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  • 1
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    Free calcium at rest during "catch" in single smooth muscle cells (1989)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1989-03-10
    Description: Tension and intracellular free calcium concentration [( Ca2+]i) were measured simultaneously in single smooth muscle cells isolated from the anterior byssus retractor muscle (ABRM) of Mytilus edulis that were loaded with the fluorescent Ca2+ indicator fura-2. Electrical stimulation evoked a transient elevation of [Ca2+]i associated with a "catch" contraction. During the catch state, however, [Ca2+]i was effectively at its resting level and was unaffected by 5-hydroxytryptamine, which induced a rapid relaxation from catch. The results indicate that a maintained high [Ca2+]i is not required for the maintenance of catch tension in intact ABRM and that there was no significant change in [Ca2+]i upon abolition of catch.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ishii, N -- Simpson, A W -- Ashley, C C -- Wellcome Trust/United Kingdom -- New York, N.Y. -- Science. 1989 Mar 10;243(4896):1367-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Zoological Institute, Faculty of Science, University of Tokyo, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2922614" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Benzofurans ; Bivalvia ; Calcium/*physiology ; Fluorescent Dyes ; Fura-2 ; In Vitro Techniques ; *Muscle Contraction ; Muscle, Smooth/*physiology ; Spectrometry, Fluorescence/instrumentation/methods
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 2
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    Detection of radial crossbridge force by lattice spacing changes in intact single muscle fibers (1990)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1990-12-07
    Description: Time-resolved lattice spacing changes were measured (10-millisecond time resolution) by x-ray diffraction of synchrotron radiation in single intact muscle fibers of the frog Rana temporaria undergoing electrically stimulated tension development during application of stretches and releases. Ramp releases, which decreased fiber length at constant speed, caused a lattice expansion. After the ramp, increasing tension during recovery was accompanied by lattice compression. Ramp stretches caused a compression of the lattice. While the fiber was held at a constant length after the stretch, tension decreased and lattice spacing increased. These observations demonstrate the existence of a previously undetected radial component of the force generated by a cycling crossbridge. At sarcomere lengths of 2.05 to 2.2 micrometers, the radial force compresses the myofilament lattice. Hence, the myofilament lattice does not maintain a constant volume during changes in force.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cecchi, G -- Bagni, M A -- Griffiths, P J -- Ashley, C C -- Maeda, Y -- New York, N.Y. -- Science. 1990 Dec 7;250(4986):1409-11.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Dipartmento di Scienze Fisiologiche, Universita degli studi di Firenze, Italy.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2255911" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Electric Stimulation ; In Vitro Techniques ; Isometric Contraction ; *Muscle Contraction ; Muscles/*physiology/ultrastructure ; Particle Accelerators ; Rana temporaria ; Sarcomeres/physiology/ultrastructure ; Stress, Mechanical ; X-Ray Diffraction
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 3
    Electronic Resource
    Electronic Resource
    Amino acid sequences and calcium-binding properties of two isoforms of barnacle troponin C (1991)
    s.l. : American Chemical Society
    Biochemistry 30 (1991), S. 702-707 
    Details
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/bi00217a017
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  • 4
    Electronic Resource
    Electronic Resource
    Carbon dioxide or bicarbonate ions release Ca2+ from internal stores in crustacean myofibrillar bundles (1981)
    Springer
    The journal of membrane biology 61 (1981), S. 115-125 
    Details
    ISSN: 1432-1424
    Keywords: Sarcoplasmic reticulum ; calcium release ; carbon dioxide ; bicarbonate ions ; crustacean myofibrils
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Summary The paper describes an investigation into the increase in intracellular free Ca2+ and resting tension of barnacle muscle fibers when exposed to CO2. Isometric tension was recorded in isolated myofibrillar bundles prepared from barnacles and crabs. On replacement of a low relaxing bathing solution (free Ca2+∶20nm) at pH 7.1 with a similar one containing 100% CO2 and 130mm HCO 3 − , also at pH 7.1, the bundles developed a phasic contraction, which aequorin experiments confirmed was due to a release of Ca2+ from a store within the bundles. The source of this Ca2+ is tentatively identified as the sarcoplasmic reticulum (SR) for the following reasons: (1) prior exposure to 20mm caffeine depleted this Ca2+ store, (2) procaine (10mm) inhibited the response, and (3) the extracellular space or “clefts” and the mitochondria could be eliminated as possible sources. An effect of the CO2+HCO 3 t- on the free Ca2+/Mg2+ ratio in the bathing solution was excluded as a possible mechanism. The diuretic furosemide (1mm) enhanced the response to CO2+HCO 3 t- . Both furosemide and SITS (1–10mm), by themselves, also released Ca2+ in myofibrillar bundles. A scheme is put forward to explain these results: it is suggested that diffusion of dissolved CO2 into the SR produces an acidification of the SR lumen, which modifies either the Ca2+/-ATPase or the Ca2+-induced release process in such a way to release Ca2+.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02007638
