Cdc42 Contributes to Phorbol Ester-Induced Ca2+-Independent Contraction of Pulmonary Artery Smooth Muscle
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- CHOI Won-Ho
- Department of Physiology and Anesthesiology, College of Medicine, Institute of Biomedical Science and Technology, Konkuk University
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- KIM Jaeheung
- Department of Physiology and Anesthesiology, College of Medicine, Institute of Biomedical Science and Technology, Konkuk University
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- LEE Youn Ri
- Department of Physiology and Anesthesiology, College of Medicine, Institute of Biomedical Science and Technology, Konkuk University
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- LEE Chang-Kwon
- Department of Physiology and Anesthesiology, College of Medicine, Institute of Biomedical Science and Technology, Konkuk University
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- KIM Yoon-Sun
- Department of Physiology and Anesthesiology, College of Medicine, Institute of Biomedical Science and Technology, Konkuk University
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- KIM Junghwan
- Department of Physiology and Anesthesiology, College of Medicine, Institute of Biomedical Science and Technology, Konkuk University
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- CHOI Yoon-Jung
- Department of Physiology and Anesthesiology, College of Medicine, Institute of Biomedical Science and Technology, Konkuk University
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- WOO Nam-Sik
- Department of Physiology and Anesthesiology, College of Medicine, Institute of Biomedical Science and Technology, Konkuk University
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- CHO SungIl
- Department of Physiology and Anesthesiology, College of Medicine, Institute of Biomedical Science and Technology, Konkuk University
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- KIM Bokyung
- Department of Physiology and Anesthesiology, College of Medicine, Institute of Biomedical Science and Technology, Konkuk University
Bibliographic Information
- Other Title
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- Cdc42 Contributes to Phorbol Ester-Induced Ca〔2+〕-Independent Contraction of Pulmonary Artery Smooth Muscle
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Abstract
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>
Journal
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- Journal of Veterinary Medical Science
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Journal of Veterinary Medical Science 67 (8), 787-793, 2005
JAPANESE SOCIETY OF VETERINARY SCIENCE
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Details 詳細情報について
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- CRID
- 1390282681403304320
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- NII Article ID
- 110003983140
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- NII Book ID
- AA10796138
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- ISSN
- 13477439
- 09167250
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- NDL BIB ID
- 7461171
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- PubMed
- 16141665
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- Text Lang
- en
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- Data Source
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- JaLC
- NDL
- Crossref
- PubMed
- CiNii Articles
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- Abstract License Flag
- Disallowed