Galectin-3 expression is induced in renal beta-intercalated cells during metabolic acidosis.
The adaptation of the cortical collecting duct (CCD) to metabolic acidosis requires the polymerization and deposition in the extracellular matrix of the novel protein hensin. HCO3(-)-secreting beta-intercalated cells remove apical Cl-:HCO3(-) exchangers and may reverse functional polarity to secrete protons. Using intercalated cells in culture, we found that galectin-3 facilitated hensin polymerization, thereby causing their differentiation into the H+-secreting cell phenotype. We examined the expression of galectin-3 in the rabbit kidney and its relationship to hensin during metabolic acidosis. In control kidneys, galectin-3 was expressed in the cortical and medullary collecting ducts. In the outer cortex 26 +/- 3% of CCD cells expressed galectin-3 compared with 64 +/- 3% of the cells of the inner cortex. In the CCD, galectin-3 was rarely expressed in beta-intercalated cells, being primarily present in alpha-intercalated and principal cells. During metabolic acidosis, the intensity of cellular staining for galectin-3 increased and more cells began to express it; the percentage of CCD cells expressing galectin-3 increased from 26 +/- 3 to 66 +/- 3% in the outer cortex and from 64 +/- 3 to 78 +/- 4% in the inner cortex. This was particularly evident in beta-intercalated cells where expression was found in only 8 +/- 2% in control animals but in 75 +/- 2% during metabolic acidosis in the outer cortex and similarly for the inner cortex (26 +/- 6 to 90 +/- 7%). Importantly, both galectin-3 and hensin were found in the extracellular matrix of microdissected CCDs; and during metabolic acidosis, many more cells exhibited this extracellular colocalization. Thus galectin-3 may play several important roles in the CCD, including mediating the adaptation of beta-intercalated cells during metabolic acidosis.
Schwaderer
Andrew L
AL
Department of Pediatrics, University of Rochester School of Medicine, New York, USA.
Vijayakumar
Soundarapandian
S
Al-Awqati
Qais
Q
Schwartz
George J
GJ
D000138:Acidosis / Q000378:metabolism*; D000818:Animals; D016326:Extracellular Matrix Proteins / Q000378:metabolism* / Q000648:ultrastructure; D037502:Galectin 3 / Q000378:metabolism* / Q000502:physiology / Q000648:ultrastructure; D007150:Immunohistochemistry; D007668:Kidney / Q000378:metabolism*; D007685:Kidney Tubules, Collecting / Q000166:cytology / Q000378:metabolism*; D051379:Mice; D018613:Microscopy, Confocal; D011817:Rabbits; D051381:Rats; D051116:Receptors, Scavenger / Q000378:metabolism* / Q000648:ultrastructure
D016326:Extracellular Matrix Proteins; D037502:Galectin 3; D051116:Receptors, Scavenger; C495130:hensin protein, rabbit