Request Demo

Last update 23 Jan 2025

AQP3

Last update 23 Jan 2025

Basic Info

Synonyms

AQP-3, AQP3, Aquaglyceroporin-3

+ [6]

Introduction

Water channel required to promote glycerol permeability and water transport across cell membranes (PubMed:12239222, PubMed:30420639). Acts as a glycerol transporter in skin and plays an important role in regulating SC (stratum corneum) and epidermal glycerol content. Involved in skin hydration, wound healing, and tumorigenesis. Provides kidney medullary collecting duct with high permeability to water, thereby permitting water to move in the direction of an osmotic gradient. Slightly permeable to urea and may function as a water and urea exit mechanism in antidiuresis in collecting duct cells. It may play an important role in gastrointestinal tract water transport and in glycerol metabolism (By similarity).

Drugs associated with AQP3

DFP00173

Target

AQP3

Mechanism

AQP3 inhibitors

Active Org.

University of Lund

Originator Org.

University of Lund

Active Indication-

Inactive Indication-

Drug Highest PhasePreclinical

First Approval Ctry. / Loc.-

First Approval Date20 Jan 1800

WO2024014523

Patent Mining

Target

AQP3

Mechanism-

Active Org.

Keio University

Originator Org.

Keio University

Active Indication

Neoplasms

Inactive Indication-

Drug Highest PhaseDiscovery

First Approval Ctry. / Loc.-

First Approval Date20 Jan 1800

CN117126296

Patent Mining

Target

AQP3

Mechanism-

Active Org.

Guangzhou Murray Pharmaceutical Technology Co., Ltd.

Originator Org.

Guangzhou Murray Pharmaceutical Technology Co., Ltd.

Active Indication

Respiratory Tract Neoplasms

Inactive Indication-

Drug Highest PhaseDiscovery

First Approval Ctry. / Loc.-

First Approval Date20 Jan 1800

100 Clinical Results associated with AQP3

100 Translational Medicine associated with AQP3

0 Patents (Medical) associated with AQP3

1,651

Literatures (Medical) associated with AQP3

01 Mar 2025·International Journal of Biological Macromolecules

AQP3-liposome@GelMA promotes overloaded-induced degenerated disc regeneration via IBSP/ITG αVβ3/AKT pathway

Article

Author: Zhu, Yibo ; Zhang, Huilin ; Li, Xiaoxiao ; Wang, Yiyang ; Hu, Junxian ; Li, Xiangwei ; Li, Pei ; Zhou, Qiang ; Pang, Zeyu

Medical and conservative treatments for intervertebral disc degeneration (IDD) primarily focus on alleviating symptoms. However, effective curative therapies that promote disc regeneration remain lacking. Recent advancements in disc repair materials offer a potential solution, but identifying effective cytokines for regeneration and developing efficient drug delivery systems are crucial for success. This study demonstrated a negative correlation between AQP3 expression levels and the extent of disc degeneration induced by mechanical overload, as evidenced in both in vivo and in vitro models, suggesting that AQP3 is a key regulator of intervertebral disc (IVD) homeostasis. Moreover, the overexpression of AQP3 or exogenous AQP3 protein significantly repaired degenerated IVDs. As a membrane protein, exogenous AQP3 is challenging for cells to recognize and internalize. To address this issue, we designed liposomes to encapsulate AQP3 and incorporated them into GelMA (AQP3-lipo@GelMA) for targeted repair of IDD resulting from high mechanical pressure. The encapsulation of AQP3 in liposomes improved cellular recognition and uptake, thereby enhancing its functionality at the cell membrane. Additionally, AQP3 within this material inhibited the binding of integrins to sialic acid-binding proteins (IBSP), which subsequently reduced the expression of the downstream integrin αVβ3. This cascade effect indirectly activated the AKT pathway, promoting the survival of NP cells. In vivo experiments, we found that AQP3-lipo@GelMA had an efficient function of repairing degenerated intervertebral disc. This study introduced AQP3-lipo@GelMA as a promising material for clinical applications in IVD repair.

