ArticleThe Journal of biological chemistry2014
Determination of carbohydrate structure recognized by prostate-specific F77 monoclonal antibody through expression analysis of glycosyltransferase genes.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 38 citations in OpenAlex.
- F77 antigen is a promising target for adoptive T cell therapy of prostate cancer.Biochemical and biophysical research communications · 2023Article
- Expression of placental glycans and its role in regulating peripheral blood NK cells during preeclampsia: a perspective.Frontiers in endocrinology · 2023Review
- The Role of Hypoxia-Inducible Factor Post-Translational Modifications in Regulating Its Localisation, Stability, and Activity.International journal of molecular sciences · 2020Review
- Role of glycosylation in hypoxia-driven cell migration and invasion.Cell adhesion & migration · 2019Review
- Glycans as Biomarkers in Prostate Cancer.International journal of molecular sciences · 2019Review
- Glycan Microarrays as Chemical Tools for Identifying Glycan Recognition by Immune Proteins.Frontiers in chemistry · 2019Review
- A spliced form of CD44 expresses the unique glycan that is recognized by the prostate cancer specific antibody F77.Oncotarget · 2018Article
- Liquid Biopsy in the OMICS Era of Tumor Medicine.Open access journal of biomedical engineering and its applications · 2018Article
- Shotgun Glycomics Identifies Tumor-Associated Glycan Ligands Bound by an Ovarian Carcinoma-Specific Monoclonal Antibody.Scientific reports · 2017Article
- Characterization of H type 1 and type 1The Journal of biological chemistry · 2017Article
- Unraveling Sugar Chain Signatures of the "Seeds" of Tumor Metastasis.Journal of proteomics & bioinformatics · 2017Article
- Glycan Markers as Potential Immunological Targets in Circulating Tumor Cells.Advances in experimental medicine and biology · 2017Review
- MALDI Mass Spectrometry Imaging of N-Linked Glycans in Cancer Tissues.Advances in cancer research · 2017Review
- Immunization with Outer Membrane Vesicles Displaying Designer Glycotopes Yields Class-Switched, Glycan-Specific Antibodies.Cell chemical biology · 2016Article
- The role of glycans in the development and progression of prostate cancer.Nature reviews. Urology · 2016Review
- I-branching N-acetylglucosaminyltransferase regulates prostate cancer invasiveness by enhancing α5β1 integrin signaling.Cancer science · 2016Article
- Carbohydrate Microarrays Identify Blood Group Precursor Cryptic Epitopes as Potential Immunological Targets of Breast Cancer.Journal of immunology research · 2015Article
- The detection and discovery of glycan motifs in biological samples using lectins and antibodies: new methods and opportunities.Advances in cancer research · 2015Review
- Carbohydrate sequence of the prostate cancer-associated antigen F77 assigned by a mucin O-glycome designer array.The Journal of biological chemistry · 2014Article
Corrections and comments
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Authors and funding
9 authors at 3 institutions in 2 countries.
Funding
Abstract
This study reports the determination of the carbohydrate epitope of monoclonal antibody F77 previously raised against human prostate cancer PC-3 cells (Zhang, G., Zhang, H., Wang, Q., Lal, P., Carroll, A. M., de la Llera-Moya, M., Xu, X., and Greene, M. I. (2010) Proc. Natl. Acad. Sci. U. S. A. 107, 732-737). We performed a series of co-transfections using mammalian expression vectors encoding specific glycosyltransferases. We thereby identified branching enzymes and FUT1 (required for Fucα1→2Gal linkage) as being essential for F77 antigen formation. When immortalized normal prostate 267B1 cells were transfected with FUT1 alone, cells showed weak expression of F77 antigen. By contrast, cells co-transfected with FUT1 plus either GCNT1, GCNT2, or GCNT3 (an enzyme required to form GlcNAcβ1→6Gal/GalNAc) showed robust F77 antigen expression, suggesting that F77 specifically binds to Fucα1→2Galβ1→4GlcNAcβ1→6Gal/GalNAc. RT-PCR for FUT1, GCNT1, GCNT2, and GCNT3 showed that F77-positive cell lines indeed express transcripts encoding FUT1 plus one GCNT. F77-positive prostate cancer cells transfected with siRNAs targeting FUT1, GCNT2, and GCNT3 showed significantly reduced F77 antigen, confirming the requirement of these enzymes for epitope synthesis. We also found that hypoxia induces F77 epitope expression in immortalized prostate RWPE1 cells, which express F77 antigen moderately under normoxia but at an elevated level under hypoxia. Quantitative RT-PCR demonstrated up-regulation of FUT1, GCNT2, and GCNT3 transcripts in RWPE1 cells under hypoxia, suggesting that hypoxia up-regulates glycosyltransferase expression required for F77 antigen synthesis. These results define the F77 epitope and provide a potential mechanism for F77 antigen synthesis in malignant prostate cancer.
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