Genetic analysis and molecular mechanism of salt-sensitive hypertension
| Project/Area Number |
10671017
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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 |
Kidney internal medicine
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| Research Institution | Fukuoka University |
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Principal Investigator |
TSUJI Emiko Fukuoka University, School of Medicine, Assistant Professor, 医学部, 助手 (10248495)
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| Project Period (FY) |
1998 – 1999
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| Project Status |
Completed (Fiscal Year 1999)
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| Budget Amount *help |
¥3,100,000 (Direct Cost: ¥3,100,000)
Fiscal Year 1999: ¥1,400,000 (Direct Cost: ¥1,400,000)
Fiscal Year 1998: ¥1,700,000 (Direct Cost: ¥1,700,000)
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| Keywords | Salt-sensitivity / htpertension / Molecular biology / Genetic analysis |
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| Research Abstract |
Human hypertension is a multifactorial disease which is complicated by genetic and environmental factors. Excessive dietary sodium intake is an important factor in the hypertension, however the molecular basis of the salt sensitivity in hypertension is not yet fully understood (Campese, 1994). Recently, we isolated novel rat cDNA named salt-tolerant protein (STP), using functional complementation to improve the growth of the yeast S. cervisiae HAL1-deficient strain under high salt conditions (Tsuji et al. l996). STP gene was expressed in several different rat tissues as a single transcript of 2.1 Kb and was induced by high-salt loading. STP may play an important role in the increase in blood pressure associated with excess salt intake. Immunohistochemical examination revealed that STP was localized mainly in the proximal tubules of rat kidney. The intracellular [Na+]/[K+] ratio in STP-transfected cells was higher than that in control cells. It is suggested that STP somehow affects intracellular cation homeostasis. The STP gene may increase renal sodium reabsorption in proximal tubules, and thus be an important determinant of hypertension associated with excess salt intake (Tsuji et al. l998). In the present study we have isolated and sequenced the cDNA encoding HSTP and mapped the gene to human chromosome by FISH. The nucleotide sequence (l988bp) of the HSTP cDNA contains an open reading frame encoding a polypeptide comprising 545 amino acids, two residues less than those of rat STP. The predicted amino acid sequence exhibits 92% identity to that of the rat protein. HSTP contains predicted coiled-coil domains and an Src Homology 3 domain, and shows a high degree of identity to CIP4 (Cdc 42 target protein) and human Tri1O (thyroid-hormone receptor interacting protein). We have mapped the HSTP gene to human chromosome 19 by fluorescence in situ hybridization.
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Report
(3 results)
Research Products
(7 results)
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[Publications] Uehara, Y., Sasaguri, M., Kinoshita, A., Tsuji, E., Kiyose, H., Taniguchi, H., Noda, K., Ideishi, M., Inoue. J., Tomita, K., Arakawa, K.: "Genetic analysis of the epithelial sodium channel in Liddle's syndrome."J. Hypertens.. 16. 1131-1135 (1998)
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