AQP1Aquaporin1 (major water channel of red blood cells)
AQP1Aquaporin1 (membrane channel protein found in red blood cells and numerous tissues)
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integerrima possesses significant anti-asthmatic activity which may be attributed to reduction in TNF-[alpha], IL-4, and IL-5 expression levels, and increase in AQP1 and AQP5 expression levels.
As shown in Figure 4A, diabetes significantly downregulated AQP1 expressions in renal tissues compared with control.
The monomer structure in the AQP1 tetramer has a right-handed helical bundle and two short helices, HB and HE, whose N-terminal sides face each other, especially the proline residues of the two asparagine-proline-alanine (NPA) sequences, which are almost perfectly conserved in AQP family proteins, called the NPA motif (Fig.
In contrast, AQP1 was present in high amounts in choroidal plexus cells, leptomeningeal cells, and perivascular and cerebellar astrocytes and in low amounts in ependymocytes.
Ocular tissue AQP1 AQP3 AQP4 AQP5 AQP7 AQP9 Cornea D D ND D D ND Iris D ND D D ND Lens D ND D D D ND Trabecular meshwork D ND ND ND D ND Ciliary D ND D ND D D Retina D ND D ND D D Choroid D ND ND ND ND Optic nerve ND ND D ND ND D AQP = aquaporin, D = detected, and ND = not detected.
More research is needed to see how early in the disease process levels of AQP1 or ADFP proteins rise and whether the concentration of these proteins in the urine correspond to the size of a kidney tumor.
29) Patients with an inability to make AQP1 have been extensively studied.
Su denominacion destaca el hecho de que fue descrita antes de la AQP1, aunque su relacion con esta familia de canales de agua es posterior.
Many aquaporins are mercury sensitive, and in AQP1 a mercury-sensitive cysteine residue (Cys-l89) is present adjacent to a conserved Asn-Pro-Ala motif.
High-resolution crystallographic studies of fungal Aqy1, together with experimental studies of mammalian AQP1 and molecular dynamics simulations, have suggested that a synergistic effect between the NPA motifs and the ar/R selectivity filter breaks the connectivity of permeating water molecules to prevent proton transport via a Grotthuss mechanism, in which excess protons could shuttle through the hydrogen bond network of water, hydroxyl, and hydronium molecules (de Grotthuss, 1806; Wu etal.
12] Recently, we reported AQP1 expression in the capillaries and venules of the urinary bladder and significant incease of protein expression of AQP1 in the BOO rat urinary bladder.