Immunochemical studies on the specificity of the peanut (Arachis hypogaea) Agglutinin

Pereira, M. E. A.; Kabat, Elvin A.; Lotan, Reuben; Sharon, Nathan

doi:10.1016/s0008-6215(00)84040-9

Cited by 272 publications

(95 citation statements)

References 34 publications

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“…THE LECTIN derived from the seeds of the peanut plant Arachis hypogaea (peanut lectin, PNL) binds to single terminal galactose residues, but more avidly to the disaccharide D-galactose 3' 1-3 D-N, acetylgalactosamine (Pereira et al, 1976). This sugar is part of the oligo-saccharide array on cell surfaces, but it is commonly covered by sialic acid.…”

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confidence: 99%

Binding of peanut lectin to germinal-centre cells: A marker for B-cell subsets of follicular lymphoma?

Rose¹,

Habeshaw²,

Kennedy³

et al. 1981

Br J Cancer

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The binding of horseradish-peroxidase-labelled peanut lectin (HRP-PNL) to cryostat sections of tonsil, lymphoma lymph nodes, reactive lymph nodes and miscellaneous tumours demonstrated that PNL binds selectively to lymphocytes in germinal centres. Lymph nodes from 21 patients with non-Hodgkin's lymphomas were phenotyped as cell suspensions for PNL binding, and the following surface markers: E rosetting, C3d, SIg, OK markers of T-cell subsets, Ig heavy-chain and light-chain classes. There was a positive correlation between PNL binding and cells with SIg and C3d receptors. 4/5 cases of centroblastic/centrocytic follicular lymphoma had a PNL+ SIg+ C3d+ phenotype. Both cases of centroblastic/centrocytic diffuse lymphoma were PNL-. There was no correlation between PNL binding and heavy- or light-chain Ig class. PNL binding and presence of C3d receptors were not always positively correlated, indicating that follicular cells may be either PNL+ SIg+ C3d+ or PNL+ SIg+ C3d-. The binding pattern of PNL to 1 case of thymic hyperplasia and 2 cases of malignant lymphoma lymphoblastic T type suggested that some but not all cortical thymocytes bind PNL. Images Fig. 1 Fig. 2

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mentioning

confidence: 99%

Binding of peanut lectin to germinal-centre cells: A marker for B-cell subsets of follicular lymphoma?

Rose¹,

Habeshaw²,

Kennedy³

et al. 1981

Br J Cancer

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“…The carbohydrate binding site of peanut agglutinin (PNA) is most complementary to the sequence galactose f1-3-Nactylgalactosamine (Pereira et al, 1976), the immunodeterminant structure of T-antigen, which is commonly expressed in many human carcinomas but not in normal tissue where it is covered by sialic acid residues (Coon & Weinstein, 1984;Springer, 1984). According to Pereira et al, (1976) PNA also demonstrates specificity to a lesser degree for other terminal, nonreducing galactosyl-containing oligosaccharides, particularly for the structure galactose f1-4-Nacetylglucosamine, galactose ,B1-3-N-acetylglucosamine and galactose.…”

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confidence: 99%

“…According to Pereira et al, (1976) PNA also demonstrates specificity to a lesser degree for other terminal, nonreducing galactosyl-containing oligosaccharides, particularly for the structure galactose f1-4-Nacetylglucosamine, galactose ,B1-3-N-acetylglucosamine and galactose.…”

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confidence: 99%

Identification of glycoproteins expressing tumour-associated PNA-binding sites in colorectal carcinomas by SDS-GEL electrophoresis and PNA-labelling

Kellokumpu¹,

Kellokumpu²,

Andersson³

1987

Br J Cancer

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Summary Many tumour-specific antigens in gastrointestinal cancers have carbohydrate immunodeterminants. These epitopes can be identified by lectins and monoclonal antibodies. By using fluoresceinisothiocyanate (FITC)-conjugated peanut agglutinin (PNA) and sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) we have investigated glycoproteins carrying altered carbohydrate epitopes in normal and carcinomatous human colorectal mucosa.In normal mucosa PNA stained goblet cell glycoconjugates in the supranuclear (Golgi) distribution. After neuraminidase pretreatment PNA stained actual mucin goblet itself at all levels of the crypts. Colorectal carcinomas displayed a strong and direct binding of PNA to apical cell membranes of carcinomatous cells and intraluminal secretions.Analysis of the glycoproteins by SDS-PAGE and PNA-labelling revealed four carcinoma-associated glycoproteins (26kD, 32kD, 35kD and 5OkD). In addition, four glycoproteins (29kD, 3OkD, 33kD and 36kD) common to normal and carcinomatous colorectal mucosa could be identified. All of these glycoproteins differed in their molecular weight from those in red cell controls which bind PNA only after desialylation.The study shows that the expression of PNA-binding sites in colorectal carcinomas signifies a cancerassociated carbohydrate alteration. Four carcinoma-associated glycoprotein antigens could be detected by this lectin. The antigens we have identified might be useful in the isolation and purification of more selective reagents for the serologic detection of colorectal cancer.

