Exploring the role of galectin 3 in kidney function: a genetic approach
Authors: Bichara, Maurice; Attmane-Elakeb, Amel; Brown, Dennis; Essig, Marie; Karim, Zoubida; Muffat-Joly, Martine; Micheli, Laetitia; Eude-Le Parco, Isabelle; Cluzeaud, Françoise; Peuchmaur, Michel; Bonvalet, Jean-Pierre; Poirier, Françoise; Farman, Nicolette
Source: Glycobiology, Volume 16, Number 1, January 2006 , pp. 36-45(10)
Publisher: Oxford University Press
Abstract:Galectin 3 belongs to a family of glycoconjugate-binding proteins that participate in cellular homeostasis by modulating cell growth, adhesion, and signaling. We studied adult galectin 3 null mutant (Gal 3–/–) and wild-type (WT) mice to gain insights into the role of galectin 3 in the kidney. By immunofluorescence, galectin 3 was found in collecting duct (CD) principal and intercalated cells in some regions of the kidney, as well as in the thick ascending limbs at lower levels. Compared to WT mice, Gal 3–/– mice had ~11% fewer glomeruli (p < 0.04), associated with kidney hypertrophy (p < 0.006). In clearance experiments, urinary chloride excretion was found to be higher in Gal 3–/– than in WT mice (p < 0.04), but there was no difference in urinary bicarbonate excretion, in glomerular filtration, or urinary flow rates. Under chronic low sodium diet, Gal 3–/– mice had lower extracellular fluid (ECF) volume than WT mice (p < 0.05). Plasma aldosterone concentration was higher in Gal 3–/– than in WT mice (p < 0.04), which probably caused the observed increase in α-epithelial sodium channel (α-ENaC) protein abundance in the mutant mice (p < 0.001). Chronic high sodium diet resulted paradoxically in lower blood pressure (p < 0.01) in Gal 3–/– than in WT. We conclude that Gal 3–/– mice have mild renal chloride loss, which causes chronic ECF volume contraction and reduced blood pressure levels.
Document Type: Research Article
Publication date: 2006-01-01
- Established as the leading journal in the field, Glycobiology provides a unique forum dedicated to research into the biological functions of glycans, including glycoproteins, glycolipids, proteoglycans and free oligosaccharides, and on proteins that specifically interact with glycans (including lectins, glycosyltransferases, and glycosidases).
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- In this Subject: Anatomy & Physiology
- By this author: Bichara, Maurice ; Attmane-Elakeb, Amel ; Brown, Dennis ; Essig, Marie ; Karim, Zoubida ; Muffat-Joly, Martine ; Micheli, Laetitia ; Eude-Le Parco, Isabelle ; Cluzeaud, Françoise ; Peuchmaur, Michel ; Bonvalet, Jean-Pierre ; Poirier, Françoise ; Farman, Nicolette