Introduction of AQP7
AQP7, encoded by AQP7 gene, is a water-selective membrane channel, which contains 6 transmembrane domains and an intracellular N and C termini. AQP7 gene is mapped to chromosome 9p13.3. As an aquaglyceroporin permeated by water and glycerol, AQP7 is in rat testis seminiferous tubules and on the plasma membrane of late spermatids, indicating that AQP7 participants in the late stages of spermatogenesis. The deduced amino acid sequences of human AQP7 is 67% identical to mouse AQP7.
|Basic Information of AQP7|
|Aliases||Aquaglyceroporin-7, Aquaporin adipose, AQPap, Aquaporin-7-like|
|Organism||Homo sapiens (Human)|
Function of AQP7 Membrane Protein
Facilitating water, glycerol and urea transport, AQP7 has been reported to participant in various physiological processes. It is documented that AQP7 can be expressed in pancreatic β-cells, where it may transport urea and glycerol, resulting in a similar β-cell swelling, activation of the volume-regulated anion channel and insulin secretion, triacylglycerol synthesis and proliferation of these endocrine cells. So, transgenic AQP7-knockout mice have been used to develop into adult-onset obesity and hyperinsulinemia model. In addition, AQP2 up-regulation and AQP7 down-regulation in the rat inner ear caused by vasopressin induce an increased production and a decreased absorption of endolymph, leading to Endolymphatic Hydrops. It is reported that lack of AQP7 expression in sperm may be an underlying mechanism of male infertility. AQP7 is also associated with Glycerol Quantitative Trait Locus and Chronic Closed-Angle Glaucoma.
Fig.1 AQP7 and AQP9 function in glucose homeostasis. (Jin, 2017)
Application of AQP7 Membrane Protein in Literature
This article reveals that AQP7 protein abundance in subcutaneous adipose tissue (SAT) or skeletal muscle are not affected by meal intake. SAT AQP7 expression is not involved in the regulation of adipose tissue lipolysis, however, skeletal muscle AQP7 abundance contributes to the excess lipid accumulation in skeletal muscle in type 2 diabetes.
This article verifies the role of aquaporins in the physiology and pathophysiology of the pancreas and concludes the role of pancreatic AQP7 as a novel player in the control of β-cell function and a potential anti-diabetic-drug.
The article demonstrates that AQP7 acts as a significant modulator of glycerol metabolism in a wide range of tissues and plays essential roles in whole-body energy balance and the pathophysiology of obesity as well as the development of insulin resistance.
This article suggests that AQP7 expression is affected by tissue-specific estrogen, which alters the balance of adipocyte metabolism between adipose tissue depots.
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