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“…This approach enables a resolution of glycoconjugate mixtures dependent on carbohydrate composition rather than on physical properties such as size and net electric charge. Lectins can be sub-categorised into those which bind 0-glycosidically or N-glycosidically linked carbohydrate chains, a-linked or /?-linked sugar residues, and non-reducing terminal or internally positioned saccharides [4] while certain lectins combine with oligosaccharides better than with monosaccharides [5].One particularly interesting lectin is the peanut agglutinin [6,7] which has a reported high affinity for a-linked and P-linked non-reducing terminal galactose and in particular for the disaccharide galactosyl-~-(l-3)-N-acetylgalactosamine, Gal(P1-3)GalNAc [8,9]. The 0-glycosidically linked derivative of this disaccharide is present in a number of membrane glycoproteins where it is normally found in the cryptic form substituted by one or two sialic acid moieties [lo].…”

mentioning

confidence: 99%

“…One particularly interesting lectin is the peanut agglutinin [6,7] which has a reported high affinity for a-linked and P-linked non-reducing terminal galactose and in particular for the disaccharide galactosyl-~-(l-3)-N-acetylgalactosamine, Gal(P1-3)GalNAc [8,9]. The 0-glycosidically linked derivative of this disaccharide is present in a number of membrane glycoproteins where it is normally found in the cryptic form substituted by one or two sialic acid moieties [lo].…”

mentioning

confidence: 99%

Glycoproteins Containing Peanu t‐Agglutinin Receptors from Human‐Peripheral‐ Blood T‐Lymphocyte Plasma Membranes

Farrar

Holz

Uhlenbruck

1981

European Journal of Biochemistry

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A glycoprotein fraction possessing peanut agglutinin receptors has been isolated from detergent extracts of neuraminidase-treated human peripheral blood T-lymphocyte plasma membranes with affinity matrices comprising the peanut agglutinin co-valently immobilised on Sepharose 4B.This fraction could be specifically eluted from affinity columns using buffer solutions supplemented with 0.2 M D-galactose and was shown, by polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulphate (0.1 %), to contain four major glycoprotein components with apparent molecular weights of 200000,190000, 110000 and 95000.It is suggested, from the observed reactivity of these glycoproteins with various lectins in double-diffusion experiments, that they possess both 0-glycosidically and N-glycosidically linked carbohydrates.It is now generally accepted that the glycoproteins of eucariotic cell plasma membranes are fundamentally involved in many membrane-mediated activities [I, 21. However, despite the fact that numerous glycoproteins have been identified from the many membranes studied, very few have been isolated in sufficient amounts to allow biochemical analysis.Affinity chromatography utilising the saccharide binding specificity of lectins has in recent years been increasingly applied to the isolation of membrane glycoproteins [3]. This approach enables a resolution of glycoconjugate mixtures dependent on carbohydrate composition rather than on physical properties such as size and net electric charge. Lectins can be sub-categorised into those which bind 0-glycosidically or N-glycosidically linked carbohydrate chains, a-linked or /?-linked sugar residues, and non-reducing terminal or internally positioned saccharides [4] while certain lectins combine with oligosaccharides better than with monosaccharides [5].One particularly interesting lectin is the peanut agglutinin [6,7] which has a reported high affinity for a-linked and P-linked non-reducing terminal galactose and in particular for the disaccharide galactosyl-~-(l-3)-N-acetylgalactosamine, Gal(P1-3)GalNAc [8,9]. The 0-glycosidically linked derivative of this disaccharide is present in a number of membrane glycoproteins where it is normally found in the cryptic form substituted by one or two sialic acid moieties [lo]. Using immobilised peanut agglutinin, Carter and Sharon [l I] isolated the glycoproteins that contained receptors for this lectin from solubilised, neuraminidase-treated human erythrocyte ghosts. These affinity-isolated molecules represented a discrete subgroup of the total membrane glycoprotein population which, like those from the bovine and porcine erythrocyte membranes, were subsequently shown to represent a major source of the protein-bound Gal(p1-3)GalNAc in these niembranes [12].We now describe the isolation, by affinity chromatography, of the glycoproteins containing peanut agglutinin Enzyme. Neuraminidase from Vibrio cholerae (EC 3.2.1.18).receptors from neuraminidase-treated human peripheral blood T-lymphocyte plasma membranes. MATERIALS AND ...

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Immunochemical studies on the specificity of the peanut (Arachis hypogaea) Agglutinin

Cited by 272 publications

References 34 publications

Binding of peanut lectin to germinal-centre cells: A marker for B-cell subsets of follicular lymphoma?

Binding of peanut lectin to germinal-centre cells: A marker for B-cell subsets of follicular lymphoma?

Identification of glycoproteins expressing tumour-associated PNA-binding sites in colorectal carcinomas by SDS-GEL electrophoresis and PNA-labelling

Glycoproteins Containing Peanu t‐Agglutinin Receptors from Human‐Peripheral‐ Blood T‐Lymphocyte Plasma Membranes

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