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  • 1
    Electronic Resource
    Electronic Resource
    Calcitonin Gene-Related Peptide-Binding Sites of Porcine Cardiac Muscles and Coronary Arteries: Solubilization and Characterization (1989)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 52 (1989), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract: Calcitonin gene-related peptide (CGRP)-binding sites were solubilized, using digitonin, from the porcine spinal cord, atria, and coronary arteries. The specific binding of 125I-human α-CGRP to the solubilized binding sites was inhibited by human α- and β-CGRP and by rat α-CGRP, but not by angiotensin II or human calcitonin. Scatchard plot analysis of saturation gave the same KD value for CGRP in the crude membrane fractions of the tissues examined. The affinity of CGRP to the binding sites was decreased by solubilization in the atria and coronary arteries, but not in the spinal cord. Affinity labeling followed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis revealed distinct molecular sizes of the specific binding sites among the tissues; 70K for the spinal cord, 70K and 90K for the coronary arteries, and 70K and 120K for the atria. These results indicate that the molecular characteristics of the specific binding sites of CGRP in the cardiovascular system are distinct from those in the central nervous system.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1989.tb07277.x
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  • 2
    Electronic Resource
    Electronic Resource
    Histological distribution and developmental changes of tropomyosin isoforms in three chicken digestive organs (1992)
    Springer
    Cell & tissue research 269 (1992), S. 391-401 
    Details
    ISSN: 1432-0878
    Keywords: Digestive organs ; Tissue differentiation ; Low-Mr-type tropomyosin isoforms ; High-Mr-type tropomyosin isoforms ; α and β tropomyosin isoforms ; Chicken
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Histological localization of tropomyosin isoforms in three digestive organs from embryonic and adult chickens was performed by using rabbit antisera against chicken skeletal muscle tropomyosin and against low-Mr-type tropomyosin from chicken small intestine mucosa. The former antiserum (named TM-SH) reacted with α, β, and high-Mr-type isoforms, and the latter (named TM-HL) reacted with α, β, high-Mr-type and low-Mr-type isoforms. α and β Isoforms were detected in muscle cells of the muscular layer and the muscularis mucosa. Low-Mr-type isoforms, however, were detected along the cell membrane and cytoplasm of almost all nonmuscle cells, especially in terminal webs of epithelial cells. Developmental changes of tropomyosin isoforms in digestive organs were studied by two-dimensional gel electrophoresis and image analysis. The relative amounts of α and β isoforms increased in the course of development, but those of low-Mr-type and high-Mr-type isoforms decreased.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00353894
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  • 3
    Electronic Resource
    Electronic Resource
    Immunohistochemical studies on regulation of alternative splicing of fast skeletal muscle troponin T: non-uniform distribution of the exon x3 epitope in a single muscle fiber (2000)
    Springer
    Cell & tissue research 299 (2000), S. 263-271 
    Details
    ISSN: 1432-0878
    Keywords: Skeletal muscle tissue Troponin T isoforms Exon x series Alternative splicing Non-uniform distribution Chicken
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract. Troponin T (TnT) isoforms of chicken fast skeletal muscle are classified into two types, breast-muscle-type (B-type) and leg-muscle-type (L-type) isoforms. These isoforms are produced from a single gene by differential alternative splicing of pre-mRNA. We investigated immunohistochemically the distribution of B-type TnT isoforms in chicken leg muscle (musculus biceps femoris), using anti-exon x3 that was raised against a synthetic peptide corresponding to exon x3 and recognized B-type, but not the L-type, TnT isoforms. Mosaic patterns of immunostaining showing locally different expression of B-type TnT isoforms in a single fiber were observed among fibers, and the non-uniform distribution of the isoforms was also detected in sectioned fibers and myofibrils from the muscle. The results indicated that regulation of pre-mRNA splicing of fast skeletal muscle TnT was different not only among the muscle fibers but also within a single fiber, suggesting that heterogeneous myonuclei in regulation of alternative splicings occur in a single muscle fiber.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s004419900137
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  • 4
    Electronic Resource
    Electronic Resource
    Development of myofibrils in the gizzard of chicken embryos (1986)
    Springer
    Cell & tissue research 243 (1986), S. 487-493 
    Details
    ISSN: 1432-0878
    Keywords: Smooth muscle ; Muscle differentiation ; Myofibrils ; Contractile proteins ; Immunofluorescence microscopy ; Chicken
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary The intracellular distributions of major muscle proteins, myosin, actin, tropomyosin, α-actinin, and desmin, in smooth muscle cells of chicken gizzard at various stages of embryogenesis were investigated by immunofluorescence-labeling of enzyme-dispersed cells cultured up to three hours. These muscle proteins, except some part of myosin, were organized into fibrous structures as soon as synthesis and accumulation of proteins started. As for myosin, a considerable amount of it was dispersed in soluble cytoplasm as well. On the other hand, Ca++-dependent contractility was detected with detergent-extracted myoblasts and glycerinated tissue from embryos older than 7 days. Although the nascent myofibrils bear a resemblance to “stress fibers,” the former could be distinguished from the latter by their high stability in dispersed, spherical cells. The above findings, therefore, show that the synthesis of contractile proteins is followed by immediate assembly of them into functional myofibrils without undergoing any intermediate structure. Based on these findings, the mechanism of myofibril formation in developing smooth muscle cells is discussed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00218055
