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  • Ca2+ release
  • Annual Reviews  (1)
  • Wiley-Blackwell  (1)
  • 2005-2009  (1)
  • 1990-1994
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  • 1980-1984
  • 1
    Publication Date: 2022-05-25
    Description: First published online as a Review in Advance on October 24, 2005. (Some corrections may occur before final publication online and in print)
    Description: Author Posting. © Annual Reviews, 2005. This article is posted here by permission of Annual Reviews for personal use, not for redistribution. The definitive version was published in Annual Review of Physiology 68 (2006): 22.1-22.29, doi:10.1146/annurev.physiol.68.040104.105418.
    Description: Superfast muscles of vertebrates power sound production. The fastest, the swimbladder muscle of toadfish, generates mechanical power at frequencies in excess of 200 Hz. To operate at these frequencies, the speed of relaxation has had to increase approximately 50-fold. This increase is accomplished by modifications of three kinetic traits: (a) a fast calcium transient due to extremely high concentration of sarcoplasmic reticulum (SR)-Ca2+ pumps and parvalbumin, (b) fast off-rate of Ca2+ from troponin C due to an alteration in troponin, and (c) fast cross-bridge detachment rate constant (g, 50 times faster than that in rabbit fast-twitch muscle) due to an alteration in myosin. Although these three modifications permit swimbladder muscle to generate mechanical work at high frequencies (where locomotor muscles cannot), it comes with a cost: The high g causes a large reduction in attached force-generating cross-bridges, making the swimbladder incapable of powering low-frequency locomotory movements. Hence the locomotory and sound-producing muscles have mutually exclusive designs.
    Description: This work was made possible by support from NIH grants AR38404 and AR46125 as well as the University of Pennsylvania Research Foundation.
    Keywords: Parvalbumin ; Ca2+ release ; Ca2+ uptake ; Cross-bridges ; Adaptation ; Sound production ; Whitman Center
    Repository Name: Woods Hole Open Access Server
    Type: Article
    Format: 567086 bytes
    Format: application/pdf
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  • 2
    Electronic Resource
    Electronic Resource
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 40 (1989), S. 331-340 
    ISSN: 0730-2312
    Keywords: auxin action ; phosphoinositide phosphorylation in vitro ; Ca2+ release ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Microsomal membranes from carrot suspension cells were phosphorylated in vitro with [γ-32P]ATP. In the presence of submicromolar concentrations of the natural auxin indoleacetic acid (IAA), a rapid, but transient decrease of the [32P] label could be detected in the phospholipid extracts of the membranes. The phytohormone effect was not the result of an inhibition of the lipid phosphorylation reactions, but was caused by a simultaneous release of water-soluble compounds, which, according to their chromatographic properties, were assumed to contain inositol polyphosphates. Although the [32P]-labeled lipids, as well as the inositol polyphosphates, were not identified unequivocally by chemical analysis, these findings point to an auxin-mediated control of a phosphoinositidase C-like reaction similar to the hormone-stimulated phosphoinositide response in animals. Exogenously applied inositol (1,4,5)trisphosphate [(1,4,5)IP3] was found to release 45Ca2+ from preloaded membrane vesicles of carrot cells. Both the detection of the auxin-stimulated phosphoinositide response and the (1,4,5)IP3-mediated Ca2+ release on isolated cell membranes offer new experimental approaches for the identification of the putative auxin receptor and its signal transduction pathway.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
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