Ultrastructural localization of binding sites for PNA and VVA-B4 lectins in human breast cancer cell lines detected by confocal fluorescence microscopy

Końska, Grażyna; Vissac, Cécile; Zagla, K; Chezet, F; Vasson, M.-P.; Bernard‐Gallon, Dominique; Guillot, Jean

doi:10.3892/ijo.21.5.1009

Cited by 5 publications

(7 citation statements)

References 0 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…[19] It has been used for over 20 years to monitor the expression of the Tn antigen. [12,13,20,[54][55][56][57] Based on 1) selective staining of carcinoma tissues, 2) excellent discrimination between the Tn antigen and the blood group A antigen, 3) a crystal structure, and 4) specificity studies with a limited number of glycopeptides and monosaccharides, VVL-B4 was thought to be highly selective for the Tn antigen. [19,[58][59][60][61][62] Binding to carbohydrates on the array was evaluated by using the optimized conditions described above.…”

Section: Carbohydrate Array Analysis Of Vvl-b4 Bric111 and Hbtn1mentioning

confidence: 99%

Carbohydrate Array Analysis of Anti‐Tn Antibodies and Lectins Reveals Unexpected Specificities: Implications for Diagnostic and Vaccine Development

Manimala

Jain³

et al. 2005

ChemBioChem

103

View full text Add to dashboard Cite

The Tn antigen is a carbohydrate antigen expressed in most carcinomas, during embryogenesis, on pathogenic parasites, and on HIV. It has been evaluated extensively as a potential diagnostic marker and several Tn-based vaccines are in clinical trials. Based on discrepancies in the literature regarding Tn expression, we began to question whether antibodies and lectins used routinely to detect the Tn antigen were providing accurate information. To investigate this possibility, a carbohydrate microarray and a highly sensitive assay were developed and three frequently used Tn receptors (HBTn1, Bric111, and VVL-B4) were evaluated. Carbohydrate-array analysis revealed unexpected cross-reactivity with other human carbohydrate epitopes. VVL-B4 bound the Tn antigen, GalNAcalpha1-6Gal, and GalNAcalpha1-3Gal. Bric111 bound the Tn antigen, blood group A, GalNAcalpha1-6Gal, and GalNAcalpha1-3Gal. HBTn1 showed the best selectivity, but still displayed moderate binding to blood group A. Implications for the development of Tn-based diagnostics and vaccines are discussed.

show abstract

Section: Carbohydrate Array Analysis Of Vvl-b4 Bric111 and Hbtn1mentioning

confidence: 99%

Carbohydrate Array Analysis of Anti‐Tn Antibodies and Lectins Reveals Unexpected Specificities: Implications for Diagnostic and Vaccine Development

Manimala

Jain³

et al. 2005

ChemBioChem

103

View full text Add to dashboard Cite

show abstract

“…Therefore, VVA has already been used to distinguish between T antigen and Tn antigen [33]. The O-glycan of rHuEPO consists of Gal(b-1,4)GalNAc-Ser (T antigen) bearing one or two sialic acid residues.…”

Section: Vva Bindingmentioning

confidence: 99%

Detection of isoforms of recombinant human erythropoietin by various plant lectins after isoelectric focusing

et al. 2005

View full text Add to dashboard Cite

A screening method to determine the binding behavior of lectins toward recombinant human erythropoietin (rHuEPO) was developed. Twenty-three different lectins were tested for this purpose. rHuEPO isoforms were separated by isoelectric focusing using the International Olympic Committee (IOC) and World Anti-Doping Agency (WADA) accredited method for the direct detection of the prohibited doping substance erythropoietin (EPO). For the visualization of the rHuEPO isoforms lectins were used instead of antibodies. Optimization of the screening protocol enabled the detection of a maximum number of rHuEPO isoforms. By means of this protocol information about the binding properties of a lectin toward each individual rHuEPO isoform was accessible. All evaluated lectins showed significant differences in their binding behavior. The most intense response was obtained with WGA, DSL, PHA-E, LEL, PSA, and LCA. While WGA, DSL, PHA-E, and LEL were able to bind all isoforms detected by the standard antibody, LCA and PSA demonstrated a clear preference for rHuEPO isoforms located in the more basic region of the electropherogram. Further lectins tested were ConA, succWGA, PHA-L, RCA, SNA, MAA, STL, ECL, GSL-II, SJA, SBA, UEA-I, Jacalin, PNA, DBA, GSL-I, and VVA. Compared to the lectins mentioned above, they showed reduced sensitivity. Endogenous and recombinant EPO only differ in the composition of their N- and O-glycan moieties. As lectins possess the unique ability to recognize subtle differences in glycan substructures, they represent an interesting approach for their structural characterization. Furthermore, they might be useful for affinity enrichment/purification of rHuEPO in doping control.

