Effects of photoreleased cADP-ribose on calcium transients and calcium sparks in myocytes isolated from guinea-pig and rat ventricle

Cui, Yi; Galione, Antony; Terrar, Derek A.

doi:10.1042/bj3420269

Cited by 54 publications

(30 citation statements)

References 23 publications

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“…At a higher concentration (500 µM), cADPR also failed to affect the rate of Ca 2+ removal when photolysed up to 10 seconds before depolarization but significantly increased the rate when photolysed 15 seconds beforehand (P<0.05; Table 2), a time consistent with the delays inherent in cADPR effects (e.g. Cui et al, 1999); the reason for the delay is not understood.…”

Section: Effect Of Cadpr On [Ca 2+ ]C Declinementioning

confidence: 54%

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Cyclic ADP-ribose increases Ca2+ removal in smooth muscle

Bradley

Currie

MacMillan

et al. 2003

Journal of Cell Science

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Ca2+ release via ryanodine receptors (RyRs) is vital in cell signalling and regulates diverse activities such as gene expression and excitation-contraction coupling. Cyclic ADP ribose (cADPR), a proposed modulator of RyR activity, releases Ca2+ from the intracellular store in sea urchin eggs but its mechanism of action in other cell types is controversial. In this study, caged cADPR was used to examine the effect of cADPR on Ca2+ signalling in single voltage-clamped smooth muscle cells that have RyR but lack FKBP12.6, a proposed target for cADPR. Although cADPR released Ca2+ in sea urchin eggs (a positive control), it failed to alter global or subsarcolemma [Ca2+]c, to cause Ca2+-induced Ca2+ release or to enhance caffeine responses in colonic myocytes. By contrast, caffeine (an accepted modulator of RyR) was effective in these respects. The lack of cADPR activity on Ca2+ release was unaffected by the introduction of recombinant FKBP12.6 into the myocytes. Indeed in western blots, using brain membrane preparations as a source of FKBP12.6, cADPR did not bind to FKBPs, although FK506 was effective. However, cADPR increased and its antagonist 8-bromo-cADPR slowed the rate of Ca2+ removal from the cytoplasm. The evidence indicates that cADPR modulates [Ca2+]c but not via RyR; the mechanism may involve the sarcolemma Ca2+ pump

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Section: Effect Of Cadpr On [Ca 2+ ]C Declinementioning

confidence: 54%

“…This delay was attributed to the time required for the SR Ca 2+ content to be increased following SERCA activation by cADPR (Lukyanenko et al, 2001). This proposal could explain the frequently observed pronounced delay in the onset of cADPR activity (Cui et al, 1999;Aarhus et al, 1995;Li et al, 2000).…”

mentioning

confidence: 76%

Cyclic ADP-ribose increases Ca2+ removal in smooth muscle

Bradley

Currie

MacMillan

et al. 2003

Journal of Cell Science

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“…This proposal has not been effectively countered by studies on ventricular myocytes, which exclusively express RyR2. This is due to the fact that the principal regulatory effect of cADPR with respect to RyR2 is to increase the sensitivity of this RyR subtype to Ca 2ϩ -induced Ca 2ϩ release (8,9), and in light of the fact that the sensitivity of RyRs to Ca 2ϩ -induced Ca 2ϩ release may be augmented by an increase in Ca 2ϩ concentration within the cytoplasm and/or S/ER lumen (15).…”

Section: Intracellular Camentioning

confidence: 99%

“…Although a wealth of evidence across a variety of cell types (3)(4)(5)(6)(7)(8)(9) supports the original proposal that cADPR activates RyRs (10), studies on reconstituted RyRs in lipid bilayers have failed to conclusively demonstrate direct regulation of these channels by cADPR (11), and it has been suggested that cADPR may initiate Ca 2ϩ signals via RyRs and IP 3 Rs by promoting Ca 2ϩ uptake into the S/ER by S/ER Ca 2ϩ ATPases (SERCA) (12)(13)(14). This proposal has not been effectively countered by studies on ventricular myocytes, which exclusively express RyR2.…”

Section: Intracellular Camentioning

confidence: 99%

Cyclic Adenosine Diphosphate Ribose Activates Ryanodine Receptors, whereas NAADP Activates Two-pore Domain Channels

Ogunbayo

Zhu

Rossi

et al. 2011

Journal of Biological Chemistry

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The mechanism by which cyclic adenosine diphosphate ribose (cADPR) and nicotinic acid adenine dinucleotide phosphate (NAADP) mobilize intracellular Ca 2؉ Intracellular Ca 2ϩ signals are initiated by Ca 2ϩ release from intracellular stores, and traditionally, the sarco/endoplasmic reticulum (S/ER) 2 has been considered to be the major releasable store. From this store, Ca 2ϩ may be released through the opening of inositol 1,4,5-trisphosphate receptors (IP 3 Rs) and/or ryanodine receptors (RyRs), the two groups of intracellular Ca 2ϩ release channels located on S/ER membranes. It is generally accepted that of the recognized Ca 2ϩ -mobilizing second messengers, inositol 1,4,5-trisphosphate facilitates this process by activating IP 3 Rs (1).By contrast, the mechanism by which the pyridine nucleotides cyclic adenosine diphosphate ribose (cADPR) and nicotinic acid adenine dinucleotide phosphate (NAADP) (2) mobilize intracellular Ca 2ϩ stores remains controversial. Although a wealth of evidence across a variety of cell types (3-9) supports the original proposal that cADPR activates RyRs (10), studies on reconstituted RyRs in lipid bilayers have failed to conclusively demonstrate direct regulation of these channels by cADPR (11), and it has been suggested that cADPR may initiate Ca 2ϩ signals via RyRs and IP 3 Rs by promoting Ca 2ϩ uptake into the S/ER by S/ER Ca 2ϩ ATPases (SERCA) (12)(13)(14). This proposal has not been effectively countered by studies on ventricular myocytes, which exclusively express RyR2. This is due to the fact that the principal regulatory effect of cADPR with respect to RyR2 is to increase the sensitivity of this RyR subtype to Ca 2ϩ -induced Ca 2ϩ release (8, 9), and in light of the fact that the sensitivity of RyRs to Ca 2ϩ -induced Ca 2ϩ release may be augmented by an increase in Ca 2ϩ concentration within the cytoplasm and/or S/ER lumen (15).The mechanism by which NAADP triggers intracellular Ca 2ϩ release has also been hotly debated. We recently identified a family of two-pore domain channels (TPC1-3, TPCN1-3 for gene name) as endolysosome-targeted, NAADP-gated Ca 2ϩ release channels (16, 17), and our findings have since been confirmed by others (18,19

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“…In contrast, a study carried out in rat ventricular myocytes using caged cADPR suggests that cADPR does not regulate sarcoplasmic reticulum Ca 2ϩ release (25). However, work from several groups strongly suggests the following possibilities for cardiac myocytes: (i) that the enzymatic machinery for synthesis of cADPR is expressed (26,27); (ii) that cADPR increases both the amplitude of whole cell Ca 2ϩ transients and the frequency of Ca 2ϩ sparks in rat and guinea pig isolated myocytes (28); and (iii) that Ca 2ϩ signaling and contractions in electrically driven guinea pig or rat cardiac myocytes are sensitive to the specific cADPR antagonists 8-NH 2 -cADPR and 8-Br-cADPR (29,30).…”

Section: Discussionmentioning

confidence: 79%