| mayumi hirano | Last modified date：2013.5.21 |
Assistant Professor /
Science for Biological Information
Department of Basic Medicine
Faculty of Medical Sciences
Department of Basic Medicine
Faculty of Medical Sciences
Graduate School
Other Organization
Homepage
[URL]
Division of Molecular Cardiology, Research Institute of Angiocardiology,
Graduate School of Medical Sciences, Kyushu University.
Phone
092-642-5550
Fax
092-642-5552
Academic Degree
PhD
Field of Specialization
Cell Biology
Outline Activities
Elucidation of the intracellular signal networks involved in the growth arrest induced by Cell-cell contact in vascular endothelial cells.
Role of endothelial proteinase-activated receptors in the early phase of the development of vascular lesions.
Role of endothelial proteinase-activated receptors in the early phase of the development of vascular lesions.
Research
Research Interests
Membership in Academic Society
- A study elucidated the role of proteinase-activated receptors(PARs) in the early phase of the development of atherosclerotic vascular lesions
keyword : Endothelial cells, Thrombin, Proteinase-activated receptor, Ateriosclerosis, NO
2008.04. - A study elucidating the molecular mechanism for the activation of vascular endothelial cells by thrombin
keyword : Endothelial cells, MLC phosphorylation, Myosin phophatase, Actin stress fiber,Permeability
2008.07. - Stromal interaction molecule-1 (STIM1) plays an important role in the thrombin-induced Ca2+ signal and Ca2+-dependent NO production in endothelial cells.
keyword : Endothelial cells, Ca influx, Ca Store
2007.04. - A study elucidating the mechanism underlying the production of nitric oxide by thrombin in vascular endothelial cells
keyword : Endothelial cells, Proteinase-activated receptor, Thrombin, NO, Ca
2003.04. - A study elucidating the mechanisms regulating the transcription of the cell cycle regulatory protein p27Kip1 in the cell-cell contact-induced growth arrest of vascular endothelial cells.
keyword : Endothelial cells, Cell-cell contact, Growth arrest, Cell cycle, Transcription, Rac1
2001.04. - A study elucidating the molecular mechanism of the growth arrest by the formation of cell-cell contact in vascular endothelial cells.
keyword : Endothelial cells, Cell-cell contact, Growth arrest, Cell cycle, Transcriptional up-regulation
1997.04～2001.03.
- Elucidation of the intracellular signal networks involved in the growth arrest induced by cell-cell contact in vascular endothelial cells.
- Effect of gravitational alteration on the structure and function of vascular system
Books
| 1. | Hirano K, Hirano M, Abe S and Kanaide H.,Cytosolic calcium transients in vascular smooth muscle. in Ion Channels of Vascular Smooth Muscle Cells and Endothelial Cells, eds Sperelakis N and Kuriyama H., Elsivier, New York,,93-105,,1991.01. |
Papers
| 1. | Katsuharu Kameda, Yuichiro Kikkawa, mayumi hirano, S Matsuo, Tomio Sasaki, Hideo Kanaide,Combined argatroban and anti-oxidative agents prevents increased vascular contractility to thrombin and other ligands after subarachnoid hemorrhage2+-sensitivity and induces vasoconstriction in porcine pulmonary arteries.,Br J Pharmacol,No.165 ,2012.01. |
| 2. | Hirano K, Hirano M, Hanada A:,Involvement of STIM1 in the proteinase-activated receptor 1-mediated Ca2+ influx in vascular endothelial cells.,J Cell Biochem,Vol.108,pp.499-507,2009.09. |
