Effects of adenine nucleotides on inositol 1,4,5-trisphosphate-induced calcium release in vascular smooth muscle cells.

Iino, Masamitsu

doi:10.1085/jgp.98.4.681

Cited by 96 publications

(59 citation statements)

References 26 publications

(55 reference statements)

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“…The present experiments indicate that both RyR and IP3R occur in ICCs. It has been proposed that some smooth muscles have distinct types of ER (endoplasmic reticulum) in terms of the distribution of RyR and IP3R (Iino, 1991;Yamazawa et al, 1992), but that other smooth muscles do not. Since application of either drugs related to RyR or IP 3R terminated [Ca 2+ ]i oscillations, both receptors appear to exist in the ER responsible for the periodic Ca 2+ release in ICCs.…”

Section: Discussionmentioning

confidence: 99%

Requirement of ryanodine receptors for pacemaker Ca2+ activity in ICC and HEK293 cells

Aoyama

Yamada

Wang

et al. 2004

Journal of Cell Science

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Intracellular Ca2+ ([Ca2+]i) oscillations seen in interstitial cells of Cajal (ICCs) are considered to be the primary pacemaker activity in the gut. Here, we show evidence that periodic Ca2+ release from intracellular Ca2+ stores produces [Ca2+]i oscillations in ICCs, using cell cluster preparations isolated from mouse ileum. The pacemaker [Ca2+]i oscillations in ICCs are preserved in the presence of dihydropyridine Ca2+ antagonists, which suppress Ca2+ activity in smooth muscle cells. However, applications of drugs affecting either ryanodine receptors or inositol 1,4,5-trisphosphate receptors terminated [Ca2+]i oscillations at relatively low concentrations. RT-PCR analyses revealed a predominant expression of type 3 RyR (RyR3) in isolated c-Kit-immunopositive cells (ICCs). Furthermore, we demonstrate that pacemaker-like global [Ca2+]i oscillation activity is endowed by introducing RyR3 into HEK293 cells, which originally express only IP3Rs. The reconstituted [Ca2+]i oscillations in HEK293 cells possess essentially the same pharmacological characteristics as seen in ICCs. The results support the functional role of RyR3 in ICCs.

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Section: Discussionmentioning

confidence: 99%

Requirement of ryanodine receptors for pacemaker Ca2+ activity in ICC and HEK293 cells

Aoyama

Yamada

Wang

et al. 2004

Journal of Cell Science

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“…In contrast, in only one set of experiments using reconstituted InsP 3 R channels was channel P o reportedly potentiated by MgATP to a similar extent as free ATP (31). Potentiating effects of MgATP on InsP 3 R channel activity were also reported in some Ca 2ϩ flux and fluorescence imaging studies (135,195,272), but such studies are complicated by multiple cellular effects of MgATP.…”

Section: Potentiation Of Insp 3 R Channel Activity By Other Nucleotidesmentioning

confidence: 98%

“…Other nucleotides have also been reported to potentiate InsP 3 R channel activity, including ADP (135,195,272,316,317), AMP (135,195,272,281,316,317), and GTP (31,195,272,281,316,317). Adenine and adenosine were also reported to be active (317).…”

Section: Potentiation Of Insp 3 R Channel Activity By Other Nucleotidesmentioning

confidence: 98%

“…However, the degree of potentiation by these agents reported varies considerably, in part probably because each of the studies was limited to determining channel activity at one arbitrarily selected Ca 2ϩ concentration. Furthermore, the existence of potentiating effects has been disputed for ADP (245,281), AMP (31), GTP (164), adenine (195), and adenosine (281). Some of this diversity may reflect differences in various isoforms studied (31,164,272).…”

Section: Potentiation Of Insp 3 R Channel Activity By Other Nucleotidesmentioning

confidence: 99%

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Inositol Trisphosphate Receptor Ca²⁺Release Channels

Foskett

White²,

Cheung³

et al. 2007

Physiological Reviews

1,067

1,334

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The inositol 1,4,5-trisphosphate (InsP3) receptors (InsP3Rs) are a family of Ca2+ release channels localized predominately in the endoplasmic reticulum of all cell types. They function to release Ca2+ into the cytoplasm in response to InsP3 produced by diverse stimuli, generating complex local and global Ca2+ signals that regulate numerous cell physiological processes ranging from gene transcription to secretion to learning and memory. The InsP3R is a calcium-selective cation channel whose gating is regulated not only by InsP3, but by other ligands as well, in particular cytoplasmic Ca2+. Over the last decade, detailed quantitative studies of InsP3R channel function and its regulation by ligands and interacting proteins have provided new insights into a remarkable richness of channel regulation and of the structural aspects that underlie signal transduction and permeation. Here, we focus on these developments and review and synthesize the literature regarding the structure and single-channel properties of the InsP3R.

