Expression of Glycoconjugates in Pancreatic, Gastric, and Colonic Tissue by Bauhinia purpurea, Vicia villosa, and Peanut Lectins

Abstract

We have earlier prepared a pancreatic cancer-associated mucin, whose altered carbohydrate structure was recognized by Vicia villosa (VVA), Bauhinia purpurea (BPA), and peanut (PNA) lectins and which was found preferentially in the sera of patients with pancreatic or gastric cancer. Cancer-associated structures of the sugar chain on serum antigen may reflect those occurring in malignant tissues. Accordingly, we investigated the tissue distribution of carbohydrate structures reactive to these lectins by using lectin histochemistry in pancreatic cancer, gastric cancer, and colonic cancer tissue specimens and in their normal counterparts. VVA showed a higher affinity for pancreatic cancer (77.5%), gastric cancer (89%), and colonic cancer (87%) cells than for the cells of their normal counterparts, whose affinity was 0%, 41.7%, and 36.4%, respectively. PNA showed a higher affinity for pancreatic (70%) and colonic cancer cells (86.5%). BPA failed to show significant binding differences between neoplastic and normal cells in any of the pancreatic, gastric, or colonic tissue specimens. It did, however, bind to intraductal contents in most of the pancreatic cancer tissues but bound to intraductal contents in only a few chronic pancreatitis and normal pancreatic tissues. VVA and PNA did not bind to intraductal contents in any of the normal, chronic pancreatitis, or pancreatic cancer tissues. These results imply that, among the lectins used so far, VVA has the highest affinity for neoplastic cells, and it may provide a supplement for use in the pathologic diagnosis of malignant diseases.(ABSTRACT TRUNCATED AT 250 WORDS)

Purification and molecular cloning of a new galactose-specific lectin from Bauhinia variegata seeds

“…Additionally, we have previously shown that B. variegata lectin has pro-infl ammatory activity, inducing neutrophil migration dependent on resident mast cells (Alencar et al 2001). BVL is similar to B. purpurea agglutinin, which has been used to probe the structural and functional role of cell surface carbohydrates (Horan et al 1999), to detect sugar moieties on normal and neoplastic cell surfaces (Sarker et al 1994), to serve as a marker for identifi cation of different cell types and as a reagent for cell separations (Shue et al 1993;Kasper et al 1994;Sarker et al 1995). This observation suggests that BVL I and BVL II can also be used as potential tools for the study of several biological activities in different cellular systems.…”

Recognition profile of Bauhinia purpurea agglutinin (BPA)

“…A chimeric lectin recombinantly produced from BPA and Lens culinaris showed a different binding affinity than its original parental ones (Yamamoto et al, 2000b). Because of the different affinity of BPA to the surface, as well as cytoplasmic glycan distribution in various cell types described previously (Kasper et al, 1994;Sarker et al, 1992Sarker et al, , 1994Sarker et al, , 1995Shue et al, 1993), we were impelled to examine its binding characteristics. Although the structural nature required for BPA binding with carbohydrates has been documented via quantitative precipitin (QPA) and precipitin inhibition assays (QPIA) (Wu et al, 1980), this information is mainly limited to monomer or submolecular Galh1-3GalNAc (T) and Galh1-related oligosaccharides.…”

“…It is a glycoprotein (gp) containing a long metal-binding loop, part of which determines its carbohydrate specificity (Yamamoto et al, 2000a). The specific binding properties of BPA have been applied to probe the structural and functional role of cell surface carbohydrates (Horan et al, 1999), to detect sugar moieties on normal and neoplastic cell surfaces (Sarker et al, 1994), to serve as a marker for identification of different cell types, and as a reagent for cell separations (Kasper et al, 1994;Sarker et al, 1992Sarker et al, , 1995Shue et al, 1993).…”

Lectin microarray technology identifies specific lectins related to lymph node metastasis of advanced gastric cancer

“…Because these cancer cell lines are heterogeneous, it is inadequate to define the NEC lectins as merely not binding to these gastric cancer cell lines. In fact, both PNA and VVA are NEC lectins expressed in primary AGC, and moreover it was reported that these lectins bind to gastric cancer cells [34][35][36]. This designation should therefore limit this analysis.…”