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AQP3 Membrane Protein Introduction

Introduction of AQP3

AQP belongs to the aquaporin (AQP) family, which comprises several membrane protein channels. These channels facilitate rapid water transport across all cell membranes, thereby maintaining body water homeostasis. The aquaglyceroporin AQP3 is expressed widely in the body and has been implicated in an increasing number of physiological and pathophysiological processes, such as metabolism process, type 2 diabetes and skin elasticity. AQP3-null mice have also been demonstrated to have a reduced capacity for wound healing.

Basic Information of AQP3
Protein Name Aquaporin-3
Gene Name AQP3
Aliases Aquaglyceroporin-3
Organism Homo sapiens (Human)
UniProt ID Q92482
Transmembrane Times 6
Length (aa) 292
Sequence MGRQKELVSRCGEMLHIRYRLLRQALAECLGTLILVMFGCGSVAQVVLSRGTHGGFLTINLAFGFAVTLGILIAGQVSGAHLNPAVTFAMCFLAREPWIKLPIYTLAQTLGAFLGAGIVFGLYYDAIWHFADNQLFVSGPNGTAGIFATYPSGHLDMINGFFDQFIGTASLIVCVLAIVDPYNNPVPRGLEAFTVGLVVLVIGTSMGFNSGYAVNPARDFGPRLFTALAGWGSAVFTTGQHWWWVPIVSPLLGSIAGVFVYQLMIGCHLEQPPPSNEEENVKLAHVKHKEQI

Function ofAQP3 Membrane Protein

Thirteen human AQPs have been identified to date, which form two distinct sub-groups: Classical AQPs (AQP0, 1, 2, 4, 5, 6 and 8) that solely transport water, and aquaglyceroporins (AQP3, 7, 9 and 10) that additionally transport small, uncharged molecules such as glycerol and urea. Regulated by vasopressin (ADH) in the kidney, AQP3 has further been suggested to have a role in bladder, colorectal, gastric, lung and skin cancers. The recent studies have suggested that AQP3 expression may be associated with disease survival in HER2 positive breast cancer. Moreover, AQP3 gene silencing is reported to significantly reduce oestradiol-induced proliferation, invasion and migration in a cell model of breast cancer. Increased AQP3 expression in breast cancer cells is possible to facilitate glycerol transport into the cell, which may then contribute to the generation of ATP, providing cancer cells with the increased energy required for proliferation and tumorigenesis.

The AQP3 structure diagram. Fig.1 The AQP3 structure diagram. (Aikman, 2018)

Application of AQP3 Membrane Protein in Literature

  1. Arif M., et al. Downregulation of aquaporin 3 inhibits cellular proliferation, migration and invasion in the MDA-MB-231 breast cancer cell line. Oncol Lett. 2018, 16: 713-720. PubMed ID: 29963136

    This study demonstrates that AQP3 gene knockdown has an effect on MDA-MB-231 breast cancer cell proliferation, migration, invasion, adherence and response to the chemotherapeutic agent 5-fluorouracil, suggesting that AQP3 may be a novel target for therapeutic intervention.

  2. Posfai D., et al. Plasmodium parasite exploits host aquaporin-3 during liver stage malaria infection. PLoS Pathog. 2018, 14: e1007057. PubMed ID: 29775485

    This study reveals that host AQP3 can be used by Plasmodium parasite to mediated nutrient transport, which is an important function for parasite development. These data identify additional host factors that are essential for Plasmodium liver stage infection and discover a previously unknown potential route for host-dependent nutrient acquisition.

  3. Alejandra R., et al. The blocking of aquaporin-3 (AQP3) impairs extravillous trophoblast cell migration. Biochem Biophys Res Commun. 2018, 499: 227-232. PubMed ID: 29567477

    This article demonstrates that blocking of AQP3 by CuSO4 or AQP3 silencing can significantly attenuate EVT cell migration, and an altered expression of placental AQP3 may produce failures in placentation such as in preeclampsia, suggesting AQP3 is required for EVT cell migration during early gestation.

  4. Wen J., et al. Helicobacter pylori infection promotes Aquaporin 3 expression via the ROS-HIF-1alpha-AQP3-ROS loop in stomach mucosa: a potential novel mechanism for cancer pathogenesis. Oncogene. 2018, 37: 3549-3561. PubMed ID: 29563612

    This study identifies the mechanistic link between H. pylori infection and AQP3 upregulation in the pathogenesis of gastric carcinoma, which involves the activation of the ROS-HIF-1α axis and the exacerbated ROS-HIF-1α-AQP3-ROS loop.

  5. Chen Q., et al. Subcellular localization of aquaporin 3 in prostate cancer is regulated by RalA. Oncol Rep. 2018, 39: 2171-2177. PubMed ID: 29532894

    This article reveals that overexpression of E-cadherin and knockdown of RaLA can lead to an increase of AQP3 in prostate cancer cell plasma membranes, suggesting a novel role f AQP3 and providing a creative view for RalA-directed therapies.

AQP3 Preparation Options

We provide custom membrane protein preparation services for worldwide customers. Aided by our advanced Magic™ membrane protein production platform, we are able to present target membrane protein in multiple active formats. Our professional scientists are happy to help you find an ideal method and make your project a success. Aided by our versatile Magic™ anti-membrane protein antibody discovery platform, we also provide customized anti-AQP3 antibody development services.


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. Aikman B, et al. (2018). Aquaporins in cancer development: opportunities for bioinorganic chemistry to contribute novel chemical probes and therapeutic agents. Metallomics. 10, 696-712.

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