Lectin binding affinities of induced pancreatic lesions in the hamster model

We examined the binding pattern of nine lectins to N-nitrosobis(2-oxopropyl)amine(BOP)-induced pancreatic lesions in Syrian hamsters. These lectinswere Arachis hypogaea(PNA), Dolichos biflorus (DBA), GriffoniasimplicifoliaI(GS-I), Helix aspersa(HAA), Helix pomatia (HPA),Sophora japonica (SJA), Ricinus communisI(RCA-I), Triticum vulgaris(WGA) and Ulex europaeus I (UEA-I). All of the lectins reactedin untreated control hamsters to varying intensities with cytoplasmiccomponents of acinar cells. GS-I, HPA, RCA-I and UEA-I boundto the basolateral surface and PNA, HAA and HPA to the luminalsurface of these cells. All but GS-I, RCA-I and UEA-I stainedthe cytoplasm of islet cells diffusely. In untreated controlhamsters, some ductal cells bound PNA, HAA and RCA-I, whereasthese cells reacted negatively to the remaining six lectins.Ductular cells did not bind any of the nine lectins. Hyperplasticductal cells in untreated hamsters were reactive with all ninelectins; however the intensity of the reactivity, cellular localizationand extent differed for each lectin. In carcinogen-treated hamsters,the binding pattern of the lectins to acinar and islet cellsdid not differ significantly from that in untreated hamsters,whereas cells of induced ductal and ductular lesions bound eachof the lectins in different patterns and intensities. The reactionof UEA-I to induced lesions was most consistent, specific andstrong, thereby indicating the presence of L-fucose in glycoproteinsproduced by altered cells. Although the binding affinity ofthe lectins to induced hyperplastic lesions differed in botha quantitative and qualitative fashion, all dysplastic and malignantlesions were reactive to each lectin. This result indicatesa heterogeneity in the carbohydrate structure of the glycoproteinsproduced by pancreatic cells during carcinogenicity.     

Lectin histochemistry of normal and neoplastic nasopharyngeal epithelium.

The cell surface carbohydrate profile of formalin-fixed paraffin-embedded tissue sections of normal and neoplastic epithelium was evaluated using 9 plant lectins. Three lectins, namely Con A, RCA and WGA, showed a similar pattern and staining intensity from normal epithelium to metaplastic squamous epithelium and nasopharyngeal intraepithelial neoplasia (NPIN). However, a decrease in staining reactivity was observed in undifferentiated nasopharyngeal carcinoma. Significant differences in intensity and distribution were seen in UEA and cryptic PNA residue (after neuraminidase pretreatment) from normal nasopharyngeal epithelium to NPIN. Infiltrative undifferentiated carcinomas showed a heterogenous lectin binding pattern and altered intensity of lectin binding in one case of DBA and three cases of PNA (no neuraminidase pretreatment), suggesting a variation in expression of carbohydrate by tumour cells. These results indicate that neoplasia in nasopharyngeal epithelium is associated with alterations in terminal sialic acid, -Fucose residues and -Gal-D-GalNac residues present in the outer parts of glycoconjugates. SBA, VVL and BSL failed to stain any types of epithelia. Desialylation of tissues by preincubation with neuraminidase did not expose DBA, SBA, VVL and BSL binding sites. These findings may be used as a baseline for evaluation of lectin binding in preinvasive and invasive lesions of the nasopharynx.     

Lectin binding sites of cultured ovarian Sertoli cell tumors and follicular granulosa cells

A panel of seven alkaline phosphatase labeled lectins was used to probe nitrocellulose electroblots of SDS-PAGE separated proteins from a primary culture of normal ovarian granulosa cells and an ENU-induced Sertoli cell tumor cell line (SCTL-I). Several additional lectin binding proteins were observed in silver stained SDS-PAGE gels as well as with lectins in SCTL-I. Succinated concanavalin A (Suc. Con A), Ricin communis agglutinin (RCA-I), Ulex europaeus agglutinin (UEA 1), Soybean agglutinin (SBA), Dolichos biflorus agglutinin (DBA) and Peanut agglutinin (PNA) stained more intensely in SCTL-I than normal granulosa cells. The same lectins as above, labeled with fluorescein isothiocyanate (FITC), were used to study the distribution of specific binding sites of tissue cultured cells grown in chamber/slides. Both normal ovarian granulosa cells and SCT cells exhibited strong peninuclear cytoplasmic labeling with Con A UEA-1 and WGA exhibited predominantly a nuclear and granular cytoplasmic staining pattern. SBA and DBA exhibited a strong coarse granular cytoplasmic labeling in granulosa cells and moderate granular cytoplasmic in SCT cells. In granulosa cells, Golgi regions stained strongly with PNA but weakly in SCT cells. RCA-I staining was negative in both cultures. Labeling of tissue cultured cells with lectins provides more details than histological sections of lectins binding sites at cellular structural levels.     

