A novel ryanodine sensitive calcium release mechanism in cultured human myometrial smooth‐muscle cells

Lynn, Stephen; Morgan, Joanna M.; Gillespie, James; Greenwell, J. R.

doi:10.1016/0014-5793(93)80279-4

Cited by 39 publications

(32 citation statements)

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“…For example, fura-2 and 45 Ca 2ϩ efflux measurements revealed that Ca 2ϩ release from intracellular stores of human uterine smooth muscle cells was ryanodine-sensitive but caffeine-insensitive (62,63). In addition, ryanodine caused an increase in intracellular Ca 2ϩ concentrations in human Jurkat T-lymphocytes that express RyR3, but caffeine did not (64).…”

Section: Discussionmentioning

confidence: 99%

Functional Characterization of the Recombinant Type 3 Ca2+ Release Channel (Ryanodine Receptor) Expressed in HEK293 Cells

Chen

Ebisawa

et al. 1997

Journal of Biological Chemistry

160

171

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To investigate the channel properties of the mammalian type 3 ryanodine receptor (RyR3), we have cloned the RyR3 cDNA from rabbit uterus by reverse transcriptase-polymerase chain reaction and expressed the cDNA in HEK293 cells. Immunoblotting studies showed that the cloned RyR3 was indistinguishable from the native mammalian RyR3 in molecular size and immunoreactivity. Ca 2؉ release measurements using the fluorescence Ca 2؉ indicator fluo 3 revealed that the cloned RyR3 functioned as a caffeine-and ryanodine-sensitive Ca 2؉ Ryanodine receptors are a family of intracellular Ca 2ϩ release channels that were originally identified in the sarcoplasmic reticulum (SR) 1 of striated muscles. To date, three members of this family have been identified in mammalian tissues, namely the skeletal muscle (RyR1), the cardiac muscle (RyR2), and the brain (RyR3) ryanodine receptor. These proteins are the products of different genes and share 66 -70% amino acid sequence identity (1-5). Earlier studies using RNA blot analysis revealed that the expression patterns of these isoforms were very different (6). RyR1 was predominantly expressed in skeletal muscle, whereas RyR2 was mainly expressed in heart and brain. The expression of RyR3 was detected in smooth muscle tissues and certain regions of the brain. However, results of recent ribonuclease protection assay demonstrate that all three RyR isoforms are widely and differentially expressed (7). These studies also indicate that most tissues express more than one RyR isoform. For example, skeletal muscles express both RyR1 and RyR3, although RyR3 is expressed at a much lower level than that of RyR1.

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Section: Discussionmentioning

confidence: 99%

Functional Characterization of the Recombinant Type 3 Ca2+ Release Channel (Ryanodine Receptor) Expressed in HEK293 Cells

Chen

Ebisawa

et al. 1997

Journal of Biological Chemistry

160

171

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“…Microspectrofluorimetry of intact cultured myometrial cells with Fura-2 suggested that a ryanodine-sensitive, caffeine-insensitive Ca 2+ release mechanism may be operational [8]. In order to directly demonstrate a caffeine-insensitive, ryanodine-sensitive Ca 2+ release activity, the non-mitochondrial stores of permeabilised human myometrial cells were loaded with 45Ca 2+.…”

Section: Effects Of Ryanodine and Caffeinementioning

confidence: 99%

“…Previous work on cultured human myometrial cells has demonstrated that a ryanodinesensitive Ca > release mechanism is operational [8] and preliminary studies indicate the expression and isolation of a ryanodine binding protein in both myometrial cultured cells and whole tissue [9].…”

Section: Introductionmentioning

confidence: 99%

Isolation and partial cloning of ryanodine‐sensitive Ca²⁺ release channel protein isoforms from human myometrial smooth muscle

et al. 1995

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Partial cDNAs of the ryanodine receptor were cloned using PCR analysis from reverse transcribed total and mRNA, extracted from freshly isolated pregnant, non-pregnant, and cultured human myometrial smooth muscle. The identity of these clones was confirmed by nucleotide sequencing of the fragments and indicate the expression of both the skeletal and brain ryanodine receptor isoforms in these preparations. In freshly isolated non-pregnant myometrial tissue, membrane fractions displaying specific [3H]ryanodine binding activities were isolated using density gradient centrifugation. SDS-PAGE of the sucrose gradient fractions indicated the specific comigration of a polypeptide with a molecular mass of~544 kDa with the ryanodine binding activity.

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“…We have previously reStudies in the rat vascular smooth muscle cell line A7r5 indicate ported that a ryanodine-sensitive, caffeine-insensitive Ca -,+ rethat the two receptors may operate functionally and spatially lease mechanism is present in intact human myometrial smooth distinct Ca 2÷ stores [28]. However, the use of this cell line may muscle cells [15]. Molecular cloning of RyR-specific transcripts require care in the interpretation of results obtained.…”

Section: Effect Of Ryanodine and Caffeine On 45ca2+ Releasementioning

confidence: 99%

“…Microspecinflux pathways and the mobilisation of Ca 2÷ from an intraceltrofluorimetry studies using intact myometrial smooth muscle lular Ca 2÷ store, the sarcoplasmic reticulum (SR). In human cells indicate that a ryanodine-sensitive but caffeine-insensitive uterine artery vascular smooth muscle cells agonists such as Ca 2+ release mechanism may be operational [15]. Therefore, to histamine can activate repetitive oscillations in intracellular investigate directly the activation of these complex responses Ca 2+ in the absence of external Ca 2÷ [1].…”

