دورية أكاديمية

Colon carcinoma glycoproteins carrying alpha 2,6-linked sialic acid reactive with Sambucus nigra agglutinin are not constitutively expressed in normal human colon mucosa and are distinct from sialyl-Tn antigen.

التفاصيل البيبلوغرافية
العنوان: Colon carcinoma glycoproteins carrying alpha 2,6-linked sialic acid reactive with Sambucus nigra agglutinin are not constitutively expressed in normal human colon mucosa and are distinct from sialyl-Tn antigen.
المؤلفون: Murayama T; Department of Pathology, University of Zurich, Switzerland., Zuber C, Seelentag WK, Li WP, Kemmner W, Heitz PU, Roth J
المصدر: International journal of cancer [Int J Cancer] 1997 Mar 04; Vol. 70 (5), pp. 575-81.
نوع المنشور: Journal Article; Research Support, Non-U.S. Gov't
اللغة: English
بيانات الدورية: Publisher: Wiley-Liss Country of Publication: United States NLM ID: 0042124 Publication Model: Print Cited Medium: Print ISSN: 0020-7136 (Print) Linking ISSN: 00207136 NLM ISO Abbreviation: Int J Cancer Subsets: MEDLINE
أسماء مطبوعة: Publication: 1995- : New York, NY : Wiley-Liss
Original Publication: 1966-1984 : Genève : International Union Against Cancer
مواضيع طبية MeSH: Plant Lectins*, Carcinoma/*metabolism , Colonic Neoplasms/*metabolism , Glycoproteins/*metabolism , Intestinal Mucosa/*metabolism , Lectins/*metabolism , N-Acetylneuraminic Acid/*metabolism , Neoplasm Proteins/*metabolism , Sialyltransferases/*metabolism, Acetylation ; Antigens, Tumor-Associated, Carbohydrate/metabolism ; Blotting, Northern ; Humans ; Ribosome Inactivating Proteins ; beta-D-Galactoside alpha 2-6-Sialyltransferase
مستخلص: In human colon carcinoma, increased amounts of sialic acids have been found and correlated with tumor progression. Further, the degree of O-acetylation of sialic acid residues in normal mucosa is higher than in colon carcinoma. Thus, tumor-associated sialylated antigens may be constitutively expressed in O-acetylated form in normal mucosa unreactive with the respective monoclonal antibodies. We have earlier demonstrated a colon carcinoma-associated expression of alpha 2,6-linked sialic acid residues with the Sambucus nigra agglutinin (SNA). We report now that de-acetylation of normal and transitional colonic mucosa, in contrast to sialyl-Tn antigen, does not result in SNA binding. Further, the alpha 2,6-linked sialic acid recognized by SNA is distinct from that of sialyl-Tn antigen. This is confirmed by Northern blotting detecting transcripts for alpha 2,6 sialyltransferase of N-glycoproteins and measurement of activity for this sialyltransferase. Blot analysis by SNA of colon carcinoma cells revealed few reactive glycoproteins. Quantitative differences in lectin labeling and sialyltransferase activity were found in HCT116 colon carcinoma cell sub-lines. Our data suggest that SNA binding in human colon carcinoma is due to de novo expression of a specific sialic acid present on selected glycoproteins.
المشرفين على المادة: 0 (Antigens, Tumor-Associated, Carbohydrate)
0 (Glycoproteins)
0 (Lectins)
0 (Neoplasm Proteins)
0 (Plant Lectins)
0 (Sambucus nigra lectins)
0 (sialosyl-Tn antigen)
EC 2.4.99.- (Sialyltransferases)
EC 3.2.2.22 (Ribosome Inactivating Proteins)
GZP2782OP0 (N-Acetylneuraminic Acid)
EC 2.4.99.1 (beta-D-Galactoside alpha 2-6-Sialyltransferase)
تواريخ الأحداث: Date Created: 19970304 Date Completed: 19970320 Latest Revision: 20221207
رمز التحديث: 20240627
DOI: 10.1002/(sici)1097-0215(19970304)70:5<575::aid-ijc14>3.0.co;2-c
PMID: 9052758
قاعدة البيانات: MEDLINE
الوصف
تدمد:0020-7136
DOI:10.1002/(sici)1097-0215(19970304)70:5<575::aid-ijc14>3.0.co;2-c