title: Different bindings to lectin in human submandibular gland after enzymatic digestion.
abstract: Lectin binding affinities were described in human submandibular gland (SMG) in the paraffin sections following alpha-amylase, sialidase, and trypsin digestions. Lectins in the present study were used Con A (Glc, Man binding lectins), PNA, and SBA(Gal, GalNAc), RCA-1(Gal), DBA(GalNAc), WGA(GlcNAc), and UEA-1(Fuc). Lectin stainings in serous and mucous acinar cells and ductal epithelia were reported to compare enzyme treated and nontreated sections. Amylase treatment showed increasing Con A staining in connective tissue fibers and no marked changes in SMG to lectin bindings. Sialidase digestion was characteristically intense in PNA and SBA bindings in SMG cells, and also enhanced staining to UEA-1 in serous and duct cells and to WGA in mucous and duct cells were noted. Trypsin digestion indicated a slight increase to Con A binding, and was relatively strong to UEA-1 in serous and duct cells and a little strong to WGA. The results suggested that SMG serous cells contain higher amounts of Gal, GalNAc, and Fuc residues; and mucous cells were also abundant in Gal, GalNAc, and GlcNAc residues.
mesh_terms: D002241:Carbohydrates / Q000032:analysis*; D003208:Concanavalin A / Q000378:metabolism; D006801:Humans; D037102:Lectins / Q000378:metabolism*; D009439:Neuraminidase; D019887:Peanut Agglutinin; D037121:Plant Lectins; D030262:Soybean Proteins; D013363:Submandibular Gland / Q000378:metabolism*; D014357:Trypsin; D014909:Wheat Germ Agglutinins; D000516:alpha-Amylases; D010835:Phytohemagglutinins
chemical_list: D002241:Carbohydrates; D003208:Concanavalin A; D037102:Lectins; D009439:Neuraminidase; D019887:Peanut Agglutinin; D037121:Plant Lectins; D030262:Soybean Proteins; D014357:Trypsin; D014909:Wheat Germ Agglutinins; D000516:alpha-Amylases; C017707:Ricinus communis agglutinin-1; C036850:Ulex europaeus lectins; C036554:dolichos biflorus agglutinin; C028824:soybean lectin; D010835:Phytohemagglutinins