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  • 1990-1994  (1)
  • 1985-1989  (1)
  • ATP  (1)
  • spermatogenesis  (1)
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  • 1990-1994  (1)
  • 1985-1989  (1)
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  • 1
    ISSN: 1432-1912
    Keywords: Smooth muscle ; ATP ; Nicorandil ; K-channels
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Nicorandil (10 μmol/l–0.3 mmol/l) and ATP (1 μmol/l–0.1 mmol/l) hyperpolarized the membrane of circular smooth muscle of the guinea-pig small intestine and increased conductance of the membrane probably to K ions as estimated by the effect on the current-voltage relationship. In the presence of a maximally hyperpolarizing concentration of nicorandil (0.1 mmol/l), ATP produced a further hyperpolarization of 5 mV. The ATP-induced but not the nicorandil-induced hyperpolarization required the presence of Ca in the medium, and the ATP-induced hyperpolarization was blocked by apamin treatment (1 nmol/l) or by MnCl2 (1.3 mmol/l). On the other hand, both hyperpolarization responses were blocked by the local anaesthetics procaine (0.1–1 mmol/l), lidocaine (0.1–1 mmol/l) or cocaine (0.3–1 mmol/l), with different potencies. Field stimulation of smooth muscle of the small intestine produced inhibitory junction potentials (i.j.p.s) and these were inhibited by apamin (10 nmol/l–100 nmol/l). In the presence of ATP, the amplitude of the i.j.p.s was markedly reduced, but in the presence of nicorandil the amplitude was only slightly reduced, consistent with the same increase in ionic conductance and hyperpolarization of the membrane. These results indicate that ATP and nicorandil hyperpolarize the membrane by activating different K-channels, i.e. Ca dependent and Ca insensitive K channels, respectively. As assessed from the effects of local anaesthetics and the membrane properties, the circular muscle may also possess other K channels different from the ATP and nicorandil sensitive K channels.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1573-6849
    Keywords: cDNA cloning ; intermediate filament ; meiosis ; mouse ; nuclear behaviour ; skeletal protein ; spermatogenesis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract It is well known that cytoskeleton and karyoskeleton proteins are associated with changes in cell shape and with the rearrangement of the dynamic structures involved in cell division and motility. In higher vertebrates, there are three major skeletal protein groups: microfilaments, microtubules and intermediate filaments, each representing a multigene family. Some of these skeletal proteins are expressed in a temporally- and spatially-specific fashion, and they establish cell-specific cytoplasmic and nucleoplasmic organization during development. Here we report the cDNA cloning of a novel 60 kDa skeletal protein from mouse spermatocytes, termed MNS 1 (meiosis-specific nuclear structural protein), whose computer-predicted protein configuration indicates long α-helical coiled-coil domains flanked by non-helical terminal domains. Functional characterization of MNS1 by ectopic expression in culture cells indicated that it is a detergent-and high salt-resistant skeletal protein which is involved in organization of the nuclear or perinuclear architecture. The MNS1 protein is specifically expressed at the pachytene stage during spermatogenesis, so that its function may involve the determination and maintenance of the appropriate nuclear morphology during meiotic prophase.
    Type of Medium: Electronic Resource
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