Localization of endogenous beta-galactoside-specific lectins by neoglycoproteins, lectin-binding tissue glycoproteins and antibodies and of accessible lectin-specific ligands by mammalian lectin in human breast carcinomas.
Protein-carbohydrate interactions constitute a system of molecular interaction with relevance to pathologic conditions. Carrier-immobilized carbohydrate structures enable the histochemical investigation of the protein part of this recognitive system. However, thorough systematic studies are inevitably required for standardized application of this relatively novel class of markers. Consequently, serial sections of 21 cases of malignant breast lesion were comparatively analyzed with three different types of probe, specific for beta-galactoside-binding lectins. In addition to the chemically lactosylated neoglycoprotein, human lectin-binding glycoproteins, purified by affinity chromatography on resins with an immobilized beta-galactoside-specific lectin, and a lectin-specific antibody were employed to answer the question whether differences occur in their capacity for lectin localization. The patterns of staining were qualitatively similar, the lectin-binding glycoproteins yielding the most intense reaction. Having assured the reliable applicability of the neoglycoprotein, structural alterations of the subterminal carbohydrate residue on the labelled carrier addressed the issue, whether selectivity of binding can be inferred histochemically, allowing rational synthetic tailoring. An N-acetylglucosamine residue in beta-1,3-linkage proved to be a less favorable extension than this type of sugar in beta-1,4-linkage or an N-acetylgalactosamine moiety in beta-1,3-linkage. Binding was clearly reduced in cells of normal breast tissue with this probe. In order to gain evidence on the expression of potential carbohydrate ligands for the glyco- and immunohistochemically localized binding activity, a labelled mammalian beta-galactoside-specific lectin was similarly used as histochemical tool. It effectively bound to accessible sites in the sections. The binding pattern was different to that of plant lectins with specificity to beta-galactosides. This result underscores that caution is necessary in the functional interpretation of results of studies with plant, not mammalian lectins.(ABSTRACT TRUNCATED AT 250 WORDS)
Gabius
H J
HJ
Max-Planck-Institut für experimentelle Medizin, Abteilung Chemie, Göttingen, FRG.
Wosgien
B
B
Brinck
U
U
Schauer
A
A
D000906:Antibodies; D001665:Binding Sites; D001943:Breast Neoplasms / Q000378:metabolism*; D005697:Galactosides / Q000378:metabolism*; D006023:Glycoproteins; D006801:Humans; D007150:Immunohistochemistry; D037102:Lectins / Q000378:metabolism*; D008024:Ligands; D013194:Staining and Labeling; D014018:Tissue Distribution
D000906:Antibodies; D005697:Galactosides; D006023:Glycoproteins; D037102:Lectins; D008024:Ligands; C007816:beta-galactoside