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“…Thus, it is fascinating to speculate that the elaborated IP 3 R1 could act as a Ca 2ϩ -sensitive signaling molecule per se in addition to its function as a simple ligand-gated Ca 2ϩ channel. This conformational change also suggests that there is likely to be interplay between the Ca 2ϩ dependence of IP 3 R and both the allosteric regulation by ATP (55,56) and the cooperative gating by IP 3 (57).…”

Section: Ca 2ϩ -Sensitive Conformational Changes In Ip 3 Receptormentioning

confidence: 96%

Three-dimensional Rearrangements within Inositol 1,4,5-Trisphosphate Receptor by Calcium

Hamada

Terauchi

Mikoshiba

2003

Journal of Biological Chemistry

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, as reconstructed by three-dimensional electron microscopy, had a "mushroom-like" appearance consisting of a large square-shaped head and a small channel domain linked by four thin bridges. The projection image of the "headto-head" assembly comprising two particles confirmed the mushroom-like side view. The "windmill-like" form of IP 3 R1 with Ca 2؉ also contains the four bridges connecting from the IP 3 -binding domain toward the channel domain. These data suggest that the Ca 2؉ -specific conformational change structurally regulates the IP 3 -triggered channel opening within IP 3 R1.Inositol 1,4,5-trisphosphate receptor (IP 3 R) 1 acts as a highly controlled decoder transducing extracellular stimuli into intracellular calcium (Ca 2ϩ ) signals, a process that plays an integral role in vital morphogenesis and physiological plasticity (1). IP 3 Rs are structurally divided into three regions: 1) a large cytoplasmic region with an IP 3 binding pocket close to the N terminus; 2) a transmembrane region near the C terminus; and 3) a short C-terminal tail (2). The most characterized IP 3 R, type 1 IP 3 R (IP 3 R1), a predominant type in the cerebellar endoplasmic reticulum (ER) and spine apparatus, is a 2749-amino acid polypeptide (2) containing the IP 3 binding core (residues 226 -578) (3, 4), a transmembrane region composed of putative six-spanning domains (residues 2276 -2589) (5, 6). The transmembranous segments are essential for the tetramerization (7, 8) to form a channel domain as in the case of the voltage-, Ca 2ϩ -, and cyclic nucleotide-gated ion channel superfamily (9, 10).The IP 3 never fully opened the channel of IP 3 R without Ca 2ϩ . Previous functional analysis indicates that the low Ca 2ϩ level acts as an essential co-agonist for IP 3 -gated Ca 2ϩ release (11)(12)(13)(14). The requirement of the dual ligands is considered to be an important basis of the signaling cross-talk involved in the cell function (15). Thus, it would be useful to understand how the binding of co-agonists structurally opens the channel of IP 3 R. Recently, the x-ray structure of the crystallized IP 3 binding core has revealed the spatial relationship among a specific IP 3 -binding site and two plausible Ca 2ϩ -binding sites (4). The local allosteric coupling of IP 3 -and Ca 2ϩ -binding sites in this domain is thought to be one of the possible elements for the requirement of dual agonists to open the channel. However, additional six Ca 2ϩ -binding sites have been detected by extensive screening of expressed IP 3 R1-fragments outside the IP 3 binding core (16,17) and, based on the primary sequence, a critical residue for the Ca 2ϩ -activated channel opening was located far from the IP 3 binding core (18,19). Furthermore, allosteric sites for regulations were widely distributed outside the IP 3 binding core (20). Thus, it is quite important to visualize the overall behavior of tetrameric IP 3 R to elucidate the mechanism underlying channel gating by IP 3 and Ca 2ϩ . Knowledge of the spatial interrelations and rearrangements of the...

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Effects of adenine nucleotides on inositol 1,4,5-trisphosphate-induced calcium release in vascular smooth muscle cells.

Cited by 96 publications

References 26 publications

Requirement of ryanodine receptors for pacemaker Ca2+ activity in ICC and HEK293 cells

Requirement of ryanodine receptors for pacemaker Ca2+ activity in ICC and HEK293 cells

Inositol Trisphosphate Receptor Ca²⁺Release Channels

Three-dimensional Rearrangements within Inositol 1,4,5-Trisphosphate Receptor by Calcium

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Effects of adenine nucleotides on inositol 1,4,5-trisphosphate-induced calcium release in vascular smooth muscle cells.

Cited by 96 publications

References 26 publications

Requirement of ryanodine receptors for pacemaker Ca2+ activity in ICC and HEK293 cells

Requirement of ryanodine receptors for pacemaker Ca2+ activity in ICC and HEK293 cells

Inositol Trisphosphate Receptor Ca2+Release Channels

Three-dimensional Rearrangements within Inositol 1,4,5-Trisphosphate Receptor by Calcium

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Inositol Trisphosphate Receptor Ca²⁺Release Channels