Isolation and partial cloning of ryanodine‐sensitive Ca<sup>2+</sup> release channel protein isoforms from human myometrial smooth muscle

Lynn, Stephen; Morgan, Joanna M.; Lamb, Heather K.; Meissner, Gerhard; Gillespie, James

doi:10.1016/0014-5793(95)00924-x

Cited by 35 publications

(33 citation statements)

References 39 publications

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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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“…IP 3 receptor types 1, 2 and 3 are expressed in human myometrium; IP 3 receptor concentration does not change in pregnancy (Rivera et al 1990;Morgan et al 1996). Myometrium also expresses type 2 and type 3 ryanodine receptors (Lynn et al 1995;Martin et al 1999a,b). These receptors are involved in calcium-induced calcium release from intracellular stores and have been suggested by some, but not all, studies to play a role in Ca 2+ i oscillations and general cellular calcium dynamics (Lynn et al 1993;Holda et al 1996;Phillippe & Basa, 1996;Burghardt et al 1999;Fu et al 2000).…”

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confidence: 99%

Hormones and Calcium: Mechanisms Controlling Uterine Smooth Muscle Contractile Activity

Sanborn¹

2001

Experimental Physiology

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The regulation of myometrial contraction is of paramount importance for the maintenance of pregnancy and for parturition. Understanding this regulation involves delineating the pathways that control myometrial contraction and relaxation and defining the regulation of these pathways. The pathways can be broken down further into those signalling cascades controlling the concentration of intracellular free calcium (Ca

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“…According to recent reports, at least in some types of smooth muscle cells (SMC), cADPR can elicit the [Ca 2ϩ ] i release (8,9) from sarcoplasmic reticulum and cell contraction (9). As in other muscle cells, the contraction of uterine myometrial smooth muscle cells (SMC) is regulated by increase in cytosolic Ca 2ϩ in part due to intracellular Ca 2ϩ release (10), and RyR was detected in myometrial SMC (11). An archetypal hormone of steroid superfamily, ␤-estradiol (E 2 ), enhances [Ca 2ϩ ] i release-mediated contractility of myometrial SMC in response to several hormones and autacoids (12).…”

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confidence: 99%

Effect of estrogen upon cyclic ADP ribose metabolism: β-Estradiol stimulates ADP ribosyl cyclase in rat uterus

Chini

Toledo

Thompson

et al. 1997

Proc. Natl. Acad. Sci. U.S.A.

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Cyclic ADP ribose (cADPR) has been shown to trigger Ca 2؉ release from intracellular stores through ryanodine receptor͞channel. In our previous study we observed that all-trans-retinoic acid stimulates cADPR synthesis by ADP ribose cyclase (ADPR cyclase) in cultured epithelial cells. We have now investigated whether cADPR may play a signaling role in action of ␤-estradiol (E 2 ), an archetypal steroid superfamily hormone, upon its major target organ, uterus, in vivo. Administration of E 2 to gonadectomized rats (0.2 mg͞kg per day for 7 days) resulted in an Ϸ⌬ ؉ 300% increase of ADPR cyclase activity in extracts from uterus, but in liver, brain, or skeletal muscle ADPR cyclase was unchanged. Most of the E 2 -stimulated uterine ADPR cyclase was associated with membranes. The higher ADPR cyclase activity in response to E 2 was due to the increase of V MAX without change in K m . Simultaneous administration of estrogen antagonist tamoxifen (8 mg͞kg per day) with E 2 (0.2 mg͞kg per day) prevented an increase in ADPR cyclase. In uterine extracts from E 2 -treated rats, the rate of cADPR inactivation by cADPR hydrolase and the activity of NADase was increased, but to a much lesser degree than activity of ADPR cyclase. Our results indicate that E 2 , via action to its nuclear receptors in vivo, increases ADPR cyclase activity in uterus. We propose that some of the estrogen effects, and by extension the effects of other steroid superfamily hormones, upon specialized cellular functions and upon hormone-induced gene expression in target cells, are mediated by cADPR-Ca 2؉ release pathway.

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

Cited by 35 publications

References 39 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

Hormones and Calcium: Mechanisms Controlling Uterine Smooth Muscle Contractile Activity

Effect of estrogen upon cyclic ADP ribose metabolism: β-Estradiol stimulates ADP ribosyl cyclase in rat uterus

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

Cited by 35 publications

References 39 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

Hormones and Calcium: Mechanisms Controlling Uterine Smooth Muscle Contractile Activity

Effect of estrogen upon cyclic ADP ribose metabolism: β-Estradiol stimulates ADP ribosyl cyclase in rat uterus

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