| 3. | Maeda Y, Hirano K, Hirano M, Kikkawa Y, Kameda K, Sasaki T, Kanaide H,Enhanced contractile response of the basilar artery to platelet-derived growth factor in subarachnoid hemorrhage.,Stroke 40, 591-596, 2009,Vol.40,pp.591-596,2009.02. |
| 4. | Hirano M, Kanaide H, Hirano K,Rac1-dependent transcriptional up-regulation of p27Kip1 by homophilic cell-cell contact in vascular endothelial cells.,Biochim Biophys Acta -Mol Cell Res 1773, 1500-1510, 2007,1773, 1500-1510, 2007 ,2007.08. |
| 5. | Yufu T, Hirano K, Bi D, Hirano M, Nishimura J, Iwamoto Y, Kanaide H,Rac1 regulation of the surface expression of PAR1 and responsiveness to thrombin in vascular smooth muscle cells,Arterioscler Thromb Vasc Biol,Vol.25,No.7,vol. 25, 1506-1511,2005.01. |
| 6. | Shiga N, Hirano K, Hirano M, Nishimura J, Nawata H, Kanaide H,Long-term inhibition of RhoA attenuates vascular contractility by enhancing endothelial NO production in an intact rabbit mesenteric artery,Cir Res,Vol.96,No.9,vol. 96, 1014-1021,2005.01. |
| 7. | Koga M, Hirano K, Hirano M, Nishimura J, Kanaide H:,Akt plays a central role in the anti-apoptotic effect of estrogen in endothelial cells,Biochem Biophys Res Commun,Vol.324,No.1,vol. 324, 321-325,2004.01. |
| 8. | Hirano K, Ihara E, Hirano M, Nishimura J, Nawata H, Kanaide H:,Facilitation of proteasomal degradation of p27Kip1 by N-terminal cleavage, and their sequence requirements,FEBS Lett,Vol.574,No.1-3,vol. 574, 111-115,2004.01. |
| 9. | Hirano K, Hirano M, Nishimura J, Kanaide H:,A critical period requiring Rho proteins for cell cycle progression uncovered by reversible protein transduction in endothelial cells,FEBS Lett,Vol.570,No.1-3,vol. 570, 149-154,2004.01. |
| 10. | Nakayama T, Hirano K, Hirano M. Nishimura J, Kuga H, Nakamura K, Takahashi S, Kanaide H:,Inactivation of protease-activated receptor-1 by proteolytic removal of the ligand region in vascular endothelial cells,Biochem Pharmacol,Vol.68,No.1,vol. 68, 23-32,2004.01. |
| 11. | Hirano K, Derkach DN, Hirano M, Nishimura J, Takahashi S, Kanaide H,Transduction of the N-terminal fragments of MYPT1 enhances myofilament Ca2+ sensitivity in an intact coronary artery,Arterioscler Thromb Vasc Biol,Vol.24,No.3,vol. 24, 464-469,2004.01. |
| 12. | Eto W, Hirano K, Hirano M, Nishimura J, Kanaide H:,Intracellular alkalinization induces Ca2+ influx via non-voltage-operated Ca2+ channels in the rat aortic smooth muscle cells,Cell Calcium,Vol.34,No.6,vol. 34, 477-484,2003.01. |
| 13. | Hirano K, Zeng Y, Hirano M, Nishismura J, Kanaide H,Sequence requirement for nuclear localization and growth inhibition of p27Kip1R, a degradation-resistant isoform of p27Kip1,J Cell Biochem,Vol.89,No.1,vol. 89, 191-202,2003.01. |
| 14. | Ihara E, Hirano K, Hirano M, Nishimura J, Nawata H, Kanaide H,The mechanism of down-regulation of L-type Ca2+ channel in the proliferating smooth muscle cells of rat aorta,J Cell Biochem 87, 242-251,vol. 87, 242-251,2002.01. |
| 15. | Hirano M, Hirano K, Nishimura J, Kanaide H,Transcriptional up-regulation of p27Kip1 during contact-induced growth arrest in vascular endothelial cells,Exp Cell Res,Vol.271,No.2,vol. 271, 356-367,2001.01. |
| 16. | Hirano K, Hirano M, Zeng Y, Nishimura J, Hara K, Muta K, Nawata H, Kanaide H,Cloning and functional expression of a degradation-resistant novel isoform of p27Kip1,Biochem J,Vol.353,vol. 353, 51-57,2001.01. |
| 17. | Hirano K, Hirano M, Eto W, Nishimura J, Kanaide H,Mitogen-induced upregulation of non-smooth muscle isoform of a-tropomyosin in rat aortic smooth muscle cells,Eur J Pharmacol,Vol.406,No.2,vol. 406, 209-218,2000.01. |
