Mammalian aquaporins (AQPs) are a family of at least 13 small, integral membrane proteins expressed in various fluidtransporting epithelial cells. Aquaporin 2 (AQP2) is mainly expressed in the kidneys, where it plays an important role in the reabsorption of water from the renal tubular fluid to concentrate urine. | Turkish Journal of Biology Turk J Biol (2015) 39: 692-697 © TÜBİTAK doi: Research Article Immunohistochemical identification of aquaporin 2 in the kidneys of wild boars (Sus scrofa) 1, 2 3 3 Katarzyna MICHAŁEK *, Ewa CZERNIAWSKA-PIĄTKOWSKA , Marta GRABOWSKA , Maria LASZCZYŃSKA Department of Physiology, Cytobiology and Proteomics, Faculty of Biotechnology and Animal Husbandry, West Pomeranian University of Technology in Szczecin, Poland 2 Department of Ruminant Sciences, Faculty of Biotechnology and Animal Husbandry, West Pomeranian University of Technology in Szczecin, Poland 3 Department of Histology and Developmental Biology, Faculty of Health Sciences, Pomeranian Medical University, Szczecin, Poland 1 Received: Accepted/Published Online: Printed: Abstract: Mammalian aquaporins (AQPs) are a family of at least 13 small, integral membrane proteins expressed in various fluidtransporting epithelial cells. Aquaporin 2 (AQP2) is mainly expressed in the kidneys, where it plays an important role in the reabsorption of water from the renal tubular fluid to concentrate urine. Studies of AQP2 expression in the kidneys have been performed in humans, monkeys, sheep, dogs, rabbits, rats, mice, and cattle. We analyzed the expression of AQP2 in the kidneys of wild boars (Sus scrofa). AQP2 was localized in the principal cells of collecting ducts in medullary rays penetrating the renal cortex and in the collecting duct of the renal medulla. The presence of AQP2 was confirmed mainly in the apical plasma membrane but also in the intracellular components and basolateral membrane of the principal cells of the collecting ducts. Due to the key role of AQP2 in the regulation of water balance in mammals and the lack of studies in the literature concerning analysis of this protein in wild boars, this work completes the present state of knowledge by providing new information on .
