In situ ultrastructural localization of sugar-binding sites in lizard granulosa cell nuclei.
Mannose-binding sites were detected at the ultrastructural level in nuclei of lizard granulosa cells in situ by means of mannosylated ferritin. When ultrathin sections of material embedded in glycol methacrylate were incubated with mannosylated ferritin, a strong labelling was observed over nucleoli, chromatin and the external leaflet of the nuclear envelope, but no labelling was detected in the perinuclear space except for nuclear pores. This labelling was clearly inhibited when sections were incubated in a solution containing both mannosylated ferritin and a sugar-related neoglycoprotein (mannosylated serum albumin). These ultrastructural data supporting the existence of nuclear lectin-like components in reptilian cells are in agreement with our previous findings about such components in nuclei isolated from mammalian cells. Owing to the unique organization of the granular component of the nucleoli in specialized granulosa cells, we are able to show that some of the mannose-binding sites are associated with ribosomal precursors.
D000818:Animals; D002352:Carrier Proteins / Q000378:metabolism*; D002467:Cell Nucleus / Q000378:metabolism* / Q000648:ultrastructure; D005260:Female; D006107:Granulosa Cells / Q000378:metabolism* / Q000648:ultrastructure; D008116:Lizards; D008358:Mannose / Q000378:metabolism*; D037241:Mannose-Binding Lectins; D008854:Microscopy, Electron; D009865:Oocytes / Q000378:metabolism / Q000648:ultrastructure
D002352:Carrier Proteins; D037241:Mannose-Binding Lectins; D008358:Mannose