Cdc42 Contributes to Phorbol Ester-Induced Ca〔2+〕-Independent Contraction of Pulmonary Artery Smooth Muscle

• CHOI Won-Ho

  Department of Physiology and Anesthesiology, College of Medicine, Institute of Biomedical Science and Technology, Konkuk University

• KIM Jaeheung

  Department of Physiology and Anesthesiology, College of Medicine, Institute of Biomedical Science and Technology, Konkuk University

• LEE Youn Ri

  Department of Physiology and Anesthesiology, College of Medicine, Institute of Biomedical Science and Technology, Konkuk University

• LEE Chang-Kwon

  Department of Physiology and Anesthesiology, College of Medicine, Institute of Biomedical Science and Technology, Konkuk University

• KIM Yoon-Sun

  Department of Physiology and Anesthesiology, College of Medicine, Institute of Biomedical Science and Technology, Konkuk University

• KIM Junghwan

  Department of Physiology and Anesthesiology, College of Medicine, Institute of Biomedical Science and Technology, Konkuk University

• CHOI Yoon-Jung

  Department of Physiology and Anesthesiology, College of Medicine, Institute of Biomedical Science and Technology, Konkuk University

• WOO Nam-Sik

  Department of Physiology and Anesthesiology, College of Medicine, Institute of Biomedical Science and Technology, Konkuk University

• CHO SungIl

  Department of Physiology and Anesthesiology, College of Medicine, Institute of Biomedical Science and Technology, Konkuk University

• KIM Bokyung

  Department of Physiology and Anesthesiology, College of Medicine, Institute of Biomedical Science and Technology, Konkuk University

書誌事項

タイトル別名

• Cdc42 Contributes to Phorbol Ester-Induced Ca2+-Independent Contraction of Pulmonary Artery Smooth Muscle

抄録

We determined the contribution of the Rho family of low molecular GTP-binding proteins to phorbol ester-induced contraction in swine pulmonary artery smooth muscle. In Ca²⁺-free medium containing 1 mM EGTA, 12-deoxyphorbol 13-isobutyrate (DPB, 1 μM), a protein kinase C (PKC) activator, elicited sustained contractions, which were not inhibited by treatment with verapamil, a voltage-dependent Ca²⁺ channel antagonist, and Y27632, a Rho-associated kinase inhibitor. Immunoblot analysis showed three PKC isoforms (α, ε, and ζ) and two Rho GTPases (RhoA and Cdc42) in both cytosolic and the membrane fractions from quiescent strips. DPB (1 μM) significantly induced PKCα and ε to translocate from the cytosolic to the membrane fraction in Ca²⁺-free medium. DPB also elicited the translocation of Cdc42, but not RhoA to the membrane fraction. Similarly, in the experiment for measurement of Rho GTPase activity by pull-down assay, DPB (1 μM) significantly increased the activity of Cdc42 in Ca²⁺-free medium. Norepinephrine (NE, 10 μM) stimulated the redistribution of RhoA from the cytosolic to the membrane fraction in swine pulmonary artery smooth muscle. In contrast, NE did not alter the subcellular distributions of Cdc42 and the PKC isoforms. These results indicate that phorbol ester evokes PKC-mediated Ca²⁺-independent contraction via a Rho GTPase pathway, especially Cdc42, in smooth muscle from swine pulmonary arteries.<br>

収録刊行物

• Ｔｈｅ　Ｊｏｕｒｎａｌ　ｏｆ　Ｖｅｔｅｒｉｎａｒｙ　Ｍｅｄｉｃａｌ　Ｓｃｉｅｎｃｅ

  Ｔｈｅ　Ｊｏｕｒｎａｌ　ｏｆ　Ｖｅｔｅｒｉｎａｒｙ　Ｍｅｄｉｃａｌ　Ｓｃｉｅｎｃｅ 67 (8), 787-793, 2005

  公益社団法人 日本獣医学会

キーワード

• Ca²⁺-independent contraction
• Cdc42
• protein kinase C
• pulmonary artery smooth muscle

詳細情報

• CRID: 1390282681403304320
• NII論文ID: 110003983140
• NII書誌ID: AA10796138
• DOI: 10.1292/jvms.67.787
• ISSN: 13477439
• ISSN: 09167250
• NDL書誌ID: 7461171
• PubMed: 16141665
• Web Site: https://ndlsearch.ndl.go.jp/books/R000000004-I7461171
• Web Site: http://www.jstage.jst.go.jp/article/jvms/67/8/67_8_787/_pdf
• Web Site: https://search.jamas.or.jp/link/ui/2005267420
• 本文言語コード: en
• データソース種別:
  • JaLC
  • NDL
  • Crossref
  • PubMed
  • CiNii Articles
• 抄録ライセンスフラグ: 使用不可