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Title:
Tumor-Associated Carbohydrate Antigens Defining Tumor Malignancy: Basis for Development of Anti-Cancer Vaccines | SpringerLink
Description:
Tumors expressing a high level of certain types of tumor-associated carbohydrate antigens (T ACAs) exhibit greater metastasis and progression than those expressing low level of TACAs, as reflected in decreased patient survival rate. Well-documented examples of such...
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a-n-acetylgalactosamine-o-serine/ threonine sialylated lacto-n-fucopentaose iij n-acetylneuraminosyl a2→6galactosyl residue glycosphingolipid-glycosphingolipid interaction [abstract]glycoconj antibody-targeted interleukin-2cancer immunol sialosyl long-chain poly-lacnac bec2-keyhole limpet hemocyanin 0-linked sialosyl-2→6 a-n-acetylgalactosaminyl fucal-2galß1→4[fucal-→3]glenac ortho-signaling therapycancer cells3 month download article/chapter ganglioside-klh conjugate vaccinesimmunol small-cell lung cancern monoclonal antibodies ncc-lu-35 low-dose intravenous cyclophosphamidej monoclonal antibody acfh-18j gm3-enriched microdomain involved cross-reacting epitope defined idiotypic anti-carbohydrate antibodies sialyl-tn epitopes correlate physiological e-selectin epitopebiochem sialosyl-fucosyl poly-lacnac e-selectin binding fractions g1cnacβ1–6mana1–6manβ-6 branching elam-1-dependent cell adhesion human blood-group mn tetrasialylpoly-n-acetyllactosaminyl gangliosides sialyl tn-klh conjugate e-selectin-dependent adhesion elicits immune responses programmed cell death concanavalin a-binding peptides monoclonal antibody-defined antigen p-selectin-dependent adhesion induce e-selectin expression n-acetylgalactosamine-a2 gm3-expressing cells based induces enhanced activity n-acetylgalactosaminyl epitope human colonic carcinomaglycoconj phage peptide library privacy choices/manage cookies random peptide libraries medicine chang-gung university glycosphingolipid-glycosphingolipid interaction monoclonal antibody specific syngeneic monoclonal antibody ganglioside gd1a functions histo-blood group cell-surface antigen

Schema {🗺️}

ScholarlyArticle:
      headline:Tumor-Associated Carbohydrate Antigens Defining Tumor Malignancy: Basis for Development of Anti-Cancer Vaccines
      pageEnd:402
      pageStart:369
      image:https://media.springernature.com/w153/springer-static/cover/book/978-1-4615-1267-7.jpg
      genre:
         Biomedical and Life Sciences
         Biomedical and Life Sciences (R0)
      isPartOf:
         name:The Molecular Immunology of Complex Carbohydrates —2
         isbn:
            978-1-4615-1267-7
            978-1-4613-5469-7
         type:Book
      publisher:
         name:Springer US
         logo:
            url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
            type:ImageObject
         type:Organization
      author:
            name:Sen-itiroh Hakomori
            affiliation:
                  name:Pacific Northwest Research Institute and University of Washington
                  address:
                     name:Pacific Northwest Research Institute and University of Washington, Seattle, USA
                     type:PostalAddress
                  type:Organization
            type:Person
      keywords:Keyhole Limpet Hemocyanin, Primary Lung Carcinoma, Anticancer Vaccine, Dynamic Flow Condition, Phage Display Random Peptide Library
      description:Tumors expressing a high level of certain types of tumor-associated carbohydrate antigens (T ACAs) exhibit greater metastasis and progression than those expressing low level of TACAs, as reflected in decreased patient survival rate. Well-documented examples of such TACAs are: (i) H/Ley/ILea in primary non-small cell lung carcinoma; (ii) sialyl-Lex(SLex) and sialyl-Lea (SLea) in various types of cancer; (iii) Tn and sialyl-Tn in colorectal, lung, breast, and many other cancers; (iv) GM2, GD2, and GD3 gangliosides in neuroectodermal tumors (melanoma and neuroblastoma); (v) globo-H in breast, ovarian, and prostate cancer; (vi) disialylgalactosylgloboside in renal cell carcinoma. Some glycosylations and TACAs suppress invasiveness and metastatic potential. Welldocumented examples are: (i) blood group A antigen in primary lung carcinoma; (ii) bisecting β1 →4G1cNAc ofN-linked structure in melanoma and other cancers; (iii) galactosylgloboside (GaIGb4) in seminoma. The biochemical mechanisms by which the above glycosylation changes promote or suppress tumor metastasis and invasion are mostly unknown. A few exceptional cases in which we have some knowledge are: (i) SLex and SLea function as E-selectin epitopes promoting tumor cell interaction with endothelial cells; (ii) some tumor cells interact through binding ofTACA to specific proteins other than selectin, or to specific carbohydrate expressed on endothelial cells or other target cells (carbohydrate-carbohydrate interaction); (iii) functional modification of adhesive receptor (integrin, cadherin, CD44) by glycosylation. So far, a few successful cases of anti-cancer vaccine in clinical trials have been reported, employing T ACAs whose expression enhances malignancy. Examples are STn for suppression of breast cancer, GM2 and GD3 for melanoma, and globo-H for prostate cancer. Vaccine development can be extended using other T ACAs, with the following criteria for success: (i) the antigen is expressed highly on tumor cells; (ii) high antibody production depending on two factors: (a) clustering of antigen used in vaccine; (b) choice of appropriate carrier protein or lipid; (iii) high T cell response depending on choice of appropriate carrier protein or lipid; (iv) expression of the same antigen in normal epithelial tissues (e.g., renal, intestinal, colorectal) may not pose a major obstacle, i.e., these tissues are not damaged during immune response. Idiotypic anti-carbohydrate antibodies that mimic the surface profile of carbohydrate antigens, when administered to patients, elicit anti-carbohydrate antibody response, thus providing an effect similar to that of T ACAs for suppression of tumor progression. An extension of this idea is the use of peptide mimetics ofTACAs, based on phage display random peptide library. Although examples are so far highly limited, use of such “mimotopes” as immunogens may overcome the weak immunogenicity ofTACAs in general.
      datePublished:2001
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Book:
      name:The Molecular Immunology of Complex Carbohydrates —2
      isbn:
         978-1-4615-1267-7
         978-1-4613-5469-7
Organization:
      name:Springer US
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         url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
         type:ImageObject
      name:Pacific Northwest Research Institute and University of Washington
      address:
         name:Pacific Northwest Research Institute and University of Washington, Seattle, USA
         type:PostalAddress
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Person:
      name:Sen-itiroh Hakomori
      affiliation:
            name:Pacific Northwest Research Institute and University of Washington
            address:
               name:Pacific Northwest Research Institute and University of Washington, Seattle, USA
               type:PostalAddress
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PostalAddress:
      name:Pacific Northwest Research Institute and University of Washington, Seattle, USA
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