| 18. | Hirano M, Niiro N, Hirano K, Nishimura J, Hartshorne DJ, Kanaide H: ,Expression, subcellular localization and cloning of the 130 kDa regulatory subunit of myosin phosphatase in porcine aortic endothelial cells. ,Biochem. Biophys. Res. Commun. ,Vol.254,No.2,pp.490-496,1999.01. |
Presentations
| 1. | Thrombin increases myosin light chain (MLC) phosphorylation, thereby increasing vascular permeability. This study investigated the regulatory mechanism of the thrombin-induced MLC phosphorylation in porcine aortic endothelial cells, by using a Phos-tag SDS-PAGE analysis. Unstimulated cells contained 25.4% mono-phosphorylated (MLC-P) and 2.3% di-phosphorylated (MLC-PP) MLC. MLC-PP transiently increased upon thrombin stimulation with a peak (33.3%) at 3min, while MLC-P showed a modest change; 28.9% at 3 min and 33.8% at 20 min. Removal of external Ca2+ decreased MLC-P at both 3 and 20min, while having no effect on MLC-PP. BAPTA loading had no effect on MLC-P at 3 min, while decreasing MLC-P at 20min and MLC-PP. Rho kinase inhibitors, Y27632 and H1152, substantially abolished the thrombin-induced MLC-PP, while they suppressed the MLC-P at 20min. However, MLC-P at 3min was suppressed by H1152 but not Y27632. The results suggest that the thrombin-induced MLC-P and MLC-PP was differentially regulated. MLC-PP was external Ca2+-independent and Rho kinase-dependent. MLC-P at an early phase was external Ca2+-dependent, while MLC-P at a late phase was Ca2+-dependent and Rho kinase-dependent.. |
| 2. | Myosin light chain (MLC) phosphorylation plays an essential role not only in smooth muscle contraction, but also in endothelial barrier function. Thrombin has been shown to increase MLC phosphorylation, thereby increasing the endothelial permeability. However, the mechanism of the thrombin-induced MLC phosphorylation still remains to be determined. This study investigated the roles of intra- and extra-cellular Ca2+ sources in the thrombin-induced MLC phosphorylation in the porcine aortic endothelial cells. The levels of mono- and di-phosphorylated forms of MLC (MLC-P and MLC-PP, respectively) were separately evaluated by utilizing Phos-tagTM SDS-PAGE and an immunoblot analysis. The unstimulated cells contained 25.4% MLC-P and 2.3% MLC-PP. Upon stimulation with 1 U/mL thrombin, MLC-PP increased to the peak of 33% at 3-5 min, and thereafter declined to the level close to the resting level. However, no significant changes in the level of MLC-P were observed. In the absence of the extracellular Ca2+, the thrombin-induced increase in MLC-PP remained unaffected, while the level of MLC-P was decreased. When a Ca2+ chelator BAPTA was loaded, the resting level of MLC-P significantly decreased. Upon thrombin stimulation, MLC-P increased to the level similar to that seen in the control by 10 min after the stimulation, while it thereafter gradually decreased to the pre-stimulation level. On the other hand, the increase in MLC-PP was substantially but not completely suppressed by BAPTA loading. These observations suggest that most parts of MLC-P and MLC-PP are Ca2+-dependent. However, MLC-PP is totally dependent on the intracellular Ca2+ source, while MLC-P is dependent on the extracellular source.. |
- The Japanese Circulation Society
- The Japaneese Pharmacological Society
- American Heart Association
- The Molecular Biology Society of Japan
- Japan Society of Smooth Muscle Research
- International Society for Heart Research
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