Glycobiology Advance Access originally published online on November 1, 2002
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Glycobiology, 2003, Vol. 13, No. 2 119-128
© 2003 Oxford University Press
Opposite effects of galectin-1 on alternative metabolic pathways of L-arginine in resident, inflammatory, and activated macrophages
2 Immunology, Department of Clinical Biochemistry, School of Chemical Sciences, National University of Córdoba, Calle Haya De La Torre Esquina Medina Allende (C. 5000), Córdoba, Argentina
3 Centre of Electron Microscopy, School of Medicine, National University of Córdoba,Casilla Postal 362 (C. 5000), Cordóba, Argentina
4 Division of Immunogenetics, Hospital de Clínicas "José de San Martín," School of Medicine, University of Buenos Aires, Av. Córdoba 2351, 3erPiso, Sala 4 (C. 1120) Ciudad de Buenos Aires, Argentina
Received on June 29, 2002; revised on September 8, 2002; accepted on September 10, 2002
Recent evidence has implicated galectins and their carbohydrate ligands as master regulators of the inflammatory response. Galectin-1, a member of this family, has shown specific anti-inflammatory and immunoregulatory effects. To gain insight into the potential mechanisms involved in these effects, we investigated the effects of galectin-1 in L-arginine metabolism of peritoneal rat macrophages. Pretreatment of macrophages with galectin-1 resulted in a dose- and time-dependent inhibition of lipopolysaccharide-induced nitric oxide (NO) production, accompanied by a decrease in inducible nitric oxide synthase (iNOS) expression (the classic pathway of L-arginine). On the other hand, galectin-1 favored the balance toward activation of L-arginase, the alternative metabolic pathway of L-arginine. Inhibition of NO production was not the result of increased macrophage apoptosis because addition of this ß-galactoside-binding protein to macrophages under the same experimental conditions did not affect the apoptotic threshold of these cells. To understand how endogenous galectin-1 is regulated in macrophages under inflammatory stress, we finally explored the ultrastructural distribution, expression, and secretion of galectin-1 in resident, inflammatory, and activated macrophages. This study provides an alternative cellular mechanism based on the modulation of L-arginine metabolism to understand the molecular basis of the anti-inflammatory properties displayed by this carbohydrate-binding protein.
1 To whom correspondence should be addressed; e-mail: gabyrabi{at}ciudad.com.ar
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