Specific ligation of surface alpha-D-galactosyl epitopes markedly affects the quantity of four major proteins secreted by macrophages

• Published in: Journal of leukocyte biology Vol. 52; no. 1; pp. 80 - 84
• Main Authors: WARFEL, A. H, ZUCKER-FRANKLIN, D
• Format: Journal Article
• Language: English
• Published: Bethesda, MD Society for Leukocyte Biology 01.07.1992; Federation of American Societies for Experimental Biology
• Subjects: Animals; Biological and medical sciences; Blood Proteins - metabolism; carbohydrates; collagenase; Epitopes - metabolism; fibronectin; Fibronectins - metabolism; Fundamental and applied biological sciences. Psychology; Fundamental immunology; Immunobiology; Lectins - physiology; Macrophages - metabolism; Male; Mice; Mice, Inbred C57BL; Microbial Collagenase - metabolism; Monocytes, macrophages; Myeloid cells: ontogeny, maturation, markers, receptors; oligosaccharide; plasminogen activator inhibitor type 2; Plasminogen Inactivators - metabolism; transglutaminase; Transglutaminases - metabolism; Proteins; Lectin; Vertebrata; Specificity; Mammalia; Antigenic determinant; Mouse; Secretion; Rodentia; Galactose; Cell surface; Macrophage

Activated macrophages (Mφs) have terminal α‐D‐galactosyl (αD‐Gal) residues on their membranes that are not apparent on resting cells. Ligation of these epitopes with Griffonia simplicifolia I‐B4 (GSI‐B4), a lectin that has specificity for α‐D‐Gal residues, alters selected Mφ functions. To explore th...