Cyclic ADP-Ribose-Dependent Ca2+Release Is Modulated by Free [Ca2+] in the Scallop Sarcoplasmic Reticulum

1999 ◽  
Vol 257 (1) ◽  
pp. 57-62 ◽  
Author(s):  
Isabella Panfoli ◽  
Bruno Burlando ◽  
Aldo Viarengo
1997 ◽  
Vol 273 (3) ◽  
pp. H1082-H1089 ◽  
Author(s):  
P. Lahouratate ◽  
J. Guibert ◽  
J. F. Faivre

Cyclic ADP-ribose (cADPR), an endogenous metabolite of beta-NAD+, activates Ca2+ release from endoplasmic reticulum in sea urchin eggs via the ryanodine receptor (RyR) pathway. A similar role has been proposed in cardiac sarcoplasmic reticulum (SR), although this remains controversial. We therefore investigated the ability of cADPR to induce Ca2+ release from canine cardiac SR microsomes using fluo 3 to monitor extravesicular Ca2+ concentration. We found that cADPR induced Ca2+ release in a concentration-dependent manner, whereas neither its precursor, NAD+, nor its metabolite, ADP-ribose, elicited a consistent effect. In addition, an additive effect on calcium release between cADPR and 9-Me-7-Br-eudistomin-D (MBED), an activator of RyR, was found as well as no cross-desensitization between cADPR and MBED. Specific blockers of the RyR did not abolish the cADPR-induced Ca2+ release. These results provide evidence for cADPR-induced Ca2+ release from dog cardiac SR via a novel mechanism which is independent of RyR activation.


FEBS Letters ◽  
1993 ◽  
Vol 330 (3) ◽  
pp. 270-274 ◽  
Author(s):  
Jeffery Morrissette ◽  
Gary Heisermann ◽  
John Cleary ◽  
Arnold Ruoho ◽  
Roberto Coronado

1996 ◽  
Vol 270 (2) ◽  
pp. H801-H806 ◽  
Author(s):  
M. S. Kannan ◽  
A. M. Fenton ◽  
Y. S. Prakash ◽  
G. C. Sieck

Cyclic ADP-ribose (cADPR) was shown to induce calcium release from the endoplasmic reticulum via ryanodine-sensitive pathways. In smooth muscle, two pathways for calcium release from the sarcoplasmic reticulum (SR) have been previously demonstrated: D-myo-inositol 1, 4, 5-trisphosphate-gated and ryanodine-gated. However, evidence for cADPR as a regulator for SR Ca2+ release in smooth muscle is lacking. We used permeabilized porcine coronary artery smooth muscle cells to directly examine the stimulation of SR Ca2+ release by cADPR. The results provide direct evidence that cADPR stimulates SR Ca2+ release and that this response is not inhibited by heparin, by depletion of the caffeine-sensitive Ca2+ pool, or by blockade or ryanodine receptors. These results indicate a novel mechanism for Ca2+ release from the SR of vascular smooth muscle.


1995 ◽  
Vol 268 (5) ◽  
pp. C1235-C1240 ◽  
Author(s):  
R. Sitsapesan ◽  
A. J. Williams

It has been suggested that adenosine 5'-cyclic-diphosphoribose (cADPR) can activate only nonskeletal isoforms of the ryanodine-sensitive Ca2+ release channel. We now demonstrate that cADPR is an effective activator of sheep skeletal sarcoplasmic reticulum (SR) Ca2+ release channels incorporated into planar phospholipid bilayers in the presence of activating levels of cytosolic Ca2+. In addition, the precursor of cADPR, beta-NAD+, and the metabolite, adenosine diphosphoribose (ADP-ribose), also increase the open probability (Po) of skeletal SR Ca2+ release channels in micromolar concentrations. At low concentrations of cADPR (1 microM), the mechanism for the increase in Po is an increase in the frequency of channel openings with no increase in the duration of the open events. We also show that the effect of cADPR is dependent on luminal [Ca2+]. cADPR has no effect on Po when the luminal [Ca2+] is < 40 microM. However, at millimolar concentrations of luminal Ca2+, cADPR 1 and 10 microM) increases Po in the presence of activating cytosolic Ca2+.


1996 ◽  
Vol 79 (1) ◽  
pp. 147-151 ◽  
Author(s):  
Xiaoqing Guo ◽  
Michael A. Laflamme ◽  
Peter L. Becker

Author(s):  
R. A. Waugh ◽  
J. R. Sommer

Cardiac sarcoplasmic reticulum (SR) is a complex system of intracellular tubules that, due to their small size and juxtaposition to such electron-dense structures as mitochondria and myofibrils, are often inconspicuous in conventionally prepared electron microscopic material. This study reports a method with which the SR is selectively “stained” which facilitates visualizationwith the transmission electron microscope.


Author(s):  
James Junker ◽  
Joachim R. Sommer

Junctional sarcoplasmic reticulum (JSR) in all its forms (extended JSR, JSR of couplings, corbular SR) in both skeletal and cardiac muscle is always located at the Z - I regions of the sarcomeres. The Z tubule is a tubule of the free SR (non-specialized SR) which is consistently located at the Z lines in cardiac muscle (1). Short connections between JSR and Z lines have been described (2), and bundles of filaments at Z lines have been seen in skeletal (3) and cardiac (4) muscle. In opossum cardiac muscle, we have seen bundles of 10 nm filaments stretching across interfibrillary spaces and adjacent myofibrils with extensions to the plasma- lemma in longitudinal (Fig. 1) and transverse (Fig. 2) sections. Only an occasional single filament is seen elsewhere along a sarcomere. We propose that these filaments represent anchor fibers that maintain the observed invariant topography of the free SR and JSR throughout the contraction-relaxation cycle.


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