Identification of peanut agglutinin receptors related to the state of tumoral liver cell differentiation

Goulut-Chassaing, Chantal; Decastel, Monique; Tran, Alexis T.; Tabary, F.; Bourrillon, R

doi:10.1016/0300-9084(92)90189-l

Cited by 6 publications

(1 citation statement)

References 36 publications

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“…This could involve displacement of the loop away from the GlcNAc ring of LacNAc, facilitated by the conformational flexibility of two consecutive glycines after Leu-212 with the consequent restructuring of the hydrogen bonds. The possible sacrifice of the interaction between the backbone amide of Gly-213 and the 3Ј-OH in the process could in effect or partly explain the observed lower affinity of PNA for LacNAc in comparison with that for Lac (34). The additional hydrophobic stabilization that might accrue due to interactions between the acetamido group and the leucyl side chain might not be large enough to compensate for the disruption referred to above.…”

Section: Resultsmentioning

confidence: 99%

Imparting Exquisite Specificity to Peanut Agglutinin for the Tumor-associated Thomsen-Friedenreich Antigen by Redesign of Its Combining Site

Sharma

Vijayan

Surolia

1996

Journal of Biological Chemistry

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Lectins from legumes constitute one of the most thoroughly studied families of proteins, yet the absence of a rigorous framework to explain their carbohydrate binding specificities appears to have prevented a rational approach to alter their ligand binding activity. Studies reported here deal with the redesign of the recognition propensity of peanut agglutinin (PNA), an important member of the family. PNA is extensively used as a tool for recognition of the tumor-associated Thomsen-Friedenrich antigen (T-antigen; Galbeta1-3GalNAc) on the surfaces of malignant cells and immature thymocytes. PNA also recognizes N-acetyllactosamine (LacNAc; Galbeta1-4GlcNAc), which is present at the termini of several cell-surface glycoproteins. The crystal structure of the PNA-lactose complex revealed, in addition to the expected interactions with the residues constituting the binding site, the presence of leucine 212 at a position close enough to be in steric contact with the acetamido group on LacNAc. We report here two leucine mutants, one to asparagine (L212N) and the other to alanine (L212A), that exhibit distinct preference for T-antigen and N-acetyllactosamine, respectively. Carbohydrate binding studies reveal that mutant L212N does not recognize LacNAc at high concentrations, thus making it an exquisitely specific cell-surface marker compared with its wild-type counterpart.

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Section: Resultsmentioning

confidence: 99%

Imparting Exquisite Specificity to Peanut Agglutinin for the Tumor-associated Thomsen-Friedenreich Antigen by Redesign of Its Combining Site

Sharma

Vijayan

Surolia

1996

Journal of Biological Chemistry

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Differential reactivities of the Arachis hypogaea (peanut) and Vicia villosa B4 lectins with human ovarian carcinoma cells, grown either in vitro or in vivo xenograft model

Avichezer

Arnon

1996

FEBS Letters

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PNA and VVA B4 recognize the tumor-associated T antigen and its immediate precursor Tn, respectively. We found have been identified in the cancer-associated mucin (MUC-1 that both lectins are highly reactive in vitro, with human ovarian gene product) antigen, which is a unique high molecular carcinoma cell lines, but only VVA B4 bound significantly to weight surface glycoprotein, overexpressed in more than breast and oral cancer cells. This binding is inhibited by specific 90% of the human ovarian cancers and in the large majority monosaccharides. The lectin binding receptors were purified, of breast carcinomas types [5]. revealing a glycoprotein of 32 kDa for PNA, and twoWe have previously shown that monoclonal (rodent)and glycoproteins of 35 and 38 kDa for VVA B4. In vivo localization polyclonal (human) anti-T and -Tn antibodies are reactive of PNA was almost exclusive (except for the kidneys) to the with the human ovarian IGROV-1, OVCAR-3 and SKOV-3 ovarian tumor xenografts. VVA B4 showed wider tissue carcinoma cells and accumulate in vivo, in ovarian carcinobiodistribution being preferentially accumulated in the tumors and ovaries, mas xenografted in nude mice [6]. In vitro, the monoclonal anti-T/Tn antibodies are cytotoxic to the ovarian cancer cells

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Expression of beta 1-6-branched N-linked oligosaccharides is associated with activation in human T4 and T8 cell populations.

Lemaire¹,

Derappe²,

Michalski³

et al. 1994

Journal of Biological Chemistry

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Identification of peanut agglutinin receptors related to the state of tumoral liver cell differentiation

Cited by 6 publications

References 36 publications

Imparting Exquisite Specificity to Peanut Agglutinin for the Tumor-associated Thomsen-Friedenreich Antigen by Redesign of Its Combining Site

Imparting Exquisite Specificity to Peanut Agglutinin for the Tumor-associated Thomsen-Friedenreich Antigen by Redesign of Its Combining Site

Differential reactivities of the Arachis hypogaea (peanut) and Vicia villosa B4 lectins with human ovarian carcinoma cells, grown either in vitro or in vivo xenograft model

Expression of beta 1-6-branched N-linked oligosaccharides is associated with activation in human T4 and T8 cell populations.

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