show abstract

“…20 Targeting with mannose moieties doubled the PDT cytotoxicity of the silica nanoparticles in vitro and allowed for effective HCT-116 tumour reduction following in vivo PDT of a subcutaneous mouse model. Conversely, exogenous lectins, such as wheat germ agglutinin 21 and peanut agglutinin 22 have also been used for the targeting of cell surface carbohydrates that exhibit expression patterns that are associated with malignancy.…”

Section: Introductionmentioning

confidence: 99%

Cancer targeting with biomolecules: a comparative study of photodynamic therapy efficacy using antibody or lectin conjugated phthalocyanine-PEG gold nanoparticles

Obaid

Chambrier

Cook

et al. 2015

Photochem Photobiol Sci

125

View full text Add to dashboard Cite

The functionalisation of therapeutic nanoparticle constructs with cancer-specific biomolecules can enable selective tumour accumulation and targeted treatment. Water soluble gold nanoparticles (ca. 4 nm) stabilised by a mixed monolayer of a hydrophobic zinc phthalocyanine photosensitiser (C11Pc) and hydrophilic polyethylene glycol (PEG) have been prepared. The C11Pc-PEG gold nanoparticle constructs were further functionalised with jacalin, a lectin specific for the cancer-associated Thomsen-Friedenreich (T) carbohydrate antigen, or with monoclonal antibodies specific for the human epidermal growth factor receptor-2 (HER-2). The two biofunctionalised nanoparticle conjugates produced similar levels of singlet oxygen upon irradiation at 633 nm. Importantly, both nanoparticle conjugates demonstrated extensive, yet comparable, phototoxicity in HT-29 colorectal adenocarcinoma cells (80-90%) and in SK-BR-3 breast adenocarcinoma cells (>99%). Non-conjugated C11Pc-PEG gold nanoparticles were only minimally phototoxic. Lysosomal colocalisation studies performed with the HT-29 colon cancer cells and the SK-BR-3 breast cancer cells revealed that both nanoparticle conjugates were partially localised within acidic organelles, which is typical of receptor-mediated endocytosis. The similarity of the targeted PDT efficacy of the two biofunctionalised C11Pc-PEG gold nanoparticles is discussed with respect to targeting ligand binding affinity and cell surface antigen density as key determinants of targeting efficiency. This study highlights how targeting small cell-surface molecules, such as the T antigen, can mediate a selective photodynamic treatment response 2 which is similar to that achieved when targeting overexpressed protein receptors, such as HER-2. The high prevalence of the T antigen present on the cellular surface of primary tumours emphasises the broad potential applications for lectin-targeted therapies.

show abstract

Ultrastructural localization of binding sites for PNA and VVA-B4 lectins in human breast cancer cell lines detected by confocal fluorescence microscopy

Cited by 5 publications

References 0 publications

Carbohydrate Array Analysis of Anti‐Tn Antibodies and Lectins Reveals Unexpected Specificities: Implications for Diagnostic and Vaccine Development

Carbohydrate Array Analysis of Anti‐Tn Antibodies and Lectins Reveals Unexpected Specificities: Implications for Diagnostic and Vaccine Development

Detection of isoforms of recombinant human erythropoietin by various plant lectins after isoelectric focusing

Cancer targeting with biomolecules: a comparative study of photodynamic therapy efficacy using antibody or lectin conjugated phthalocyanine-PEG gold nanoparticles

Contact Info

Product

Resources

About