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  • 1
    Electronic Resource
    Electronic Resource
    The Polyclonal Origin of Mycyte Lineages (1996)
    Palo Alto, Calif. : Annual Reviews
    Annual Review of Physiology 58 (1996), S. 509-521 
    Details
    ISSN: 0066-4278
    Source: Annual Reviews Electronic Back Volume Collection 1932-2001ff
    Topics: Medicine , Biology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1146/annurev.ph.58.030196.002453
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  • 2
    Electronic Resource
    Electronic Resource
    Monoclonal Antibodies to Desmin: Evidence for Stage-dependent Intermediate Filament Immunoreactivity during Cardiac and Skeletal Muscle Development (1985)
    Oxford, UK : Blackwell Publishing Ltd
    Annals of the New York Academy of Sciences 455 (1985), S. 0 
    Details
    ISSN: 1749-6632
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Natural Sciences in General
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1749-6632.1985.tb50411.x
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  • 3
    Electronic Resource
    Electronic Resource
    Isolation of newly synthesised myosin filaments from skeletal muscle homogenates and myofibrils (1975)
    [s.l.] : Nature Publishing Group
    Nature 255 (1975), S. 259-261 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] Female Sprague-Dawley rats (200-220 g) were killed and the muscles excised, minced and soaked in an EGTA-pyrophosphate containing relaxing solution, and then homogenised in a solution containing EGTA. The homogenate was centrifuged at 800# to sediment myofibrils and centri-fugation was repeated ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/255259a0
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  • 4
    Electronic Resource
    Electronic Resource
    Diversity in expression of myosin heavy chain isoforms and M-band proteins in rat muscle spindles (1989)
    Springer
    Histochemistry and cell biology 92 (1989), S. 185-194 
    Details
    ISSN: 1432-119X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary The composition of adult rat soleus muscle spindles, with respect to myosin heavy chain isoforms and M-band proteins, was studied by light-microscope immunohistochemistry. Serial sections were labelled with antibodies against slow tonic, slow twitch, fast twitch and neonatal myosin isoforms as well as against myomesin, M-protein and the MM form of creatine kinase. Intrafusal fiber types were distinguished according to the pattern of ATPase activity following acid and alkaline preincubations. Nuclear bag1 fibers were always strongly stained throughout with anti-slow tonic myosin, were positive for anti-slow twitch myosin towards and in the C-region but were unstained with anti-fast twitch and anti-neonatal myosins. The staining of nuclear bag2 fibers was in general highly variable. However, they were most often strongly stained by anti-slow tonic myosin in the A-region and gradually lost this reactivity towards the poles, whereas a positive reaction with anti-slow twitch myosins was found along the whole fiber. Regional staining variability with antineonatal and anti-fast myosins was apparent, often with decreasing intensity towards the polar regions. Nuclear chain fibers showed strong transient reactivity with anti-slow tonic myosin in the equatorial region, did not react with anti-slow twitch and were always evenly stained by anti-fast twitch and anti-neonatal myosins. All three intrafusal fiber types were stained with anti-myomesin. Nuclear bag1 fibers lacked staining for M-protein, whereas bag2 fibers displayed intermediate staining, with regional variability, often increasing in reactivity towards the polar regions. Chain fibers were always strongly stained by anti-M-protein. The MM form of creatine kinase was present in all three fiber types, but bag1 fibers were less reactive and clear striations were not observed, in contrast to bag2 and chain fibers. Out of 38 cross sectioned spindles two were found to have an atypical fiber composition, (lack of chain fibers) and a rather diverse staining pattern for the different antibodies tested. Taken together, the data show that in adult rat solcus, slow tonic and neonatal myosin heavy, chain isoforms are only expressed in the muscle spindle fibers and that each intrafusal fiber type has a unique, although variable, composition of myosin heavy chain isoforms and M-band proteins. We propose that both motor and sensory innervation might be the determining factors regulating the variable expression of myosin heavy chain isoforms and M-band proteins in intrafusal fibers of rat muscle spindles.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00500917
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  • 5
    Electronic Resource
    Electronic Resource
    Intercellular junctions in the developing neural retina of the chick embryo (1970)
    Springer
    Cell & tissue research 104 (1970), S. 405-418 
    Details
    ISSN: 1432-0878
    Keywords: Retina ; Intercellular junctions ; Development ; Histogenesis ; Neurogenesis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary The development of intercellular junctions in the neural retina of the chick embryo between the seventh and nineteenth day of incubation has been studied. The main findings are: 1. The zonulae adhaerentes, which make up the outer limiting membrane of the adult retina, are present throughout the period of development covered by this study. 2. Small intercellular junctions of the macula adhaerens diminuta type appear in large numbers in the plexiform layers of the retina of 10 days incubation and are retained throughout development. 3. Synapse-like structures appear in the inner plexiform layer of the retina after 14 days of incubation. The possible relevance of these intercellular junctions to retinal morphogenesis is discussed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00335691
