Sodium-hydrogen antiporter protein in normotensive Wistar-Kyoto rats and spontaneously hypertensive rats.
J Hypertens
; 12(7): 775-81, 1994 Jul.
Article
en En
| MEDLINE
| ID: mdl-7963506
ABSTRACT
OBJECTIVE:
To examine the mechanism of increased Na-H antiport activity in tissues of the spontaneously hypertensive rat (SHR) by measuring the amount of sodium-hydrogen exchanger isoform 1 (NHE-1) in cultured vascular and striated muscle cells, and in ex vivo tissue extracts of membranes from the brain, heart, kidney and skeletal muscle.METHODS:
A polyclonal rabbit antibody was raised against a fusion protein consisting of a section of the carboxyl tail of NHE-1 and beta-galactosidase. Cell extracts were separated by sodium dodecyl sulphate-polyacrylamide gel electrophoresis, and proteins were transferred to supported nitrocellulose. NHE-1 was detected by Western blotting and quantified by densitometry.RESULTS:
Cultured aortic and striated muscle cells from SHR contained similar amounts of NHE-1 on Western blots to those from control Wistar-Kyoto (WKY) rat cells. Ex vivo extracts of crude membranes from SHR tissues also contained quantities of NHE-1 similar to those from WKY rat tissues.CONCLUSION:
The increased Na-H antiport activity observed in SHR cells in vitro and in vivo is not due to an increased amount of NHE-1 protein in SHR cells. This suggests that in this model of hypertension the increased transport activity results from an increased turnover number per NHE-1 molecule.
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Colección:
01-internacional
Banco de datos:
MEDLINE
Asunto principal:
Intercambiadores de Sodio-Hidrógeno
/
Hipertensión
Límite:
Animals
Idioma:
En
Revista:
J Hypertens
Año:
1994
Tipo del documento:
Article
País de afiliación:
Reino Unido