Loss of epithelial cell surface carbohydrates during experimental oral carcinogenesis in the rat

Cell surface glycoconjugates were investigated in a rat model of oral chemical carcinogenesis. The lectins Griffonia simplicifolia (GS-I-B4; specific for alpha-D-galactosyl end groups) and Ulex europeus (UEA-I; specific for alpha-L-fucosyl groups) were examined microspectrofluorimetrically in the oral epithelium of rats painted with the carcinogen 4-nitroquinoline N-oxide (4NQO) and compared with those treated with solvent alone. After labelling with GS-I-B4, the fluorescent intensity of the basal and parabasal epithelial cells was significantly less after 9 months of 4NQO treatment and in overt squamous cell carcinomas compared to controls. The fluorescent activity of the spinous epithelial cells in the non-invasive tissues treated with 4NQO and in the well differentiated (sites of keratin elaboration) malignant epithelium of squamous cell carcinomas was unchanged after labelling with UEA-I. UEA-I failed to stain undifferentiated (areas lacking keratin) malignant epithelium. The findings indicate that alpha-D-galactosyl residues are diminished on the membranes of premalignant and malignant rat epithelial cells. The expression of alpha-L-fucosyl groups, however, remains unchanged in premalignant rat oral epithelium and is closely correlated to the presence of keratin in the malignant epithelium of squamous cell carcinomas.     

Lectin histochemistry of the thyroid gland

The authors carried out a histochemical study with lectins (Ulex europaeus agglutinin-I [UEA-I], Triticum vulgaris [WGA], Glycine max [SBA], Dolichos biflorus [DBA], and Arachis hypogaea [PNA]) in different thyroid gland conditions (17 benign nodular goiters, three diffuse hyperplasias, five Hashimoto's thyroiditis, 20 follicular adenomas, 14 well-differentiated papillary carcinomas, five well-differentiated follicular carcinomas, and 30 normal thyroids) in order to determine if specific lectin patterns are developed during neoplastic transformation. The results showed that (1) in normal thyroid glands, the lectin, UEA-I, is able to discriminate between follicular cells and C-cells; (2) pathologic follicular epithelium had an increased expression of UEA-I, SBA, and WGA receptors; (3) no lectin or group of lectins allow a distinction between follicular carcinoma and papillary carcinoma; (4) when benign and malignant tumors are compared for UEA-I affinity there is a significantly greater frequency of malignant tumour with UEA-I receptor; and (5) although all investigated lectins have shown receptors in endothelial cells at least in one case, the most constant findings have been obtained with UEA-I and WGA. These findings suggest that lectins are not useful in routine diagnostic pathologic examination; however, in particular cases of follicular carcinoma, UEA-I may be a useful tool for the recognition of small vessels invaded by tumoral cells and the demonstration of fucose residues in malignant tumor cells.     

Brenner瘤细胞分化的凝集素受体标记

研究７种生物素化的凝集素对卵巢Ｂｒｅｎｎｅｒ瘤不同分化方向和分化性质瘤细胞的标记特点，麦胚素、花生素受体在瘤细胞呈顶浆型表达是瘤细胞向腺上皮分化的标志；双花扁豆素受体瘤细胞膜阳性显示其向鳞状上皮分化倾向；ＷＧＡ、ＰＮＡ、兀鹰素（ＢＳ－１）和刀豆素在瘤细胞浆内弥漫性结合增强表明Ｂｒｅｎｎｅｒ瘤由良性、增生性向恶性转化。凝集素受体表达差异可做为Ｂｒｅｎｎｅｒ瘤细胞的分化标志，体现该瘤上皮成分分化，失分     

Lectin binding to prostatic adenocarcinoma

The binding of different lectins (concanavalin A [Con A], triticum vulgaris [WGA], glycine maximum [SBA], dolichos bilflorus [DBA], ulex europaeus [UEA I], arachis hypogaea [PNA], and ricinus communis [RCA I]) to cells of normal prostate glands, hyperplastic glands and adenocarcinoma was studied. The Con A, WGA, DBA, PNA and RCA I bound to both normal and hyperplastic glands. The binding in the malignant glands differed from that of the benign conditions. The SBA, which was not bound by benign cells, was bound to the malignant glandular cells. Also, UEA I was bound to a part of the carcinoma cells. In addition, the binding pattern of Con A and WGA in the cells differed between the malignant and benign conditions. Based on the results of this study, it is suggested that lectin histochemical study might be useful in routine pathologic examination to detect malignant cells in cases which are doubtful with regard to malignancy by routine methods.     