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  • 6
    Electronic Resource
    Electronic Resource
    Size and charge heterogeneity of C-protein isoforms in avian skeletal muscle. Expression of six different isoforms in chicken muscle (1989)
    Springer
    Journal of muscle research and cell motility 10 (1989), S. 369-378 
    Details
    ISSN: 1573-2657
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary C-protein is an abundant protein, of unknown function, found in the striated muscles of all vertebrates (Offeret al., 1973). Based on differences in size, charge, antigenicity and sarcomere distribution, at least three different isoforms of this protein have been identified (Callaway & Bechtel, 1981; Yamamoto & Moos, 1983; Reinachet al., 1982; Dhootet al., 1985). These have been termed fast-, slow-and cardiac-type isoforms, relative to their distribution in adult striated muscles. Each of these isoforms appears to be expressed sequentially during the development of the chicken pectoralis muscle (Obinataet al., 1984; Obinata, 1985). To better characterize the various isoforms of C-protein, we have reexamined itsin vivo expression during avian myogenesis using a combination of 1-and 2-dimensional gel electrophoresis, cell-free translation and immunoblotting procedures. In this manuscript we demonstrate for the first time that at least four major C-protein isoforms can be distinguished in adult chicken muscles. These include a fast-type isoform in the pectoralis (PECT) muscle (Cnf), a slow-type isoform in the anterior latissimus dorsi (ALD) muscle (Cs3), a second slow-type isoform in the posterior latissimus dorsi (PLD) muscle (Cs4) and a cardiac-type in the ventricle (Cc). During embryonic development of the PECT muscle two additional isoforms can be resolved. These are both slow-type isoforms based on their reactivities with ALD66, a monoclonal antibody specific for adult slow-type C-protein. These latter isoforms have been termed Cs1 and Cs2. Several of the isoforms, particularly Cns1 ands Cs3, exhibit two or more spots of different charge but identical molecular weight on 2-D gels. This observation suggests the possibility that these isoforms are post-translationally modified and possibly phosphorylated. Our data show the C-protein family in avian striated muscles to be highly complex. Additional genetic analyses and primary sequence studies will be required to distinguish transcriptional from post-transcriptional variants.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01758433
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  • 7
    Electronic Resource
    Electronic Resource
    Visualization of myosin exchange between synthetic thick filaments (1991)
    Springer
    Journal of muscle research and cell motility 12 (1991), S. 225-234 
    Details
    ISSN: 1573-2657
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Exchange of myosin molecules between synthetic thick filaments was examined by fluorescence energy transfer and visualized by electron microscopy using streptavidin-gold to detect exchanged biotinylated myosin molecules. N-hydroxysuccinimidobiotin (NHS-biotin) was covalently linked to purified adult chicken pectoralis myosin to obtain assembly-competent biotinylated myosin molecules. Two distinct classes of synthetic filaments, distinguishable by length, were prepared. Biotinylated filaments (575±100 nm) were assembled by a quick dilution (QD) method and unlabelled filaments (1025±250 nm) were obtained by a sequential dilution (SD). The two filament population maintained their distinct length distributions even when mixed. To measure exchange, biotinylated short (QD) filaments were combined with unlabelled long (SD) filaments at a 1∶5 ratio, sampled at varying times and the entry of biotinylated myosin into the previously unlabelled long filaments visualized by the addition of streptavidin-gold. The number of gold particles per micron was examined for fully biotinylated short filaments (〈700 nm), unlabelled long filaments (〉900 nm), and exchanged filaments. Equivalent binding of streptavidin-gold to the two filament types was detected by 60 min suggesting randomization of biotinylated monomers by this time. The precise location of streptavidin-gold sites on the long filaments was also measured. Although labeling was detected along the full length of the filaments, at the earliest time points (5 min) filament ends contained twice the number of gold particles as the filament centers. Approximately equivalent labeling along the entire length of the filaments was observed by 60 min. These results provide additional support for our earlier report of extensive myosin exchange between synthetic thick filaments and show that extensive exchange takes place rapidly along the full length of synthetic thick filaments.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01745111
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  • 8
    Electronic Resource
    Electronic Resource
    The interface between MyBP-C and myosin: site-directed mutagenesis of the CX myosin-binding domain of MyBP-C (1999)
    Springer
    Journal of muscle research and cell motility 20 (1999), S. 703-716 
    Details
    ISSN: 1573-2657
