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AQP10 Membrane Protein Introduction

Introduction of AQP10

Identified in human small intestine, AQP10 is the newest member of aquaporins in mammals and expressed selectively in the duodenum and the jejunum in human functioning as aquaglyceroporin. AQP10 is approximately 53% identical to AQP3 and AQP9, containing a cytosolic N terminus and 6 membrane-spanning domains with 5 connecting loops. The second and fifth loops possess the NPA motif, and there are 2 potential N-glycosylation sites in the third loop. The short cytoplasmic C terminus of AQP10 is reported to have a potential phosphorylation site.

Basic Information of AQP10
Protein Name Aquaporin-10
Gene Name AQP10
Aliases Aquaglyceroporin-10, Small intestine aquaporin
Organism Homo sapiens (Human)
UniProt ID Q96PS8
Transmembrane Times 5
Length (aa) 301
Sequence MVFTQAPAEIMGHLRIRSLLARQCLAEFLGVFVLMLLTQGAVAQAVTSGETKGNFFTMFLAGSLAVTIAIYVGGNVSGAHLNPAFSLAMCIVGRLPWVKLPIYILVQLLSAFCASGATYVLYHDALQNYTGGNLTVTGPKETASIFATYPAPYLSLNNGFLDQVLGTGMLIVGLLAILDRRNKGVPAGLEPVVVGMLILALGLSMGANCGIPLNPARDLGPRLFTYVAGWGPEVFSAGNGWWWVPVVAPLVGATVGTATYQLLVALHHPEGPEPAQDLVSAQHKASELETPASAQMLECKL

Function of AQP10 Membrane Protein

As a kind of aquaporin, the main function of AQP10 is to transport water molecules or glycerol molecules inside and outside the cell. In addition, AQP10 has been shown the dual characteristics of carrier/channel for solute transport. Except for the main expression of AQP10 in the apical membrane domain of absorptive intestinal epithelial cells, the unusual expression is associated with diseases of psoriasis, sweat herpes, and intestinal ulcers, etc. It is documented that AQP10 in fat cells can transfer glycerol molecules to the outside of the cell to maintain normal or low glycerol content, thus protecting humans from obesity. In epidermal cells, overexpression of the AQP10 protein is reported to transport large amounts of water molecules and glycerol molecules out of the cell, resulting in cell dehydration and possibly the induction of pompholyx.

AQP10-The water-activated water loss mechanism. Fig.1 AQP10-The water-activated water loss mechanism. (Soler, 2015)

Application of AQP10 Membrane Protein in Literature

  1. Soler D.C., et al. Overexpression of AQP3 and AQP10 in the skin exacerbates psoriasiform acanthosis. Exp Dermatol. 2017, 26: 949-951. PubMed ID: 28111811

    The author reveals that overexpression of AQP3 and AQP10 in the murine skin will increase psoriasiform acanthosis, supporting a role for cutaneous aquaporins in the pathogenesis of dermatitis and as potential targets in their treatment.

  2. Soler D.C., et al. The key role of aquaporin 3 and aquaporin 10 in the pathogenesis of pompholyx. Med Hypotheses. 2015, 84: 498-503. PubMed ID: 25725905

    This article demonstrates that overexpression of AQP3 and AQP10 can bridge the abundantly hydrated dermis and basal epidermis to the outer environment allowing cutaneous water and glycerol to flow outward in pompholyx patient. And the regulation of AQP3 and AQP10 by alitretinoin may be responsible for the beneficial effects of alitretinoin-treated patients with chronic hand eczemas.

  3. Ansar T., et al. Immunolocalization of aquaporin-10 in tuberculous human ileum. J Coll Physicians Surg Pak. 2013, 23: 392-396. PubMed ID: 23763797

    The authors conduct a cross-sectional analytical study to determine the presence of AQP-10 in the ileum of patients suffering from intestinal tuberculosis and they reveal that AQP-10 is significantly associated with granulomas, caseation necrosis and tuberculous lesion.

  4. Laforenza U., et al. Aquaporin-10 represents an alternative pathway for glycerol efflux from human adipocytes. PLoS One. 2013, 8: e54474. PubMed ID: 23382902

    This article suggests that the expression of AQP7 in both adipocyte and capillary plasma membranes of human adipose tissue and AQP10 exclusive in the adipocytes is particularly important for the maintenance of normal or low glycerol contents inside the adipocyte, thus protecting humans from obesity.

  5. Ishii M., et al. Dual functional characteristic of human aquaporin 10 for solute transport. Cell Physiol Biochem. 2011, 27: 749-756. PubMed ID: 21691092

    The authors use Xenopus laevis oocytes expressing human AQP10 to demonstrate that AQP10 can act as a carrier/channel for solute transport, which would help further elucidate its physiological role.

AQP10 Preparation Options

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As a forward-looking research institute as well as a leading custom service provider, Creative Biolabs provides high-quality membrane protein preparation service to facilitate the development of worldwide customer’s research. During the past years, we have successfully established a powerful Magic™ membrane protein platform which enables us to provide a series of membrane protein preparation services. For more detailed information, please feel free to contact us.

Reference

  1. Soler, et al. (2015). The key role of aquaporin 3 and aquaporin 10 in the pathogenesis of pompholyx. Med Hypotheses. 84, 498-503.

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