Research output: Contribution to journal › Article › peer-review
Increase in the concentration of sEH protein in renal medulla of ISIAH rats with inherited stress-induced arterial hypertension. / Abramova, T. O.; Ryazanova, M. A.; Antonov, E. V. et al.
In: Molecular Biology, Vol. 51, No. 3, 01.05.2017, p. 389-392.Research output: Contribution to journal › Article › peer-review
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TY - JOUR
T1 - Increase in the concentration of sEH protein in renal medulla of ISIAH rats with inherited stress-induced arterial hypertension
AU - Abramova, T. O.
AU - Ryazanova, M. A.
AU - Antonov, E. V.
AU - Redina, O. E.
AU - Markel, A. L.
PY - 2017/5/1
Y1 - 2017/5/1
N2 - The concentration of soluble epoxide hydrolase (sEH) protein was studied in renal medulla of adult rats from hypertensive ISIAH strain and normotensive WAG strain. The sEH is a key enzyme in metabolism of epoxyeicosatrienoic acids capable of activating endothelial NO-synthase and nitrogen oxide formation, and therefore being vasodilators. An increase in the sEH protein concentration (that we found) allows one to assume that the oxidative stress is increased in the renal medulla of hypertensive rats, and the bloodflow is decreased.
AB - The concentration of soluble epoxide hydrolase (sEH) protein was studied in renal medulla of adult rats from hypertensive ISIAH strain and normotensive WAG strain. The sEH is a key enzyme in metabolism of epoxyeicosatrienoic acids capable of activating endothelial NO-synthase and nitrogen oxide formation, and therefore being vasodilators. An increase in the sEH protein concentration (that we found) allows one to assume that the oxidative stress is increased in the renal medulla of hypertensive rats, and the bloodflow is decreased.
KW - arterial hypertension
KW - ELISA
KW - ISIAH rat strain
KW - real time PCR
KW - renal medulla
KW - soluble epoxide hydrolase
UR - http://www.scopus.com/inward/record.url?scp=85021289281&partnerID=8YFLogxK
U2 - 10.1134/S0026893317020029
DO - 10.1134/S0026893317020029
M3 - Article
AN - SCOPUS:85021289281
VL - 51
SP - 389
EP - 392
JO - Molecular Biology
JF - Molecular Biology
SN - 0026-8933
IS - 3
ER -
ID: 8674927