2002 Fiscal Year Final Research Report Summary
Regulatory mechanism of CI^- transport via tyrosine phophorylation by cAMP
| Project/Area Number |
13670046
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
General physiology
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| Research Institution | Kyoto Prefectural University of Medicine |
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Principal Investigator |
NIISATO Naomi Kyoto Prefectural University of Medicine, Physiology, Assistant Professor, 医学部, 講師 (00237645)
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| Co-Investigator(Kenkyū-buntansha) |
MARUNAKA Yoshinori Kyoto Prefectural University of Medicine, Physiology, Professor, 医学部, 教授 (00127036)
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| Project Period (FY) |
2001 – 2002
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| Keywords | Tyrosine phophorylation / CI^- transport / cAMP |
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| Research Abstract |
We studied the regulatory mechanism of Samp-stimulated CI^- transport through tyrosime phosphorylation in renal epithelial A6 cells. Our results supported by a Grant-in-aid for Scientific Research (2001-2002) are summarized as follows.
1.Camp is known to stimulate biphasic CI^- transport in renal epithelial A6 cells. Preteatment with tyrphostin A23 (a protein tyrosine kinase (PTK) inhibitor) abolished the Camp-stimulated CI^- transport by inhibiting the Na^+/K^+/2CI^- cotransporter. These results suggest that PTK is involved in regulation of the Na^+/K^+/2CI^- cotransporter in cAMP-stimulated CI^- transport
2. Camp stimulation increased tyrosine phosphorylation in several proteins which was sensitive to tyrphotin A23, suggesting that these tyrosine phosphorylated proteins might contribute to regulate the Camp stimulation CI^- transport
3. We examined whether Camp stimulation activates PTK by a change in plasma membrane tension. To increase plasma membrane tension by chlorpromazine also induced an increase in tyrosine phosphorylation of several proteins likely to Camp stimulation
Based on these results, it is indicated that Camp stimulation increased tyrosine phophorylation of several proteins via cell volume-dependent changes in membrane tension, resulting in stimulation of CI^- transport in A6 cells
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