Helix pomatia agglutinin binding in human tumour cell lines: correlation with pulmonary metastases in nude mice.

The extent of lectin binding by three human melanoma (LOX, FEMX-1 and SESX) and two sarcoma lines (MHMX and OHSX) was related to their potential for experimental metastasis formation in athymic nude mice. The Helix pomatia agglutinin (HPA), which recognises the N-acetyl-D-galactosamine ligand, showed differential binding to the cell lines in a manner that correlated with their ability to give lung colonies after i.v. injection in the mice (P < 0.005). The degree of HPA binding and lung colony formation of the cell lines studied was ranked in the following order, LOX > MHMX > OHSX > SESX > FEMX-I. Similar patterns were not observed with the other lectins used in this study (WGA, Con A, PNA and UEA-I). The high HPA reacting LOX melanoma line shows extensive pulmonary metastatic formation with no extrapulmonary colonies, whereas the low HPA reacting FEMX-I cells give only extrapulmonary metastases with no detectable colonies in the lungs. Precoating of tumour cells with HPA prior to injection did not reduce the ability of cells to give pulmonary metastases, suggesting that the HPA epitope was not functionally associated with the pulmonary metastatic potential observed in nude mice. These findings support recent human studies of a correlation between HPA binding and incidence of metastasis, however, our data indicate that there is no causal relationship. Further analyses are required to identify the specific HPA-binding glycoconjugates that may be involved.     

Lectin histochemistry of astrocytic tumors and in vitro characterization of lectin-induced modifications on the proliferation of the SW1088, U373 and U87 human astrocytic cell lines

The role of lectins as biosignalling molecules oras markers of human astrocytic tumors remains relativelyunexplored. The aim of the present work isto investigate (1) whether or not human astrocytictumors express specific glycans, evidenced experimentally by meansof lectin histochemistry, and (2) whether, in turn,these lectins can significantly modulate astrocytic tumor cellproliferation. Using a cell image processor, we thereforebegan by quantitatively measuring the histochemical binding patternof 5 lectins (WGA, PNA, PHA-L, GSA-IA4 andCon A) in 5 astrocytomas, 5 anaplastic astrocytomasand 5 glioblastomas. Secondly, we measured the influenceof these 5 lectins on the proliferation of3 astrocytic tumor cell lines (SW1088, U373 andU87) growing in vitro as monolayers. Cell proliferationwas assessed by means of the colorimetric MTTassay. The histochemical lectin staining markedly varied intra-and inter-group. However, some constant results were obtained.Indeed, the staining increased markedly from GSA-IA4 andPHA-L through WGA and PNA to Con Ain the three histopathological groups. The assessment ofcell proliferation demonstrated that WGA, Con A andPHA-L very significantly decreased proliferation in the 3astrocytic cell lines in a dose-dependent manner. Astrocytictumor cells in the confluent growth phase wereless sensitive to the WGA, Con A andPHA-L lectin-induced effects than cells in the loggrowth phase. The GSA-IA4 and PNA lectins hadglobally very weak effects on the proliferation ofthe astrocytic tumor cell lines. Increasing the fetalcalf serum from 1% to 10% in theculture media significantly antagonized the WGA-, Con A-and PHA-L-induced cell proliferation decrease in the 3astrocytic cell lines. In conclusion, the present datastrongly suggest that some lectins (including WGA, ConA and PHA-L) significantly influence the proliferation ofastrocytic tumor cells.     

Frequent expression of inducible nitric oxide synthase in esophageal squamous cell carcinomas.

Nitric oxide (NO) plays important biological roles in cardiovascular, nervous and immune systems, and is synthesized by nitric oxide synthase (NOS). Intracellular NO is known to cause DNA damage as a mutagen. We examined the expression of cytokine-inducible NOS (iNOS) in human esophageal squamous cell carcinomas. Weak iNOS immunoreactivity was seen in the basal and parabasal layers of non-neoplastic esophageal stratified squamous epithelium. iNOS expression was detected in 50 (87.7%) of the 57 esophageal squamous cell carcinomas, regardless of the depth of tumor invasion, histological differentiation and lymph node status. Early-stage cancers, i.e. mucosal squamous cell carcinomas, also showed significant iNOS expression. We speculate that increased iNOS expression is associated with the carcinogenesis of human esophageal cancer.     

