ADP-ribosyl cyclase couples to cyclic AMP signaling in the cardiomyocytes

Xie, Guang-Hua; Rah, So-Young; Kim, Sang-Jin; Nam, Tae-Sik; Ha, Ki-Chan; Chae, Soo‐Wan; Im, Mie‐Jae; Kim, Uh-Hyun

doi:10.1016/j.bbrc.2005.03.114

Cited by 34 publications

(34 citation statements)

References 31 publications

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“…Several studies using H89 as PKA inhibitor, used the compound at concentrations of 10 ìM or higher (see for example ref. 23,63,80), However, at 10 ìM, H89 has been shown to affect ROCK II (49), the sarcoplasmic reticulum Ca 2+ -uptake (47), K + channels (72), and phosphatidylcholine biosynthesis (78), without involvement of PKA. In studies on the Golgi network, H89 was used at a concentration of 50-100 ìM (38,48,58).…”

Section: Discussionmentioning

confidence: 99%

“…It is wellestablished that the PKA signalling cascade is of major importance for cellular function and accounts for the intense interest in a specific, high affinity inhibitor. A recent survey of the literature showed that H89 has been used extensively for evaluation of the role of PKA in heart muscle (63,80), osteoblasts (41,61), hepatocytes (23,82), smooth muscle cells (24,70), neuronal tissue (42,44), epithelial cells (11,69), to name but a few. No fewer than 1500 articles have appeared on this subject.…”

Section: Introductionmentioning

confidence: 99%

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The Many Faces of H89: A Review

Lochner

Moolman

2006

Cardiovascular Drug Reviews

288

230

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H89 is marketed as a selective and potent inhibitor of protein kinase A (PKA). Since its discovery, it has been used extensively for evaluation of the role of PKA in the heart, osteoblasts, hepatocytes, smooth muscle cells, neuronal tissue, epithelial cells, etc. Despite the frequent use of H89, its mode of specific inhibition of PKA is still not completely understood. It has also been shown that H89 inhibits at least 8 other kinases, while having a relatively large number of PKA-independent effects which may seriously compromise interpretation of data.Thus, while recognizing its kinase inhibiting properties, it is advised that H89 should not be used as the single source of evidence of PKA involvement. H-89 should be used in conjunction with other PKA inhibitors, such as Rp-cAMPS or PKA analogs.

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

The Many Faces of H89: A Review

Lochner

Moolman

2006

Cardiovascular Drug Reviews

288

230

View full text Add to dashboard Cite

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“…However, cGMP-independent cADPR synthesis had also been found in the eggs [130]. In mammalian cells, both cGMP- [110,[131][132][133] and cAMP-dependent [134][135][136][137] cADPR-synthesis have been reported. Likewise, in lymphokine-activated killer cells, NAADP synthesis is stimulated by both cAMP and cGMP [110].…”

Section: Membrane Topology and Regulation Of Cd38mentioning

confidence: 99%

Cyclic ADP-ribose and NAADP: fraternal twin messengers for calcium signaling

Lee

2011

Sci. China Life Sci.

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The concept advanced by Berridge and colleagues that intracellular Ca 2+ -stores can be mobilized in an agonist-dependent and messenger (IP 3 )-mediated manner has put Ca 2+ -mobilization at the center stage of signal transduction mechanisms. During the late 1980s, we showed that Ca 2+ -stores can be mobilized by two other messengers unrelated to inositol trisphosphate (IP 3 ) and identified them as cyclic ADP-ribose (cADPR), a novel cyclic nucleotide from NAD, and nicotinic acid adenine dinucleotide phosphate (NAADP), a linear metabolite of NADP. Their messenger functions have now been documented in a wide range of systems spanning three biological kingdoms. Accumulated evidence indicates that the target of cADPR is the ryanodine receptor in the sarco/endoplasmic reticulum, while that of NAADP is the two pore channel in endolysosomes.As cADPR and NAADP are structurally and functionally distinct, it is remarkable that they are synthesized by the same enzyme. They are thus fraternal twin messengers. We first identified the Aplysia ADP-ribosyl cyclase as one such enzyme and, through homology, found its mammalian homolog, CD38. Gene knockout in mice confirms the important roles of CD38 in diverse physiological functions from insulin secretion, susceptibility to bacterial infection, to social behavior of mice through modulating neuronal oxytocin secretion. We have elucidated the catalytic mechanisms of the Aplysia cyclase and CD38 to atomic resolution by crystallography and site-directed mutagenesis. This article gives a historical account of the cADPR/NAADP/CD38-signaling pathway and describes current efforts in elucidating the structure and function of its components.cyclic ADP-ribose, cADPR, NAADP, nicotinic acid adenine dinucleotide phosphate, CD38, ADP-ribosyl cyclase, Calcium mobilization and signaling Citation:Lee H C. Cyclic ADP-ribose and NAADP: fraternal twin messengers for calcium signaling. Sci China Life Sci, 2011Sci, , 54: 699 -711, doi: 10.1007 In 1983, Berridge and colleagues published a study showing that agonists, such as carbachol, can activate Ca 2+ release from non-mitochondrial Ca 2+ stores and the effect is mediated by a Ca 2+ messenger, inositol 1,4,5-trisphosphate (IP 3 ) [1]. The targeted Ca 2+ stores were later identified as the endoplasmic reticulum (ER), which has since been shown to be the major intracellular Ca 2+ stores. This seminal study ushered in the current field of Ca 2+ signaling as we know it and has made the field center stage. IP 3 is derived from a phospholipid, phosphatidyl inositol 4,5-bisphosphate, present on the cytoplasmic side of the plasma membrane. Agonist binding to its specific receptor leads to activation of phospholipase C and the hydrolysis of the phospholipid, releasing the head group that is IP 3 . The structure of IP 3 is shown in Figure 1. It has three phosphates on the inositol ring. Both the number of phosphates and the position of the phosphates are critical to the binding of IP 3 to its receptor in the ER. The space-filling model of IP 3 shown in Figu...

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“…Briefly, cardiomyocytes attached to laminine-coated plates were loaded with 5 µM Fluo 3-AM (Molecular Probe, Eugene, OR) in KH buffer containing 1% BSA at 37 o C for 30 min, and the plates were washed three times with KH buffer and used for the treatment with various drugs. SR Ca 2+ channel blockers, ryanodine (20 µM) (Xie et al, 2005) and dantrolene (2 µM) (Buyukokuroglu et al, 2004) and antioxidants, α-lipoic acid (100 µM) (Cao et al, 2003) and α-tocopherol (100 µM) (Ulker et al, 2003) were preincubated at 37 o C for 20 min prior to treatment with DOX (3 µM). Signal of [Ca 2+ ]i in cardiomyocytes was measured every 6 s for 90 min on confocal microscope (Nikon) equipped with air-cooled argon laser system.…”

Section: +mentioning

confidence: 99%