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract Myosin-binding protein-C (MyBP-C or C-protein) is a ca. 130 kDa protein present in the thick filaments of all vertebrate striated muscle. The protein contains ten domains, each of ca. 90–100 amino acids; seven are members of the IgI family of proteins, three of the fibronectin type III family. The motifs are arranged in the following order (from N- to C-terminus): Ig-Ig-Ig-Ig-Ig-Fn-Fn-Ig-Fn-Ig. The C-terminal Ig motif (domain X or CX) contains its light meromyosin-binding site. A recombinant form of CX, beginning at Met-1027, exhibits saturable binding to myosin with an affinity comparable to the C-terminal 13 kDa chymotryptic fragment of native MyBP-C. To identify the surface in CX involved in its interaction with myosin, nine site-directed mutants (R37E, K43E, N49D, E52R, D56K, R73E, R74E, G80D and R103E) were constructed. Using a new assay for assessing the binding of CX with the light meromyosin (LMM) portion of myosin, we demonstrate that recombinant CX, just as the full-length protein, is able to facilitate LMM polymerization. Moreover, we show that residues Arg-37, Glu-52, Asp-56, Arg-73, and Arg-74 are involved in this interaction with the myosin rod. All of these amino acids interact with negatively charged residues of LMM, since the mutants R37E, R73E and R74E are unable to bind myosin, whereas E52R and D56K bind myosin with higher affinity than wild-type CX. Residues Lys-43 and Arg-103 show a small but significant influence on the binding reaction; residues Asn-49 and Gly-80 seem not to be involved in this interaction. Based on these data, a model is proposed for the interaction between MyBP-C CX and myosin filaments. In this model, CX interacts with four molecules of LMM at four different sites of the binding protein, thus explaining the effects of MyBP-C on the critical concentration of myosin polymerization.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1005513312939
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  • 9
    Electronic Resource
    Electronic Resource
    An electron microscopic study of the spermathecal complex of virgin aedes Aegypti mosquitoesThe opinions or assertions contained herein are the private views of the authors and are not to be construed as official or as reflecting the views of the Department of the Army or the Department of Defense. (1970)
    New York, NY : Wiley-Blackwell
    Journal of Morphology 132 (1970), S. 293-311 
    Details
    ISSN: 0362-2525
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Virgin mosquitoes were studied with the electron microscope. Spermathecal duct walls contain cuticle, epithelium, and a richly innervated spiral muscle; myocytes are linked by desmosome-like attachment plaques to the underlying epithelium. Periductal cells along upper portions of the ducts have a large secretory droplet within a highly irregular extracellular lacuna and are attached to a long secretory ductule through which finely granular material is delivered to the duct lumen and this enters the spermathecae. Basal gland cells of spermathecae have short ductules containing secretion in virgins. Secretory material in spermathecae of virgins does not form a complete internal membrane.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jmor.1051320305
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  • 10
    Electronic Resource
    Electronic Resource
    Expression of sarcomeric myosin in the presumptive myocardium of chicken embryos occurs within six hours of myocyte commitment (1992)
    New York, NY [u.a.] : Wiley-Blackwell
    American Journal of Anatomy 193 (1992), S. 257-265 
    Details
    ISSN: 0002-9106
    Keywords: Heart ; Development ; Immunocytochemistry ; Immunofluorescence ; Myofibril ; Cell polarity ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: The distribution of sarcomeric myosin heavy chain (MyHC) has been examined immunoctochemically in the presumptive myocardial cells of chicken embryos (stages 6-10) prior to the onset of the heart beat. Embryos were stained with monoclonal antibody MF20, a reagent which recognizes all chicken sarcomeric MyHCs (Bader et al., 1982), and then examined both in whole mount by immunofluorescence and in semithin, plastic-embedded sections following immunoperoxidase labeling. We observed that myosin could be detected as early as stage 7 (0-2 pairs of somites) in 29% of the 31 embryos examined, and by stage 8 (4 pairs of somites) more than 80% of the embryos were MF20+, Every embryo with 5 pairs of somites (stage 8+) labeled strongly with MF20. Labeling was first detected at stage 7 to 7+ as a diffuse fluorescent signal within pleomorphic cells of the splanchnic mesoderm located in two crescent-shaped regions bordering each side of the anterior intestinal portal (AIP). With progressive development, the two crescent-shaped regions merged at the apex of the AIP, and as the two heart tubes began fusion at stage 9, the MyHC+ regions extended cranially and medially. By somite stages 9-10, the myosin-positive cells completely encircled the heart tube. From stages 7 to 9 the myosin signal had no sarcomeric distribution; i.e., there were no MyHC striations nor periodic repeats evident in the presumptive myocytes until late stage 9 and stage 10. Semithin sections revealed that myosin was first distributed in apical regions of the myocytes, adjacent to the pericardial coelom. The implications of these findings for myocyte determination, differentiation and morphogenesis are discussed.© 1992 Wiley-Liss, Inc.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/aja.1001930306
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