged heavy meromyosin by modification of critical thiol groups, i.e., a chemically modified motor without activity that can be reactivated at will using a pulse of near-ultraviolet light. Heavy meromyosin modified at Cys-707 with the thiol reactive reagent 1-(bromomethyl)-2-nitro-4,5-dimethoxybenzene does not exhibit an actin-activated ATPase activity and may be viewed as a caged protein. Absorption spectroscopy showed that the thioether bond linking the cage group to Cys-707 is cleaved following irradiation (340-400 nm) via a transient aci-nitro intermediate which has an absorption maximum at 440 nm and decays with a rate constant of 45.6 s(-1). The in vitro motility assay showed that caged heavy meromyosin cannot generate the force necessary to move actin filaments although following irradiation of the image field with a 30 ms pulse of 340-400 nm light the caged group was removed with the concomitant movement of most filaments at a velocity of 0.5-2 micron/s compared to 3-4 micron/s for unmodified HMM. The specificity and simplicity of labeling myosin with the caged reagent should prove useful in studies of muscle contraction in vivo.
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PMID:Light-directed generation of the actin-activated ATPase activity of caged heavy meromyosin. 860 51

Myosin was detected on Western blots of Micrasterias denticulata extracts by use of antibodies from different sources. Inhibitors with different targets of the actomyosin system, such as the myosin ATPase-blockers N-ethylmaleimide (NEM) and 2,3-butanedione monoxime (BDM), or the myosin light chain kinase inhibitor 1-(5-iodonaphthalene-1-sulfonyl)-1H-hexhydro-1,4-diazapine (ML7), had similar effects on intracellular motility during cell development in the green alga Micrasterias, thus pointing towards a participation of myosin in these processes. The drugs markedly altered the mode of postmitotic nuclear migration, slowed down cytoplasmic streaming, changed cell pattern development and prevented normal chloroplast distribution and spreading into the growing semicell. In addition, an increase and dilatations in ER cisternae and marked morphological changes of the Golgi system were observed by transmission electron microscopy after exposure of growing cells to BDM. Neither BDM nor ML7 exhibited any effect on the distribution or arrangement of the cortical F-actin network nor on the F-actin basket around the nucleus, characteristic of untreated growing Micrasterias cells (J Cell Sci 107 (1994) 1929). This is particularly interesting since BDM caused disintegration of the microtubule system co-localized to the F-actin cage during normal nuclear migration. Together with the fact that other microtubules not connected to the F-actin system remained uninfluenced by BDM, this observation is evidence of an integrative function of myosin between the cytoskeleton elements.
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PMID:Involvement of myosin in intracellular motility and cytomorphogenesis in Micrasterias. 1464 29


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