Over activation of hippocampal serine/threonine protein phosphatases PP1 and PP2A is involved in lead-induced deficits in learning and memory in young rats.

Serine/threonine protein phosphatases regulate several key cellular events in the brain, including learning and memory. These enzymes, when over-activated, are known to function as a constraint on learning and memory. We investigated whether these phosphatases are implicated in lead (Pb)-induced deficits in learning and memory.

The selective expression of distinct fucosylated glycoproteins on murine T and B lymphocyte subsets.

The putative expression of distinct terminally fucosylated glycoconjugates among murine lymphocyte subpopulations was sought using Ulex europaeus agglutinin-I (UEA-I) and Anguilla anguilla agglutinin (AAA), each with a distinctive primary binding preference to type II and type I blood group H oligosaccharide determinants, respectively. In newly born and adult mice, direct labeling of isolated lymphocyte subsets in suspension, as well as immunohistochemical assays were indicative of the age-regulated co-expression of the UEA-I-reactive ligand among thymic epithelial cells and a subset of the mature (PNA-), medullary thymocytes. In the spleen, UEA-I-ligand expression was selectively confined to a subset of the CD4+ T lymphocytes scattered around red pulp sinuses in newly born mice, but distinctively localized within the T cell-dependent periarteriolar lymphoid sheath compartment in adult mice.

Distinct binding patterns of fucose-specific lectins from Biomphalaria alexandrina and Lotus tetragonolobus to murine lymphocyte subsets.

The putative expression of distinct terminally fucosylated glycoconjugates among murine lymphocyte subpopulations was sought using a Biomphalaria alexandrina-derived lectin (BaSI), of proven specificity to a fucosyllactose determinant, and the fucose-binding lectin from Lotus tetragonolobus seeds. Direct labeling of isolated lymphocyte subsets in suspension as well as immuno-histochemical and two-dimensional Western blotting assays demonstrated the exclusive expression of the BaSI-reactive ligand among multiple isoforms of two major 95 and 92 kDa and a minor 82 kDa acidic glycoproteins, selectively localized to the splenic marginal zone B lymphocytes of adult mice. The expression of the L.