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confidence: 99%

Basic properties of a novel ryanodine‐sensitive, caffeine‐insensitive calcium‐induced calcium release mechanism in permeabilised human vascular smooth muscle cells

Lynn

Gillespie

1995

FEBS Letters

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tion varies among smooth muscle tissues [5]. Caffeine has been Abstract The efllux of 45Ca2+ from preloaded intracellular the accepted means with which to identify Ca2+-induced Ca 2+ stores of saponin-permeabilised human uterine artery smooth release (CICR) in many excitable cells, however, both human muscle cultured cells was used to study the mechanisms nnderlyvascular and myometrial smooth muscle cells do not respond ing Ca 2+ release from the sarcoplasmic reticulum (SR). The present paper demonstrates directly a functional Ca 2+ release mechato caffeine with a release of intracellular Ca 2+ [6]. The IP 3 nism that is dependent on an increase in free Ca 2÷ (100 nM-30 receptor can be activated by IP 3 and Ca 2+, and has been shown pM) and is completely inhibited by 20 pM Ruthenium red. The to be inhibited by caffeine in some cells [3]. The IP 3 receptor amount of Ca 2+ released at 30 pM free Ca 2÷ was reduced by is capable of considerable variability in the sensitivity of IP 3-approximately 50% compared to the release at 10 ~M. This induced Ca 2+ release, which may give rise to the phenomenon Ca2+-induced Ca 2+ release (CICR) mechanism was not sensitive of quantal Ca 2+ release [7]. These variations may depend on to caffeine. Exposure of cells to low free Ca2+-containing solureceptor types differently expressed from different gene prodtions (10 nM) indicated that a component of the CICR mechaucts, alternative splicing or from co-expression of different IP 3 nism may be functional at basal free Ca 2+ levels of 100 nM.receptor subtypes in a single cell [8,9]. The inhibitory action of Application of ryanodine (0.1-100 /tM) induced 45Ca2+ efflux caffeine has also been explained by the reduction of IP 3 producfrom the sarcoplasmic retlculum and this release was also inhibited by 20 ~M Ruthenium red.tion in a dose-dependent manner [10]. Parker and Ivorra using Xenopus oocytes found that caffeine inhibited responses to IP3 Key words." CICR; Ryanodine; Saponin; Smooth muscle; and this may be explained by an antagonistic effect of binding Human vascular of IP 3 to its receptor [11]. The RyR has been studied predominantly in cardiac and skeletal muscle and is sensitive to Ca 2+, Mg 2+ and ATP and may be modulated by calmodulin and activated by caffeine [12]. The 1. Introduction physiological role of the RyR in smooth muscle is uncertain, however CICR, which is presumed to be the mechanism of The processes underlying smooth muscle contraction can RyR-induced Ca 2+ release in cardiac tissue [13], has been suginvolve the activation of voltage and receptor operated Ca 2+ gested to occur in skinned smooth muscle [14]. Microspecinflux pathways and the mobilisation of Ca 2÷ from an intraceltrofluorimetry studies using intact myometrial smooth muscle lular Ca 2÷ store, the sarcoplasmic reticulum (SR). In human cells indicate that a ryanodine-sensitive but caffeine-insensitive uterine artery vascular smooth muscle cells agonists such as Ca 2+ release mechanism may be operational [15]. Therefore, to histamine can activate repetit...

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A novel ryanodine sensitive calcium release mechanism in cultured human myometrial smooth‐muscle cells

Cited by 39 publications

References 20 publications

Functional Characterization of the Recombinant Type 3 Ca2+ Release Channel (Ryanodine Receptor) Expressed in HEK293 Cells

Functional Characterization of the Recombinant Type 3 Ca2+ Release Channel (Ryanodine Receptor) Expressed in HEK293 Cells

Isolation and partial cloning of ryanodine‐sensitive Ca²⁺ release channel protein isoforms from human myometrial smooth muscle

Basic properties of a novel ryanodine‐sensitive, caffeine‐insensitive calcium‐induced calcium release mechanism in permeabilised human vascular smooth muscle cells

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A novel ryanodine sensitive calcium release mechanism in cultured human myometrial smooth‐muscle cells

Cited by 39 publications

References 20 publications

Functional Characterization of the Recombinant Type 3 Ca2+ Release Channel (Ryanodine Receptor) Expressed in HEK293 Cells

Functional Characterization of the Recombinant Type 3 Ca2+ Release Channel (Ryanodine Receptor) Expressed in HEK293 Cells

Isolation and partial cloning of ryanodine‐sensitive Ca2+ release channel protein isoforms from human myometrial smooth muscle

Basic properties of a novel ryanodine‐sensitive, caffeine‐insensitive calcium‐induced calcium release mechanism in permeabilised human vascular smooth muscle cells

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Isolation and partial cloning of ryanodine‐sensitive Ca²⁺ release channel protein isoforms from human myometrial smooth muscle