منابع مشابه
Aquaporin-5 levels of lung following the taper program and Nigella sativa in the maturing rat
The aquaporin5 (AQP5) is an integral membrane protein that plays an important role in maintaining water homeostasis in the lung during of puberty. The purpose of this study was to evaluate the effect of period of reduced training with Nigella Sativa (NS) supplementation on AQP5 levels in the lung of Male Wistar rats during of puberty. 110 newborn three-week old male Wistar rats with average wei...
متن کاملThe -1364A/C Aquaporin 5 Gene Promoter Polymorphism Is Not Associated with Menière's Disease
Objective. Aquaporin 5 plays an important role in maintaining inner ear water and fluid homeostasis. Since the aquaporin (AQP) 5 promoter-1364A/C polymorphism is associated with altered AQP5 expression and this could impact upon key mechanisms of Menière's disease, we tested the hypothesis that genotypes of the AQP5 promoter-1364A/C polymorphism are associated with the incidences of Menière's d...
متن کاملThe Gating Mechanism of the Human Aquaporin 5 Revealed by Molecular Dynamics Simulations
Aquaporins are protein channels located across the cell membrane with the role of conducting water or other small sugar alcohol molecules (aquaglyceroporins). The high-resolution X-ray structure of the human aquaporin 5 (HsAQP5) shows that HsAQP5, as all the other known aquaporins, exhibits tetrameric structure. By means of molecular dynamics simulations we analyzed the role of spontaneous fluc...
متن کاملIdentification of androgen-selective androgen-response elements in the human aquaporin-5 and Rad9 genes.
The AR (androgen receptor) is known to influence the expression of its target genes by binding to different sets of AREs (androgen-response elements) in the DNA. One set consists of the classical steroid-response elements which are partial palindromic repeats of the 5'-TGTTCT-3' steroid-receptor monomer-binding element. The second set contains motifs that are AR-specific and that are proposed t...
متن کاملThe fold of human aquaporin 1.
The fold of human aquaporin 1 is determined from cryo-electron microscopic data at 4.5 A resolution. The monomeric structure consists of two transmembrane triple helices arranged around a pseudo-2-fold axis connected by a long flexible extracellular loop. Each triplet contains between its second and third helix a functional loop containing the highly conserved fingerprint NPA motif. These funct...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1996
ISSN: 0021-9258
DOI: 10.1074/jbc.271.15.8599