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  • 5
    Electronic Resource
    Electronic Resource
    A study of the systematics of cyprinid fishes by two-dimensional gel electrophoresis (1998)
    Springer
    Environmental biology of fishes 52 (1998), S. 173-179 
    Details
    ISSN: 1573-5133
    Keywords: genetic distance ; Cyprininae ; Acheilognathinae ; Leuciscinae ; Gobioninae ; Cyprinidae ; phenogram
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract This study was carried out to shed light on confused subfamilial groupings in the Cyprinidae from the biochemical viewpoint at the molecular level, specifically by using two-dimensional gel electrophoresis of liver proteins. Six pairs of cypriniform fishes, which are different from one another at familial, subfamilial, generic, specific, subspecific, and individual levels, were compared. The genetic distances between pairs of fishes increased as taxonomic ranks of the pairs became higher, confirming the reliable usefulness of this technique. Four species representing the different subfamilies, Cyprininae, Gobioninae, Acheilognathinae, and Leuciscinae, were compared to give new insight into relationships at the subfamilial level. Cyprinus carpio (Cyprininae) and Pseudogobio esocinus esocinus (Gobioninae) gave the smallest genetic distance and the largest values were obtained between either one of the above species and Acheilognathus melanogaster (Acheilognathinae), suggesting that the former two subfamilies compose the most closely related group that is in turn distantly related to Acheilognathinae. Tribolodon hakonensis (Leuciscinae) had almost equal genetic distances to the three other species.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1007329201046
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  • 6
    Electronic Resource
    Electronic Resource
    Skeletal muscle regeneration induced by chorio-allantoic grafting (1998)
    Springer
    Journal of muscle research and cell motility 19 (1998), S. 169-177 
    Details
    ISSN: 1573-2657
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract To examine whether the expression pattern of fast-muscle type troponin-T (TnT) isoforms was fixed in cell lineage, breast muscle pieces (pectoralis major) from chick embryos and young and adult chickens were grafted on to chorio-allantoic membrane of 9-day-old chick embryos and cultured until the host embryos hatched out. Muscle fibre formation of the grafts was investigated by histological and immunohistochemical methods with anti-fast-muscle type and anti-slow-muscle type TnT sera, and the expression of fast-muscle type TnT in the grafts from chick embryos and young chickens was studied by SDS-polyacrylamide gel electrophoresis (SDS-PAGE), two-dimensional SDS-PAGE, and immunoblotting. In the chorio-allantoic grafting, the breast muscle initially degenerated forming pyknotic nuclei and hyaline cytoplasm. The surviving cells, which were supposed to be satellite cells, regenerated new muscle fibres of the same type as those of the grafted muscle in respect of TnT isoform expression. Therefore, we considered that the ability to express specific isoforms of TnT was fixed in the satellite cells, and that chorio-allantoic grafting was a useful technique for studying muscle differentiation.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1005312729381
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  • 7
    Electronic Resource
    Electronic Resource
    The structure of the avian fast skeletal muscle troponin T gene: seven novel tandem-arranged exons in the exon x region (1999)
    Springer
    Journal of muscle research and cell motility 20 (1999), S. 655-660 
    Details
    ISSN: 1573-2657
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract To elucidate the mechanism that produces enormous molecular diversity in troponin T (TnT) of fast skeletal muscle, we determined the 5′-half genomic sequence of the chicken fast muscle TnT gene. The sequence of ca. 16 kb included seven exons (exons 1, 2, 3, 4, w, 5, and 6), which have been reported previously and presumed by sequencing TnT cDNAs. Additionally we found six 15 nt and one 18 nt sequences in the region between exons 5 and 6 (i.e. the exon x region). They were encompassed by consensus splice donor and acceptor sites and preceded by putative branch sites, and designated herein as exons xa to xg. Our result shows that the sequence derived from exons x1, x2, and x3, the exons presumed previously by cDNA sequencing, is actually encoded by the seven exons xa to xg, establishing the precise gene structure in the exon x region. Based on our data, together with that on the 3′-half genomic sequence of the quail fast muscle TnT gene, we conclude that the avian fast skeletal muscle TnT gene includes 27 exons, 16 of which are alternatively spliced.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1005504018059
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  • 8
    Electronic Resource
    Electronic Resource
    Immunohistochemical localization of troponin-C in cultured neurons (1983)
    Springer
    Journal of muscle research and cell motility 4 (1983), S. 163-175 
    Details
    ISSN: 1573-2657
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Our previous immunofluorescence studies on neurons have demonstrated the presence of myosin in regions of neurons which contained actin. To determine if a system similar to the troponin complex of striated muscle is present in neurons, antibody shown to be specific for the calcium-binding component of troponin (troponin-C) was applied to cultures of embryonic chick and rat dorsal root ganglia. Neurites treated with anti-troponin-C exhibited a bright fluorescence. Accompanying non-neuronal cells were less reactive than the neuronal elements. Immunodiffusion and immunofluorescence showed that the anti-troponin-C did not react with calmodulin, whereas homogenates of the ganglia elicited a positive immunochemical reaction with the anti-troponin-C in Ouchterlony tests. Our results suggest that some intra-axonal movements may be generated by the interaction of actin and myosin and controlled in part by a calcium-troponin-C-dependent mechanism.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00712028
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