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  • Title: Cyclic ADP-ribose-dependent Ca2+ release is modulated by free [Ca2+] in the scallop sarcoplasmic reticulum.
    Author: Panfoli I, Burlando B, Viarengo A.
    Journal: Biochem Biophys Res Commun; 1999 Apr 02; 257(1):57-62. PubMed ID: 10092509.
    Abstract:
    Cyclic ADP-ribose (cADPR) elicits calcium-induced calcium release (CICR) in a variety of cell types. We studied the effect of cADPR on Ca2+ release in muscle cells by incubating SR vesicles from scallop (Pecten jacobaeus) adductor muscle in the presence of the Ca2+ tracer fluo-3. Exposure of SR to cADPR (20 microM) produced Ca2+ release, which was a function of free [Ca2+] in a range between about 150 and 1000 nM, indicating an involvement of ryanodine-sensitive Ca2+ channels. This Ca2+ release was not significantly enhanced by calmodulin (7 micrograms/ml), but it was enhanced by equimolar addition of noncyclic ADPR. Also, the Ca2+ release elicited by cADPR/ADPR was a function of free [Ca2+] in a range between about 150 and 3000 nM, over which Ca2+ was inhibitory. cADPR self-inactivation was observed at low free [Ca2+] (about 150 nM), but it tended to disappear upon [Ca2+] elevation (about 250 nM). Caffeine or ryanodine induced a Ca2+ release which was ruthenium red (2.5 microM) sensitive at low [Ca2+]. However, the Ca2+ release induced by either ryanodine or cADPR was no longer ruthenium red sensitive when free [Ca2+] was increased. Based on these data, a model is proposed for Ca2+ signaling in muscle cells, where a steady-state cADPR level would trigger Ca2+ release when free [Ca2+] does reach a threshold slightly above its resting level, hence producing cascade RyR recruitment along SR cisternae from initial Ca2+ signaling sites.
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