Integrity of actin-network is involved in uridine 5′-triphosphate evoked store-operated Ca<sup>2+</sup> entry in bovine adrenocortical fasciculata cells
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- Kawamura Masahiro
- Department of Pharmacology (I), Jikei University School of Medicine
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- Terasaka Osamu
- Division of Biology, Jikei University School of Medicine
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- Ebisawa Takanori
- Department of Pharmacology (I), Jikei University School of Medicine
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- Kondo Ichiro
- Department of Pharmacology (I), Jikei University School of Medicine
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- Masaki Eiji
- Department of Pharmacology (I), Jikei University School of Medicine
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- Ahmed Ashram
- Department of Anesthesiology, Ain Shams University
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- Kagata Miyuki
- Department of Pharmacology (I), Jikei University School of Medicine
書誌事項
- タイトル別名
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- Integrity of Actin-Network Is Involved in Uridine 5'-Triphosphate Evoked Store-Operated Ca2+ Entry in Bovine Adrenocortical Fasciculata Cells.
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抄録
Store-operated Ca2+ entry channels (SOCs) play an important role in the regulation of diverse non-excitable cell functions. However, the precise mechanism of SOCs activation is still controversial. Uridine 5'-triphosphate (UTP) was shown to induce Ca2+ entry in a dihydropyridines-insensitive manner and accelerated steroidogenesis in bovine adrenocortical fasciculata cells (BAFCs) via the Gq/11 protein-coupled P2Y2 receptor. Therefore we investigated whether UTP is involved in SOCs activation and the mechanism of UTP-induced SOCs activation. Fura 2-loaded BAFCs were used for the measurement of intracellular concentration of Ca2+ ([Ca2+]i) mobilization. Extracellular UTP evoked Ca2+ release from intracellular stores followed by an increase in Ca2+ entry. The Ca2+ influx elicited by UTP was inhibited not by nifedipine, but by Zn2+, Cd2+, and Ni2+ (potency order: Zn2+ > Cd2+ >> Ni2+), and the effect of UTP was also attenuated by a phospholipase C inhibitor (U73122). These results indicate that UTP activates SOCs in BAFCs. The increase in [Ca2+]i by UTP was attenuated by ML-9, a myosin-light chain kinase inhibitor, and calmodulin inhibitors, W-7 and E6 berbamine, in a concentration-dependent manner. These reagents depolymerized actin filaments with rhodamine staining in BAFCs. Cytochalasin D also inhibited UTP-activated SOCs and depolymerized actin filaments. From these results, we proposed that calcium/calmodulin dependent myosin-light chain kinase is involved in the mobilization of actin filaments and the integrity of actin-network plays an important role in UTP-induced SOCs activation in BAFCs.<br>
収録刊行物
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- Journal of Pharmacological Sciences
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Journal of Pharmacological Sciences 91 (1), 23-33, 2003
公益社団法人 日本薬理学会
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詳細情報 詳細情報について
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- CRID
- 1390001205176658304
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- NII論文ID
- 130000073725
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- NII書誌ID
- AA11806667
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- ISSN
- 13478648
- 13478613
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- NDL書誌ID
- 6494411
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- PubMed
- 12686727
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- 本文言語コード
- en
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- データソース種別
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- JaLC
- NDL
- Crossref
- PubMed
- CiNii Articles
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- 抄録ライセンスフラグ
- 使用不可