01 Feb 2025·Journal of Molecular Histology

Expression and Immunolocalization of Aquaporins in the Buffalo Liver and Adipose Tissue

Article

Author: Nagpal, Anju ; Meena, Sunita ; Onteru, Suneel Kumar ; Rajput, Shiveeli ; Jasmin A T, Fathima ; Mate, Payal S ; Ashutosh

Increasing incidences of fatty liver in humans and animals worldwide is the leading cause of liver related morbidities. Currently, in the face of the growing global increase in fatty liver, and the necessity to explore new factors significantly affecting it, aquaporins (AQPs) have become the focus of interest for many researchers. AQPs are membrane integral proteins involved in the transport of water, glycerol and other small solutes. These are expressed in all tissues and play multiple roles under normal and pathophysiological conditions. Despite ongoing advancements in understanding the involvement of aquaporins in metabolic processes, there remains a notable lack of knowledge concerning cellular and subcellular localization of the AQPs in bovine tissues and organs. Understanding this could provide a new therapeutic target for metabolic syndromes such as fatty liver disease in bovine. In this study, AQPs in bovine liver, adipose tissue and gall bladder are examined using immunohistochemistry. AQP9 immunoreactivity is predominantly detected at the sinusoidal surfaces of hepatocytes. AQP8 is mostly intracellular and localized to the central vein and sinusoid, whereas AQP7 is found around the portal vein. Notably, AQP3 is observed in the bovine gall bladder and adipose tissue but not in the liver. In adipose tissue, AQP7 is also detected in the cytoplasmic membranes of adipocytes. AQPs in liver and adipose tissue were also studied using the western blotting technique. Higher AQP9 and AQP3 expression is observed in the liver and adipose tissue, respectively, indicating they are the dominant aquaporins in these tissues. This suggests they could be potential therapeutic targets for treating fatty liver disease and other metabolic disorders in bovine.

01 Feb 2025·Toxicology

Non-dioxin-like polychlorinated biphenyls (PCB 101, 153, and 180) and adipocyte lipid dysfunctions: Involvement of glycerol and role of aquaglyceroporins in mature 3T3-L1 cells

Article

Author: Ferrante, M C ; Del Piano, F ; Meli, R ; Pelagalli, A ; Lama, A ; Pirozzi, C ; Monnolo, A ; Comella, F ; Melini, S ; Naccari, C

Non-dioxin-like polychlorinated biphenyls (NDL-PCBs), as well as dioxin-like PCBs, are endocrine disruptors that persist in human and animal tissues worldwide. Due to their lipophilicity and resistance to enzymatic degradation, PCBs accumulate in fat deposits contributing to the onset of endocrine and metabolic diseases. Aquaporins (AQPs) are transmembrane channel proteins that allow the transport of water and small solutes. In particular, the aquaglyceroporins AQP3, AQP7, and AQP9 mediate the release and the uptake of glycerol in adipose tissue. Here, we investigate the modulation of these AQPs by NDL-PCBs and the following effects on lipid metabolism in mature 3T3-L1 adipocytes exposed for 48 h to PCB 101, 153, or 180 (1 μM). NDL-PCBs modulated protein expression of AQP3 and AQP7, involved in glycerol release, and AQP9, implicated in glycerol uptake. This modulation induced a greater accumulation of glycerol in treated adipocytes indirectly evaluated by its reduction in the culture media. Interestingly, only PCB 153 altered the expression of enzymes involved in glycerol metabolism and lipid accumulation (i.e. Pparg, Fabp4, Gyk, Dgat1, and Agpat9). These modifications indicated an increase of adipocyte lipid accumulation confirmed by Oil Red O staining. The role of AQPs in the increased cellular accumulation of glycerol was confirmed using phloretin, an AQP9 inhibitor, that reverted the PCB 153 effect. Our results show the involvement of AQPs in PCB 153-induced dysfunction of glycerol metabolism and lipid storage in adipocytes, contributing to better defining the mechanisms underlying its known obesogenic effect.

Analysis

Perform a panoramic analysis of this field.

view full example data

Chat with Hiro

Get started for free today!

Accelerate Strategic R&D decision making with Synapse, PatSnap’s AI-powered Connected Innovation Intelligence Platform Built for Life Sciences Professionals.

Start your data trial now!

Synapse data is also accessible to external entities via APIs or data packages. Empower better decisions with the latest in pharmaceutical intelligence.

Bio

Bio Sequences Search & Analysis

Chemical

Chemical Structures Search & Analysis

AQP3

Basic Info

Related

Analysis