Tissue binding of lectins in disorders of the breast

Twenty breast lesions including seven scirrhous ductal carcinomas, one infiltrating lobular carcinoma, one colloid carcinoma, four fibroadenomas, and seven cases of fibrocystic disease were analyzed by fluorescence microscopy for the presence and distribution of lectin-binding carbohydrates. Paraffin-embedded tissue sections were tested with wheat germ agglutinin (WGA), Ricin communis agglutinin I (RCA I), peanut agglutinin (PNA), Soybean agglutinin (SBA), Dolichos biflorus agglutinin (DBA), Ulex europaeus agglutinin I (UEA I), and concanavalin A (Con A). Brightest and most consistent staining regardless of the nature of the breast lesion was obtained with WGA followed in approximate order of staining intensity by RCA, PNA, SBA/DBA and Con A. UEA I stained many of the benign breast lesions but no malignant lesions. Lectin binding carbohydrate in benign lesions was localized mainly along the apices of mammary epithelial cells but there was considerable variation in staining patterns among malignant tumors. The fluorescence microscopic arrangement of lectin binding carbohydrate appears distinct for each malignant neoplasm of breast but is more consistent in benign conditions.     

Binding of FITC-labelled lectins to the gastrointestinal epithelium of the rat

Biotechnology uses lectin genes to transfect into crop plants for protection against insects and nematodes. On the other hand, the information is limited on lectin-binding properties of cells in the gastrointestinal tract. Therefore, binding of a panel of FITC-labelled plant lectins to gastrointestinal cells of the rat was studied. In the stomach, cytoplasmic staining of parietal cells by PHA appeared to be due to glycoproteins attached to the tubulovesicles. PNA also stained the parietal cells, but only in the isthmus and neck regions, reacting with desialylated glycoproteins. WGA bound to the mucous neck cells with higher affinity than to the surface and foveolar mucous cells. The mucous cells were also stained by SNA-I, UEA-I and, less intensively, by LCA. Chief cells did not show detectable reaction with any of the applied lectins. Binding of PHA to gastric cells showed differences when compared with the results of in vivostudies. Small intestinal brush border was stained with UEA-I and SNA-I, the latter lectin also strongly stained the surface of small intestinal crypts. Both lectins reacted with the mucus of goblet cells. In the large intestine UEA-I and SNA-I stained the goblet cells at the base and upper part of the crypts, respectively. Accordingly, we provided evidences for the unique lectin-binding phenotype of the various segments of the gastrointestinal tract.     

Lectin histochemistry as a predictor of dysplasia grade in colorectal adenomas

Lectins are sugar-binding proteins that bind to specific cellular carbohydrates, commonly affecting cellular physiology. Phaseolus vulgaris leucoagglutinin (PHA), ulex europaeus isoagglutinin-I (UEA-I), wheat germ agglutinin (WGA) and peanut agglutinin (PNA) are among the most well studied lectins in various tissues. The purpose of this study was to detect the above lectins binding sites and so examine alterations in glycoconjugate expression in neoplastic cells of 52 colorectal adenomas with various clinicopathologic characteristics and proliferation rates. Lectin histochemistry was performed in paraffin sections with and without neuraminidase treatment. Proliferative fraction was determined by immunolabelling for Proliferating Cell Nuclear Antigen. PHA was the more frequently positive lectin in the examined specimens; however, it was simultaneously detected in normal colonic mucosa and so was WGA. The frequency of high grade dysplasia was significantly greater in older patients and in samples with UEA-I positivity without neuraminidase pretreatment. UEA-I-reactive adenomas were generally characterized by high cell proliferation rates. A statistical model based on patients age and UEA-I binding without neuraminidase treatment can generally predict grade of dysplasia in 83% of adenomas and particularly high grade dysplasia in up to 93% of adenomas; so, such a model may be potentially useful for the early detection of neoplasia, for instance in exfoliative cells from the large intestine.     

