Binding of soybean agglutinin lectin to prostatic hyperplasia and adenocarcinoma

Loy, Timothy S.; Kyle, J.; Bickel, John T.

doi:10.1002/1097-0142(19890415)63:8<1583::aid-cncr2820630823>3.0.co;2-k

Cited by 11 publications

(3 citation statements)

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“…64 Another report indicated that SBA was not useful in distinguishing prostatic hyperplasia from an adenocarcinoma because positive staining was obtained in both of them. 65 Cytoagglutination or aggregation is one of the mechanisms used by lectins to interact with cancer cells. 66,67 Table 3 shows some examples of studies on the inhibitory effect of soybean lectin on malignant cells.…”

Section: Lectins: Structure Binding Speci Cities and Physiologic Efmentioning

confidence: 99%

The Anticarcinogenic Potential of Soybean Lectin and Lunasin

2003

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Cancer is one of the leading causes of death worldwide, generally exceeded only by cardiovascular disease in the developed world. The number of people diagnosed with cancer within the next few decades is expected to double. There will therefore be increased demand for novel diagnostic and medical therapies that use new non-traditional sources. Soybeans contain a variety of anticarcinogenic phytochemicals. Recently, there has been increased interest in the potential health benefits of bioactive polypeptides and proteins from soybeans, including lunasin and lectins. Lunasin is a polypeptide that arrests cell division and induces apoptosis in malignant cells. Lectins are glycoproteins that selectively bind carbohydrates; lectins are used in medicine in a variety of new applications. Additional research, including clinical trials, should continue to examine and elucidate the therapeutic effects, nutritional benefits, and toxic consequences of commonly ingested soybean lectins and lunasin.

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Section: Lectins: Structure Binding Speci Cities and Physiologic Efmentioning

confidence: 99%

The Anticarcinogenic Potential of Soybean Lectin and Lunasin

2003

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“…These findings are consistent with the observations of previous lectin studies [6][7][8], except for McMahon et al [9] who found no staining with the lectins directed against fucosylated structures (UEA-1 and LTA), and Loy et al [10], McNeal & Alroy et al [11] and Drachenberg & Papadimitriou [12] who found no staining with DBA. These exceptions can be explained by understanding the possible biochemical pathway of the synthesis of The staining intensity of lectin reaction was graded as, ++++: very strong binding; +++: strong binding; ++: moderate binding; +: weak binding; -: negative staining.…”

Section: Discussionmentioning

confidence: 99%

Glycophenotype of prostatic carcinomas.

Khabaz

McClure

et al. 2011

Folia Histochem Cytobiol.

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Abstract:The factors that affect the progression of prostatic carcinoma are poorly understood, but it is known that carbohydrate antigens on the tumour cell surface play a role in the transforming and metastatic processes. The present report aimed to perform a comparative, lectin-histochemical study of benign and carcinomatous prostates, using a battery of lectins, in combination with monoclonal antibodies against Lewis antigens, and a semi quantitative study, to investigate the changes in glycosylation patterns that occur in prostatic carcinoma. Blocks from 27 necropsy cases of prostatic carcinoma were sectioned and stained with H+E, fifteen biotinylated lectins chosen to probe for a wide range of oligosaccharide sequences within several categories of glycoprotein glycans, using a lectin-biotin avidin-peroxidase method, and monoclonal antibodies against Lewis a , sialyl Lewis a and sialyl Lewis x antigens. The glycophenotype of prostatic carcinoma differed from that of the noncancerous prostate in revealing more intense staining with the following lectins (AAA, UEA-1, DBA, WFA, VVA, HPA, BSA-1 B4 , MPA, ECA, AHA, and CTA), while the binding patterns of (GNA and NPA) were almost similar in both prostatic carcinoma and the noncancerous prostate. Lewis antigens are found to be expressed in prostatic carcinomas but not in the noncancerous prostate. The observations of this study suggest that the gylcophenotype of transformed prostatic cells was modified. It showed a moderate increase in, and changing patterns of, fucosylation and galactosylation, increased branching of side chains and sharp rise in 2 deoxy, 2 acetamido galactosylation and masking process by sialylation, especially by α2-3 and α2-6 linkages. All these changes in the glycosylation pattern of the transformed prostatic cells were observed on O-glycans, no changes were observed on N-glycans.

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“…Namely, SBA and UEA-I showed to be useful indicators of the prostate malignancy, as they distinguished between benign and malignant prostate cells, binding exclusively to dysplasic/carcinoma cells [ 24 , 27 , 28 ], or binding stronger to these cells, comparing to normal/hyperplasic cells binding [ 8 , 26 , 30 ]. However, in some studies SBA could not distinguish the referred cells [ 25 , 26 ]. In addition, the PNA lectin bound stronger to neoplasic cells than to normal and hyperplasic cells [ 8 , 17 , 26 , 27 ].…”

Section: Discussionmentioning

confidence: 99%

A comparative study of recombinant and native frutalin binding to human prostate tissues

et al. 2009

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Background: Numerous studies indicate that cancer cells present an aberrant glycosylation pattern that can be detected by lectin histochemistry. Lectins have shown the ability to recognise these modifications in several carcinomas, namely in the prostate carcinoma, one of the most lethal diseases in man. Thus, the aim of this work was to investigate if the α-D-galactose-binding plant lectin frutalin is able to detect such changes in the referred carcinoma. Frutalin was obtained from different sources namely, its natural source (plant origin) and a recombinant source (Pichia expression system). Finally, the results obtained with the two lectins were compared and their potential use as prostate tumour biomarkers was discussed.

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Binding of soybean agglutinin lectin to prostatic hyperplasia and adenocarcinoma

Cited by 11 publications

References 4 publications

The Anticarcinogenic Potential of Soybean Lectin and Lunasin

The Anticarcinogenic Potential of Soybean Lectin and Lunasin

Glycophenotype of prostatic carcinomas.

A comparative study of recombinant and native frutalin binding to human prostate tissues

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