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Journals / Turkish Journal of Biology / 2015 / Cilt: 39 - Sayı: 5

Immunohistochemical identification of aquaporin 2 in the kidneys of wild boars (Sus scrofa)

KATARZYNA MICHALEK
EWA CZERNIAWSKA-PIATKOWSKA
MARTA GRABOWSKA
MARIA LASZCZYNSKA
Pages
692–697
Publication Date
2015-12-04
DOI
—
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AI Summary & Key Takeaways

AI Insight
⚡ TL;DR(Too Long; Didn't Read)

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 immunolocalization and immunoexpression of aquaporin 2 in Sus scrofa kidneys.

📌 3 Key Takeaways

🎯
Objective & Hypothesis:Abstract: Mammalian aquaporins (AQPs) are a family of at least 13 small, integral membrane proteins expressed in various fluid-transporting epithelial cells.
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Key Findings & Data: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.
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Conclusion & Impact: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 immunolocalization and immunoexpression of aquaporin 2 in Sus scrofa kidneys.
🔬Design:Research Article
📍Scope:Comprehensive Sample
⚙️Variables:Aquaporin 2 · wild boars · immunohistochemistry

Abstract

Abstract: Mammalian aquaporins (AQPs) are a family of at least 13 small, integral membrane proteins expressed in various fluid-transporting 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 immunolocalization and immunoexpression of aquaporin 2 in Sus scrofa kidneys.

Özet

Abstract: Mammalian aquaporins (AQPs) are a family of at least 13 small, integral membrane proteins expressed in various fluid-transporting 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 immunolocalization and immunoexpression of aquaporin 2 in Sus scrofa kidneys.

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Cite This Article

MICHALEK, K., CZERNIAWSKA-PIATKOWSKA, E., GRABOWSKA, M., LASZCZYNSKA, M. (2015). Immunohistochemical identification of aquaporin 2 in the kidneys of wild boars (Sus scrofa). Turkish Journal of Biology, Cilt: 39 - Sayı: 5, 692–697. https://ajindex.com/articles/181475

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References (9)

  1. Agre P, Preston GM, Smith BL, Jung JS, Raina S, Moon C, Guggino WB, Nielsen S (1993). Aquaporin chip: the archetypal molecular water channel. Am J Physiol Renal Physiol 265: F463–F476. Bauchet AL, Masson R, Guffroy M, Slaoui M (2011). Immunohistochemical identification of kidney nephron segments in the dog, rat, mouse, and cynomolgus monkey. Toxicol Pathol 39: 1115–1128.
  2. Benga G (2009). Water channel proteins (later called aquaporins) and relatives: past, present, and future. IUMB Life 6: 112–133.
  3. Boone M, Deen P (2008). Physiology and pathophysiology of the vasopressin- regulated renal water reabsorption. Eur J Physiol 456: 1005–1024.
  4. Christensen BM, Zelenina M, Aperia A, Nielsen S (2000). Localization and regulation of PKA-phosphorylated AQP2 in response to V(2)-receptor agonist/antagonist treatment. Am J Physiol Renal Physiol 278: F29–42. Drolet R (2012). Urinary system. In: Zimmerman JJ, Karriker LA, Ramirez A, Schwartz KJ, Stevenson GW, editors. Disease of Swine. 10th ed. Oxford, UK: Wiley-Blackwell, pp. 263–283.
  5. Eskild-Jedsen A, Paulsen LF, Wogensen FL, Olesen P, Pedersen L, Frøkiær J, Nyengaard JR (2007). AT1 receptor blockade prevents interstitial and glomerular apoptosis but not fibrosis in pigs with neonatal induced partial unilateral obstruction. Am J Physiol Renal Physiol 292: F1771–F1781. Fenton R, Moeller HB, Hoffert DJ, Yu MJ, Nielsen S, Knepper M (2008). Acute regulation of aquaporin-2 phosphorylation at Ser-264 by vasopressin. Proc Natl Acad Sci USA 105: 3134– 3139. Fenton RA, Knepper MA (2007). Mouse models and the urinary concentrating mechanism in the new millennium. Physiol Rev 87: 1083–1112.
  6. Floyd RV, Mason SL, Proudman CJ, German AJ, Marples D, Mobasheri A (2007). Expression and nephron segmentspecific distribution of major renal aquaporins (AQP1-4) in Equus caballus, the domestic horse. Am L Physiol Integr Comp Physiol 293: 492–503.
  7. Fushimi K, Uchida S, Hara Y, Hirata Y, Marumo F, Sasaki S (1993). Cloning and expression of apical membrane water channel of rat kidney collecting tubule. Nature 361: 549–552.
  8. Gomes G, Agasse A, Thiébaud P, Delrot S, Gerós H, Chaumont F (2009). Aquaporins are multifunctional water and solute transporters highly divergent in living organisms. Biochim Biophys Acta 1788: 1213–1228.
  9. Hoffert JD, Fenton RA, Moeller HB, Simons B, Tchapyjnikov D, McDill BW, Yu MJ, Pisitkun T, Chen F, Knepper MA (2008). Vasopressin-stimulated increase in phosphorylation at Ser269 potentiates plasma membrane retention of aquaporin