Lectin binding to oral squamous carcinoma

Ten benign epithelial hyperplasias, ten invasive squamous carcinomas, and one each of verrucous carcinoma and carcinoma in situ of the oral mucosa were examined immunoenzymatically using biotinylated lectins and avidin-biotin-peroxidase complex to localize glycoconjugates in the epithelial cells. All of the lectins intercellularly bind to benign and malignant epithelial cells. Also, lectins bind to the cytoplasm of the basal cells and all layers of carcinoma in situ. Verrucous carcinoma shows a similar binding as does the benign epithelial hyperplasia. However, in invasive squamous carcinoma some nests and individual invasive cells show intense cytoplasmic binding and a loss of cell surface binding to lectins, especially with Con A, and may be a marker for invasive potential of squamous carcinoma.     

Lectin binding sites in normal rat ovary and ENU-induced Sertoli cell tumors of the ovaries

A panel of seven fluorescein isothiocyanate (FITC) labeled lectins were used to study the distribution of specific binding sites in histologic sections of rat ovaries and ENU-induced Sertoli cell tumors (SCT) of the ovaries. Ten SCT and 5 normal ovaries derived from Berlin Druckey IV (BD-IV) rats were examined by FITC lectins. The tissues examined were fixed in 10% buffered formalin and embedded in paraffin blocks. In normal ovaries, lectin binding sites were more uniform, ordered and consistent than in ovarian SCT where some lectin staining appeared disorderly inconsistent and varied with the degree of tumor differentiation. Two lectins, (from Triticum vulgaris [WGA] and Arachis hypogaea [PNA], uniformly stained the apices of the ovarian surface epithelium and subadjacent tunica vaginalis. The ovarian stroma, oocyte nucleus, follicular and granulosa-theca cells, stained uniformly strong with succinated Con A (from Con-canavalia ensiformis). Three lectins (from Triticum vulgaris, Ulex europeaus [UEA-1] and Arachis hypogeae) accentuated the basal lamina in the SCT and normal ovarian follicles. The zona pellucida was strongly labeled with lectin derived from Triticum vulgaris, Ricinus communis (RCA) and moderately with lectin derived from Arachis hypogeae. The oviduct ampulla exhibited an intracytoplasmic strong vesicular labeling with lectins derived from Triticum vulgare, Dolichos biflorus (DBA), Glycin max (Soybean-SBA) and Arachis hypogeae. The SCT cells showed an inconsistent, irregular labeling pattern with lectins derived from Ulex europaeus, Dolichos biflorus and Soybean mostly as a coarse granular cytoplasmic labeling. Neuraminidase digestion enhanced lectin staining with PNA in normal ovary and in SCT. This data provided at list of lectin markers for distinct components of the BD-IV rat ovary and ovarian SCT.     

Lectin binding properties of human follicular center lymphocytes and follicular (nodular) lymphomas

The distribution of lectin binding receptors in normal human lymphoid tissue and follicular (nodular) lymphoma was studied in tissue sections using a panel of lectin-peroxidase and lectin-fluorescein conjugates: Concanavalin A (Con A), Peanut agglutinin (PNA), Lotus tetragonolobus agglutinin (LTA), Soybean agglutinin, Ulex europeus and Bandeiraea simplicifolia. Two lectins studied, PNA and LTA were found to bind selectively to the cell membranes of follicular centre lymphocytes in normal lymphoid tissue, and to the neoplastic cells of follicular (nodular) lymphomas. Con A, in contrast, bound selectively to follicular centre macrophages (tingible body cells) and identified in follicular (nodular) lymphomas a population of dendritic-like cells not otherwise recognized and possibly corresponding to dendritic cells identified ultrastructurally. Follicular (nodular) lymphomas share the lectin binding properties of non-neoplastic follicular centres. The expression of receptors for lectins with blood group activity (PNA T-like, LTA H-like) on follicular lymphocytes may play a role in follicle formation.     

Binding of wheat and peanut lectins to human transitional cell carcinomas. Correlation with histopathologic grade, invasion, and DNA ploidy

The binding of peanut (PNA) and wheat germ (WGA) lectins to tissue sections was examined in biopsy specimens from normal urothelium (ten patients) and from tumor tissue of noninvasive (17 patients) and invasive bladder (31 patients) carcinomas. The results were correlated to DNA content, histopathologic grade, and the presence or absence of invasion. Significant alterations in lectin binding associated with the development of cancer were found. A gradual loss of both PNA and WGA binding was found to correlate with higher grades of atypia (P less than 0.001). The loss of WGA binding was significantly correlated with both tumor aneuploidy (P less than 0.001) and the presence of invasion (P less than 0.05), whereas no significant correlation was found between loss of PNA binding and these variables. We concluded that the loss of WGA binding structures associated with bladder cancer shows a better correlation with known risk factors (aneuploidy and invasion) than the loss of PNA binding does.     

