Otolaryngology · 1989 · 11 citations · 7 references
Life SciencesCell BiologyOncologyGlycobiologyNeoplasiaTumor ImmunologyCell-surface GlycansGlycan-protein InteractionsLaryngeal CancerSquamous Cell CarcinomaTumor AntigensTumor-associated AntigensBlood Group Antigen StructureGlycoprotein StructureLectin Binding SpecificityLectin-carbohydrate InteractionsLectin-carbohydrate RecognitionLectin-glycan Interactions In CancerLectin-glycan RecognitionLectins
Previous reports have shown specific binding characteristics of peanut lectin to a variety of lymphatic and epithelial tumors. This study demonstrates the presence of lectin binding sites on cell membrane of laryngeal cancer cells, but not on adjacent normal epithelial linings. It also demonstrates the presence of glycoconjugates responsible for lectin adherence in fetal larynges. The Thomsen-Friedenreich antigen is a glycoprotein structure participating in the structure of the MN blood group antigen. It is also the structure that binds the peanut agglutinin. Perhaps this antigen, which we found on fetal larynges as well as on malignant laryngeal epithelial lining, is another oncodevelopmental antigen.
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β1-6 Branching of Asn-Linked Oligosaccharides Is Directly Associated with Metastasis
James W. Dennis, Suzanne Laferté, Carol Waghorne et al. · Science · 1987 · 940 citations
L. E. Glynn · BMJ · 1977 · 743 citations
Precursors of the Blood Group MN Antigens as Human Carcinoma‐Associated Antigens
Georg F. Springer, P. R. Desai, M. Satya Murthy et al. · Transfusion · 1979 · 62 citations
Life Sciences, Immunology, Oncology +14
Peanut lectin binding sites in human fetal colon.
R. A. Coapman, Harry S. Cooper · PubMed · 1986 · 29 citations