Activation of oxidative burst and degranulation of porcine neutrophils by a homologous spleen galectin-1 compared to N-formyl-L-methionyl-L-phenylalanine and phorbol 12-myristate 13-acetate.

ELOLA, M. T.; CHIESA, M. E.; FINK, N. E.

COMPARATIVE BIOCHEMISTRY AND PHYSIOLOGY. PART B, BIOCHEMISTRY & MOLECULAR BIOLOGY.

Elsevier

Lugar: ONTARIO; Año: 2005 vol. 141 p. 23 - 31

1096-4959

Galectins are a family of animal lectins defined by their beta-galactoside-binding activities and a consensus sequence in their carbohydrate-recognizing domain (CRD). Relevant roles of galectins are described in adaptive immune response, innate immunity and modulation of the acute inflammatory response. We have extended our previous studies on a porcine spleen galectin-1 in relation to its functional roles such as polymorphonuclear neutrophils (PMNs) stimulation compared to well known PMN acticators e. g. N-formyl-L-methionyl-L-leucyl-L-phenylalanine (fMLP) and phorbol 12-myristate 13-acetate (PMA). Relative to activation of NADPH-oxidase, fMLP and PMA are stronger than galectin-1 plus cytochalasin B (CB) when the lectin is employed at low concentrations (gal-1 1 µM, 3.6 ±0.8 nm O2-/min/107 PMN). Higher doses of galectin-1 (10 µM) plus CB produced a significant activation of NADPH-oxidase (27.9±14.8 nm O2-/min/107 PMN) and stimulated PMN degranulation up to 50%. We propose that local galectin-1 concentrations under physiolological conditions might reach suitable levels for pig PMN stimulation, and might be a natural inducer of O2- formation or degranulation. Porcine galectins might produce enhanced responses in vivo when they stimulate neutrophils in combination with some other stimuli.