Results 131 to 140 of about 4,789 (161)

Pentavalent methylated arsenicals are substrates of human AQP9 [PDF]

BioMetals, 2009
Liver aquaglyceroporin AQP9 facilitates movement of trivalent inorganic arsenite (As(III)) and organic monomethylarsonous acid (MAs(III)). However, the transport pathway for the two major pentavalent arsenic cellular metabolites, MAs(V) and DMAs(V), remains unknown in mammals.
Zijuan Liu, Barry P Rosen, Liu Zijuan
exaly   +3 more sources

Oxygen tension modulates AQP9 expression in human placenta

Placenta, 2013
Placental hypoxia has been implicated in pregnancy pathologies such as preeclampsia. We have previously reported that AQP9 is highly expressed in syncytiotrophoblast from normal placentas and shows an overexpression in preeclamptic placentas, with a lack of functionality for water transport.
A E Damiano
exaly   +4 more sources

AQP3 and AQP9—Contrary Players in Sepsis?

International Journal of Molecular Sciences
Sepsis involves an immunological systemic response to a microbial pathogenic insult, leading to a cascade of interconnected biochemical, cellular, and organ–organ interaction networks. Potential drug targets can depict aquaporins, as they are involved in immunological processes. In immune cells, AQP3 and AQP9 are of special interest.
Stefan Ehrentraut, Alexander Wolf, Hartmuth Nowak   +2 more
exaly   +4 more sources

CFTR May Modulate AQP9 Functionality in Preeclamptic Placentas

Placenta, 2009
Preeclampsia (PE) is a hypertensive disorder unique to human pregnancy. Although its causes remain unclear, it is known that altered placental villous angiogenesis and a poorly developed fetoplacental vasculature can affect the transport functions of the syncytiotrophoblast (hST).
A E Damiano
exaly   +4 more sources

Evidence for insulin-mediated control of AQP9 expression in human placenta

Placenta, 2011
The AQP9 gene contains a negative insulin response element, suggesting that it may be modulated by insulin. Previously, we reported AQP9 overexpression in preeclamptic placentas but a lack of functionality of AQP9 in water and mannitol transport. We also observed high serum levels of insulin and TNF-α in preeclamptic women.To evaluate whether AQP9 ...
A E Damiano
exaly   +4 more sources

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miR-330-3p alleviates the progression of atherosclerosis by downregulating AQP9

Functional and Integrative Genomics, 2023
Atherosclerosis (AS) is the main cause of cardiovascular diseases. However, the role of AQP9 in AS is not well understood. In the present study, we predicted that miR-330-3p might regulate AQP9 in AS through bioinformatics analysis, and we established AS model using ApoE-/- mouse (C57BL/6) with high-fat diet (HFD).
Wenbo Tang, Yu Yuanyuan
exaly   +3 more sources

Analysis of mice with targeted deletion of AQP9 gene provides conclusive evidence for expression of AQP9 in neurons

Journal of Neuroscience Research, 2008
AbstractAQP9 is an aquaglyceroporin that serves important functions in peripheral organs, including the liver. Reflecting the lack of AQP9 knockout mice, uncertainties still prevail regarding the localization and roles of AQP9 in the central nervous system.
Mylonakou, Maria N, Petersen, Petur H, Rinvik, Eric, Rojek, Aleksandra, Valdimarsdottir, Erla, Zelenin, Sergey, Zeuthen, Thomas, Nielsen, Søren, Ottersen, Ole P, Amiry-Moghaddam, Mahmood   +9 more
openaire   +3 more sources

Osteoclast differentiation and function in aquaglyceroporin AQP9‐null mice [PDF]

Biology of the Cell, 2009
Background information. Osteoclasts are cells specialized for bone resorption and play important roles in bone growth and calcium homoeostasis. Differentiation of osteoclasts involves fusion of bone marrow macrophage mononuclear precursors in response to extracellular signals.
Liu, Yangjian, Song, Linhua, Wang, Yiding, Rojek, Aleksandra, Nielsen, Søren, Agre, Peter, Carbrey, Jennifer   +6 more
exaly   +4 more sources

Immunolocalization of AQP9 in Liver, Epididymis, Testis, Spleen, and Brain

Biochemical and Biophysical Research Communications, 2000
The aims of this study were to determine the cellular and subcellular localization of aquaporin-9 (AQP9) in different rat organs by immunoblotting, immunohistochemistry and immunoelectron microscopy. To analyze this, we used rabbit antibodies to rat AQP9 raised against three different AQP9 peptides (amino acids 267-287, 274-295, and 278-295).
Elkjær, M.-L., Vajda, Z, Nejsum, Lene Niemann; id_orcid 0000-0003-4368-8821, Kwon, T, Jensen, U B; id_orcid 0000-0002-6205-6355, Amiry-Moghaddam, M, Frøkiaer, J, Nielsen, Søren   +7 more
openaire   +3 more sources

AQP9: A novel target for bone loss induced by microgravity

Biochemical and Biophysical Research Communications, 2012
The aim of current study was to elucidate whether aquaporin-9 (AQP9) expression was involved in the progression of bone loss induced by microgravity. We used the hind-limb suspension (HLS) mice model to simulate microgravity and induce bone loss. It was found that HLS exposure decreased femur bone mineral density (BMD), and enhanced femur AQP9 mRNA and
Guoyun, Bu, Feng, Shuang, Ye, Wu, Dongfeng, Ren, Shuxun, Hou   +4 more
openaire   +2 more sources