Stimulated macrophages express a new glycoprotein receptor reactive with Griffonia simplicifolia I-B4 isolectin.
AUTOR(ES)
Maddox, D E
RESUMO
This paper presents data on reactions of murine macrophages with a variety of lectins, with special focus on Griffonia simplicifolia I-B4 isolectin, the only lectin we tried that distinguishes stimulated macrophages from resident populations. Specificity of Griffonia simplicifolia I reaction with carbohydrate determinants at the cell surface is shown by (i) ability of alpha-galactosidase treatment of intact cells to abolish all lectin binding whereas beta-galactosidase has no effect on lectin binding, (ii) ability of methyl alpha-D-galactopyranoside to completely inhibit lectin binding with methyl alpha-D-galactopyranoside having no effect on lectin binding, (iii) ability of brief treatment of intact cells with trypsin to liberate a glycopeptide but reacts with G. simplicifolia I to form a precipitate that is dissolved by addition of methyl-alpha-D-galactopyranoside or alpha-galactosidase, (iv) ability of methyl alpha-D-galactopyranoside (but no other monosaccharide) to completely inhibit avid binding of macrophages to G. simplicifolia I lectin immobilized on an insoluble support, and (v) ability of immobilized lectin to separate macrophages into highly pure subpopulations of lectin-reactive and lectin-unreactive cells, as shown by examination of fluorescein-labeled lectin-treated cells with phase-contrast/fluorescence microscopy.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=345683Documentos Relacionados
- An insecticidal N-acetylglucosamine-specific lectin gene from Griffonia simplicifolia (Leguminosae).
- A new “kid” on the platelet thrombin receptor “block”: Glycoprotein Ib–IX–V
- Carbohydrate binding and resistance to proteolysis control insecticidal activity of Griffonia simplicifolia lectin II
- A thrombin receptor function for platelet glycoprotein Ib–IX unmasked by cleavage of glycoprotein V
- Platelet storage results in a redistribution of glycoprotein Ib molecules. Evidence for a large intraplatelet pool of glycoprotein Ib.