A Study of Glycoconjugates in Nasopharyngeal Carcinoma with Correlation to Clinical Transformation

Little is known about the glycoconjugate changes in human nasopharyngeal epithelium following neoplastic changes. Glycoconjugate histochemistry (Glycine maximus (SBA), Griffonia simplicifolia II (GSA-II), Ulex europaeus (UEA-I), Arachis hypogaea (PNA) and Canavalia ensiformis (ConA)) were performed on the following nasopharyngeal biopsies: 10 adenoid tissues (benign controls), 10 chronic inflammation, 20 squamous metaplasia, 20 undifferentiated carcinoma and 5 squamous cell carcinoma. These results were correlated with the clinical transformations findings. Strong ConA and PNA staining (after neuraminidase treatment (NA)) characterized a subpopulation of squamous metaplasia subjects who later transformed to nasopharyngeal carcinoma. Strong ConA and PNA (before and after NA) depicted the majority of undifferentiated carcinoma subjects having local recurrence following irradiation therapy. In squamous metaplasia, ConA and PNA (after NA) staining may serve as a warning sign for neoplastic changes. Strong stainings for ConA and PNA (before and after NA) in undifferentiated carcinoma subjects may predict a risk for local recurrence.     

Lectin binding patterns in diffuse large cell lymphoma

The staining reaction of a panel of lectins in paraffin embedded lymph node specimens of diffuse large cell lymphoma was studied in relation to survival. In 47 of 49 patients, varying degrees of lectin binding were observed with Ricinus communis agglutinin (RCA), crude extract of Arachis hypogaea (c-PNA), Concanavalin ensiformis A (Con A), Triticum vulgaris A (WGA) and Phaseolus vulgaris A (PHA). Binding was either absent or only minimal with Pisum sativum A (PSA) and Lens culinaris A (LCA). Two categories of binding were observed: cell surface and cytoplasmic. Cell surface binding was seen in tumor cells, while cytoplasmic binding was observed in macrophage-histiocytes. Varying numbers of tumor cells were stained with RCA, WGA, c-PNA or PHA; but with Con A virtually no tumor cells were stained. Stromal macrophage-histiocytes were stained with RCA, WGA, or Con A in all but one case, frequently with all three lectins; c-PNA binding macrophage-histiocytes were absent in one third of the cases. With PHA the staining of stromal macrophage-histiocytes was extremely rare. Tumor cells that stained with RCA but not with c-PNA were observed in 9 of 15 patients who survived more than 2 years after diagnosis. In all 15 long-term survivors, stromal macrophage-histiocytes were positive for c-PNA. Tumor cells that reacted with c-PNA but not with RCA were seen in five patients who survived less than two years. All 16 patients whose tumors lacked c-PNA binding stromal macrophage-histiocytes in the presence of RCA binding macrophage-histiocytes were short-term survivors. These observations suggest the heterogeneity of stromal macrophage-histiocytes as well as that of tumor cells. Furthermore, the variation of lectin binding might be useful in assessing prognosis.     

Relationships between degree of binding,cytotoxicity and cytoagglutinating activity of plant-derived agglutinins in normal lymphocytes and cultured leukemic cell lines

PURPOSE: To clarify the relationships between the degree of lectin-cell binding, cytotoxicity and cytoagglutinating activity of plant-derived lectins in normal lymphocytes and cultured leukemic cell lines. METHODS: Plant lectins with different quaternary structures and saccharide specificity were used: Dolichos biflorus agglutinin (DBA), Soybean agglutinin (SBA) and Wheat germ agglutinin (WGA). The leukemic cell lines used were: Jurkat, MOLT-4, RPMI-8402, HPB-ALL, CCR-HSB-2 and BALL-1 (derived from acute lymphoblastic leukemia); Raji and Daudi (derived from Burkitt's lymphoma); K-562 (derived from myelogenous leukemia). The lectin-cell binding was detected microscopically and fluorimetrically using FITC-conjugated lectins. Cytotoxicity was estimated by the CellTiter-Glo luminescent cell viability assay, and cytoagglutinating activity by a spectrophotometric method. RESULTS: The binding of DBA and SBA to normal lymphocytes was negligible, while their binding to leukemic cells increased markedly with increasing lectin concentration. Analogous results were obtained for WGA. However, it was found that WGA also interacted to a significant degree with normal lymphocytes. The degree of lectin-cell binding increased in the order: DBA相似文献