Aquaporins (AQPs) are water channels of cell membranes. All living cells experience osmotic pressure changes in their environment, but the mechanism by which water influx occurs was not known until the discovery of AQPs. AQP9, which is expressed in human polymorphonuclear leukocytes (PMNLs), is reported to relate to morphologic changes of PMNLs in vitro. We examined the expression of AQP9 in PMNLs from patients with systemic inflammatory response syndrome (SIRS) and addressed the role of AQP9 in both morphologic and functional changes of PMNLs in the SIRS condition. Fourteen patients with SIRS were included in our study. Polyclonal antibody was used for the AQP9 assay. F-actin polymerization, oxidative activity, and the expression of AQP9 in PMNLs with and without stimulation by N-formylmethionyl-leucyl-phenylalanine were evaluated by flow cytometry. Expression of AQP9, F-actin polymerization, and oxidative activity in PMNLs were increased significantly in patients with SIRS compared with those in healthy volunteers. The time course of AQP9 fluorescence in PMNLs corresponded to the time course of F-actin polymerization, which showed peak fluorescence at 1 min after N-formylmethionyl-leucyl-phenylalanine stimulation. The expression of AQP9 in PMNLs is increased significantly in SIRS patients. The increased expression of AQP9 in SIRS patients might be associated with F-actin polymerization in PMNLs, which could affect both morphologic and functional changes of PMNLs in the SIRS condition.
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http://dx.doi.org/10.1097/SHK.0000000000000218 | DOI Listing |
Toxicology
January 2025
Department of Veterinary Medicine and Animal Productions, University of Naples Federico II, Naples 80137, Italy. Electronic address:
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.
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Department of Geriatrics, The First Affiliated Hospital of Soochow University, Suzhou, Jiangsu, China.
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Department of Orthopaedic Surgery, Washington University in St. Louis, St. Louis, MO, USA.
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