Aquaporin-10 Antibodies

Aquaporin-10 (AQP10)

Water channel required to promote glycerol permeability and water transport across cell membranes. May contribute to water transport in the upper part of small intestine.

Isoform 2 isn't permeable to urea and glycerol. .

Gene Information

Human
Gene Name:	AQP10
Uniprot:	Q96PS8
Entrez:	89872

Family

Belongs to:
MIP/aquaporin (TC 1.A.8) family

Alternative Names

AQP-10; AQPA_HUMAN; aquaglyceroporin-10; aquaporin 10; aquaporin-10; Small intestine aquaporin

Molecular Weight

Mass (kDA):
31.763 kDA

Genomic Context

Human
Location:	1q21.3
Sequence:	1; NC_000001.11 (154321059..154325325)

Tissue Specificity

Expressed exclusively in duodenum and jejunum. Highest expression in absorptive epithelial cells at the tips of villi in the jejunum.

Subcellular Localizations

Apical cell membrane; Multi-pass membrane protein. Cell membrane; Multi-pass membrane protein. Lipid droplet. Detected around lipid droplets.

Diseases

• Diabetes Mellitus
• Severe Diarrhea
• Cholera
• Insulin Resistance
• Ulcerative Colitis
• Ulcer
• Polycystic Kidney Diseases
• Obesity
• Hyperglycemia

• Crohn Disease
• Diarrhea
• Nephrogenic Diabetes Insipidus
• Colitis

Interacting Proteins

• PGRMC2

Pathways

• Transport
• Glycerol Transport
• Localization
• Glycosylation
• Secretion
• Gene Silencing
• Insulin Secretion
• Gluconeogenesis
• Arsenite Transport
• Intestinal Absorption

• Translation
• Urea Transport
• Water Transport
• Wound Healing
• Excretion

PTMs

• Glycosylation

For details, visit:
bosterbio.com/bosterbio-gene-info-cards/AQP10

Best Uses Of The AQP10 Marker

This article will explain how to use AQP10, a new biomarker, which is permeable only to very low amounts of water. This biomarker is not compatible with urea and glycerol. Scientists will find this important, as urea or glycerol are polar compounds which can affect the performance of AQP10 in biomarkers.

AQP10 can be permeable to very low amounts of water

AQP10 is a type o aquaporin that promotes water and glycerol transport across cell membranes. It may also be involved in water transport within the upper small intestine. It is available in two forms (AQP1 or AQP10). They differ in their permeability to urea, glycerol and other substances. Alternative splicing of protein produces the two isoforms.

AQP10 can be expressed in cells that express AQP4 H201, a mutant form. This mutant forms membrane channels that are similar to the wild-type protein. Because AQP4H201 expression is on the cell surface of cells, AQP4H201 in cell culture has the same single-channel water permeability that wild-type AQP41313.

Studies on AQP1 and AQP4 have revealed that glycerol is a hydrophobic corner of AQP10 and that its pore size determines solute permeability. However, the differences between AQP1 and AQP4 mutants suggest that structural context is crucial for solute permeability. Crystallographic analyses of AqpZ showed that the hydrophobicity and pore size of selectivity filters residues was also correlated.

A porous lining occurs when F56A/h280A mutation is used in AQP1 in H293 cells. This mutation also increases the glycerol permeability of AQP10 to high levels. Its glycerol permeability was higher than that of both AQP3 & AQP10.

AQP10 has a low water permeability. It is also highly permeable to water. Aquaporins allow water to move through an osmotic gradient because of their structure. AQPs can also be found in bacteria, invertebrates, plants, and other animals. Electrophysiological properties of AQPs have been studied using both native and heterologously expressing channels.

GlpF can also be used as a model to describe the structure of water channels. Its structural, functional and functional comparisons enable it to be applied to the entire family. During the water channel selectivity, major conformational shifts occur in the pores-lining residues. GlpF can also be permeable for larger solutes. Moreover, siRNA reduces the glycerol permeability coefficient by more than 50%.

After insulin stimulation, AQP7/AQP10 are found within the adipocyte membranes. Insulin enhanced staining of AQP10 near lipid droplets. Below is a representative confocal 3D reconstruction from adipocytes after they were labeled by AQP10. The nucleus of the nucleus had been counterstained using DAPI. This discovery is a significant step in understanding the body's water-transport processes.

Silencing AQP10 was shown to reduce the permeability between water and glycerol by 50% in human adipocytes. Silencing aquaporin-10 reduced glycerol and osmotic water permeability. These results indicate that AQP10 is an important cellular component in the formation of adipocytes. These findings require further investigation.

It is not permeable by urea, glycerol.

We investigated the permeability AQP9 & AQP10, which are two genes that regulate glycerol transport in small intestines. The permeability of the two genes was similar, with AQP9 being nearly twice as open to glycerol. We hypothesized that these two genes might have different biases towards urea or glycerol and that their permeability ratios could be a physiological mechanism.

In the simulations, glycerol and urea are not permeable to AQP10, but to glycerol and urea. This result is consistent with other observations. Both proteins show significant conformational change consistent with their roles within water and glucose transport. The permeation of glycerol through AQP10 is modeled as a force acting on a residue that contains arginine.

The hydrophobic corner at a pore's surface is crucial for solute selection in AQP10. Mutations that reduce the hydrophobic corner promote glycerol-permeability. Mutations of the H201A/G201A mutation in AQP4 do not allow for urea and glycerol to pass through them.

The size of AQP10 and its polarity are both factors that determine its water-permeability. The water/glycerol selectivity will be determined by the ar/R restriction. Mutations that alter ar/R constriction can decrease water permeability or hinder water isolation. Mutations of the h280A/R195V dual mutation did not alter water permeability, but altered glycerolpermeability.

A novel aquaporin has been identified in the small intestine. Although the gene encoding AQP10 has a close relationship to the AQP3 Subfamily, it differs in sequence and location. AQP10 expression was also found in Xenopus oocytes, which increased osmotic water permeability by mercury-sensitive means.

The partial negative charge on carbonyl is thought to provide the basis for the anion exclusion. The ar/R constricttion of AqpZ, which contains the carbonyl, is located only a few meters from guanidinium NHs. This close proximity between charges strengthens the interplay of geometry and polarity. The ar/R site can only permit the passage of dipoles containing positive and/or negative charges. Therefore, cations and anions are excluded from the passage of AQP10. Consequently, water and glycerol are the only two molecules that can pass through the AQP10 interface.

Aquaporins, transmembrane protein that allows for rapid cellular responses to osmotic change, are transmembrane proteins. These proteins enable neutral polar solvents to move through them, which improves membrane permeability. As mentioned, aquaporins can be water-selective. However, some are permeable to neutral solutes such as urea, while others are not permeable to glycerol.

The cytoplasmic loop D of AQP10 is different from that of AQP1 and AQP10. The NPA does not anchor the loop D to its N terminus. Instead, a divalent Cation (Ca2+), anchors it. The hydrophobic barrier formed by loop D and other residues forms a closed conformation in the cytoplasm. L197, which is also located in the cytoplasm blocks entry to the channel into the cell. It also forms a barrier against hydrophobic forces with the rest D of the loop.

It is not permeable for urea

As a promising solution to airway-monitoring, a dilution biomarker, called urea, was proposed. Its uniform distribution throughout body makes it an ideal candidate for dilution biological marker tests. However, the current EBC-urea analytical methods require a desivatization step or prior treatment. In addition, urea is highly permeable to water vapor, making it difficult to measure at an adequate concentration.