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  • 5
    Electronic Resource
    Electronic Resource
    Simultaneous Recording of Membrane Potential, Calcium Transient and Tension in Single Muscle Fibres (1968)
    [s.l.] : Nature Publishing Group
    Nature 219 (1968), S. 1168-1169 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] Single muscle fibres from the barnacle Balanus nubilus3 were injected with the calcium-sensitive bioluminescent protein, aequorin, as described before2, except that the injection solution was potassium phosphate buffer, pH. 6.1. The purification and properties of aequorin have already been ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/2191168a0
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  • 6
    Electronic Resource
    Electronic Resource
    CALCIUM ION REGULATION IN BARNACLE MUSCLE FIBERS AND ITS RELATION TO FORCE DEVELOPMENT (1978)
    Oxford, UK : Blackwell Publishing Ltd
    Annals of the New York Academy of Sciences 307 (1978), 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.1749-6632.1978.tb41959.x
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  • 7
    Electronic Resource
    Electronic Resource
    Free Ca 2+ and cytoplasmic streaming in the alga Chara (1982)
    [s.l.] : Nature Publishing Group
    Nature 296 (1982), S. 647-651 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] Aequorin was injected into internodal cells of Chara corallina or Nitella sp., and initially showed a high light emission that, except for occasional transient increases, declined rapidly for 30-50 min (Fig. la). This probably reflected a relatively highcytoplasmic free Ca2+ concentrationinjection ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/296647a0
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  • 8
    Electronic Resource
    Electronic Resource
    Increase in free Ca 2+ in muscle after exposure to CO 2 (1978)
    [s.l.] : Nature Publishing Group
    Nature 275 (1978), S. 236-238 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] Single muscle fibres from the barnacle Balanus nubilus were axially injected with the calcium-sensitive photoprotein aequorin6, prepared by chromatography from extracts of Aequorea forskalea4. Usually a period of 2 h was allowed for uniform distribution of the photoprotein internally, after which ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/275236a0
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  • 9
    Electronic Resource
    Electronic Resource
    Hormone-induced release of intracellular Ca 2+ triggers meiosis in starfish oocytes (1978)
    [s.l.] : Nature Publishing Group
    Nature 272 (1978), S. 251-253 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] Marthasterias glacialis oocytes, collected during May or early June from Roscoff (France) or Oban (Scotland) and prepared free of follicular cells18 in Ca-free seawater (CFSW), resumed meiosis when the concentration of external Ca2+ was increased from 0-10 to 25-300 mM. We established by the ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/272251a0
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  • 10
    Electronic Resource
    Electronic Resource
    Functional characterization of the two isoforms of troponin C from the arthropodBalanus nubilus (1991)
    Springer
    Journal of muscle research and cell motility 12 (1991), S. 532-542 
    Details
    ISSN: 1573-2657
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Two isoforms of troponin C (BTnC1 and BTnC2) from the striated muscle of the arthropodBalanus nubilus Darwin (giant barnacle) have been purified (Potteret al., 1987; Collinset al., 1991). Both isoforms were present in all of the white striated muscle fibres studied but not in the red fibres. The ratio of BTnC2 to BTnC1 in different fibre types varied between 3∶1 and 1∶1. Both forms of TnC could be readily extracted from myofibrillar bundles of barnacle muscle in low ionic strength EDTA solutions, reducing force activation to 〈10%. Both forms either separately or together reassociated with the TnC-depleted fibres in a relaxing (LR) solution (pCa〉8.0, [Mg2+] free=1mm, I=0.15m), and the reconstituted fibres could be subsequently activated in contraction (LA) solution (pCa=〈 3.8, [Mg2+] free=1mm, I=0.15m,). The dissociation of BTnC 1+2 is blocked in low ionic strength solutions containing Mg2+ (⩾10mm). The two isoforms of crayfish TnC (CrTnC1 and CrTnC2) were also found to be equivalent to the barnacle TnCs in their ability to reactivate TnC-depleted barnacle myofibrillar bundles. Similar experiments using rabbit skeletal muscle TnC (STnC) (I=0.15m) in BTnC-depleted myofibrillar bundles of barnacle showed considerable variability. STnC could associate, although weakly, with the depleted bundles in either LR or LA, and force could be partially restored. In neither situation was it as effective as either BTnC or CrTnC. Interestingly, bovine cardiac TnC (CTnC), although it did not associate at pCa〉7.0, did associate and effectively activate force at pCa 〈 3.8, but dissociated on return to pCa〉7.0 (LR). Neither barnacle TnC isoform associated with TnC-depleted skinned fibres from rabbit skeletal muscle at pCa〉7.0, but did associate and activate these fibres at pCa〈3.8. Once these fibres were returned to LR and then placed in LA at pCa 3.8 all BTnC-restored force was lost, indicating a dissociation of BTnC once the Ca2+ is lowered, as observed with CTnC in barnacle myofibrillar bundles. Finally, the inhibitory effect of BTnI on force and the absence of an effect of calmodulin, trifluoperazine or ATP-γ-S on force were all taken as evidence for a thin filament regulated Ca2+ control system.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01738441
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