{"doi":"10.1042/cs0890397","title":"Expression and Regulation of Glycosyltransferases for <i>N</i>-Glycosyl Oligosaccharides in Fresh Human Surgical and Murine Tissues and Cultured Cell Lines","abstract":"<jats:p>1. Mammalian membrane and serum proteins are glycosylated by the addition of heterogeneous N-linked oligosaccharides. It has been widely speculated that oligosaccharide diversity is achieved by corresponding heterogeneity of expression of the glycosyltransferases that are responsible for oligosaccharide synthesis.</jats:p>\n               <jats:p>2. We surveyed mRNA levels of three sequentially acting glycosyltransferases, N-acetylglucosaminyltransferase I, β1,4-galactosyltransferase and α2,6-sialyltransferase, in 11 human tissues and confirmed the expected variations.</jats:p>\n               <jats:p>3. The size heterogeneity of α2,6-sialyltransferase transcripts reported in rat tissues was evident neither in the human tissue survey nor in a panel of murine RNAs. Tissue distributions of alternative terminal sialyltransferases, α2,6-sialyltransferase and α2,3-sialyltransferase, were distinct.</jats:p>\n               <jats:p>4. Relative glycosyltransferase mRNA levels in four transformed human cell lines cultured in vitro did not fully reflect levels in the corresponding human tissues.</jats:p>\n               <jats:p>5. Expression of α2,6-sialyltransferase mRNA was approximately 2.6-fold greater in adenocarcinomatous than in normal human colon, and β1,4-galactosyltransferase expression was approximately 1.8-fold greater in normal than in adenocarcinomatous colon.</jats:p>\n               <jats:p>6. n-Butyrate (0.003–0.005 mol/l), a short-chain fatty acid that is produced by colonic bacterial fermentation, caused approximately 80% inhibition of α2,6-sialyltransferase, approximately 2.5-fold induction of β1,4-galactosyltransferase and approximately 6-fold induction of N-acetylglucosaminyltransferase mRNAs in T84 (colonic) cells. The effects on α2,6-sialyltransferase and β1,4-galactosyltransferase were near maximal by 6 h, but induction of N-acetylglucosaminyltransferase was fully apparent only after exposure for 24 h.</jats:p>","journal":"Clinical Science","year":1995,"id":593076,"datarank":1.6136840346887023,"base_score":3.1354942159291497,"endowment":3.1354942159291497,"self_citation_contribution":0.47032413238937254,"citation_network_contribution":1.1433599022993297,"self_endowment_contribution":0.47032413238937254,"citer_contribution":1.1433599022993297,"corpus_percentile":null,"corpus_rank":null,"citation_count":22,"citer_count":20,"citers_with_citation_signal":19,"citers_with_endowment":19,"datacite_reuse_total":0,"is_dataset":false,"is_dataset_confidence":null,"is_data_producer":false,"deposit_databanks":null,"is_oa":false,"file_count":0,"downloads":0,"has_version_chain":false,"published_date":null,"fair_score":null,"fair_percentile":null,"algorithm_id":"datarank_citation_only_1hop_v6","ranking_scope":"data_only","authors":[{"id":1517861,"name":"V. Andersen","orcid":null,"position":1,"is_corresponding":false},{"id":1517862,"name":"P. Lance","orcid":null,"position":2,"is_corresponding":false},{"id":491259,"name":"M. Li","orcid":null,"position":0,"is_corresponding":false}],"reference_count":0,"raw_metadata":{"has_enrichment":true,"resolved":true,"title":"Expression and Regulation of Glycosyltransferases for <i>N</i>-Glycosyl Oligosaccharides in Fresh Human Surgical and Murine Tissues and Cultured Cell Lines","abstract":"<jats:p>1. Mammalian membrane and serum proteins are glycosylated by the addition of heterogeneous N-linked oligosaccharides. It has been widely speculated that oligosaccharide diversity is achieved by corresponding heterogeneity of expression of the glycosyltransferases that are responsible for oligosaccharide synthesis.</jats:p>\n               <jats:p>2. We surveyed mRNA levels of three sequentially acting glycosyltransferases, N-acetylglucosaminyltransferase I, β1,4-galactosyltransferase and α2,6-sialyltransferase, in 11 human tissues and confirmed the expected variations.</jats:p>\n               <jats:p>3. The size heterogeneity of α2,6-sialyltransferase transcripts reported in rat tissues was evident neither in the human tissue survey nor in a panel of murine RNAs. Tissue distributions of alternative terminal sialyltransferases, α2,6-sialyltransferase and α2,3-sialyltransferase, were distinct.</jats:p>\n               <jats:p>4. Relative glycosyltransferase mRNA levels in four transformed human cell lines cultured in vitro did not fully reflect levels in the corresponding human tissues.</jats:p>\n               <jats:p>5. Expression of α2,6-sialyltransferase mRNA was approximately 2.6-fold greater in adenocarcinomatous than in normal human colon, and β1,4-galactosyltransferase expression was approximately 1.8-fold greater in normal than in adenocarcinomatous colon.</jats:p>\n               <jats:p>6. n-Butyrate (0.003–0.005 mol/l), a short-chain fatty acid that is produced by colonic bacterial fermentation, caused approximately 80% inhibition of α2,6-sialyltransferase, approximately 2.5-fold induction of β1,4-galactosyltransferase and approximately 6-fold induction of N-acetylglucosaminyltransferase mRNAs in T84 (colonic) cells. The effects on α2,6-sialyltransferase and β1,4-galactosyltransferase were near maximal by 6 h, but induction of N-acetylglucosaminyltransferase was fully apparent only after exposure for 24 h.</jats:p>","is_dataset_classified":null,"base_score":3.1354942159291497,"endowment":3.1354942159291497,"datacite_reuse_total":0,"file_count":0,"downloads":0,"views":0,"has_version_chain":false,"is_dataset":false,"is_oa":false,"pmid":"7493440","pmcid":null,"openalex_id":"https://openalex.org/W2422762874","authors":[],"funders":[{"funder_name":"NCI NIH HHS","grant_id":"CA09051","title":null},{"funder_name":"NIDDK NIH HHS","grant_id":"DK43649","title":null}],"total_grants":2,"fwci":0.2685,"citation_percentile":0.54936192,"influential_citations":0,"citation_trend":[],"oa_status":"closed","license":null,"oa_locations":[{"url":"https://portlandpress.com/clinsci/article-pdf/89/4/397/465916/cs0890397.pdf","host_type":"publisher"},{"url":"https://doi.org/10.1042/cs0890397","host_type":"journal"},{"url":"https://pubmed.ncbi.nlm.nih.gov/7493440","host_type":"repository"}],"fields_of_study":["Glycosylation and Glycoproteins Research","Galectins and Cancer Biology","Infant Nutrition and Health","Adenocarcinoma","Animals","Blotting, Northern","Butyrates","Butyric Acid","Colonic Neoplasms","Galactosyltransferases","Gene Expression Regulation, Enzymologic","Glycosyltransferases","Humans","Mice","N-Acetylgalactosaminyltransferases","Oligosaccharides","RNA, Messenger","Sialyltransferases","Tumor Cells, Cultured","beta-D-Galactoside alpha 2-6-Sialyltransferase"],"mesh_terms":["beta-D-Galactoside alpha 2-6-Sialyltransferase","Adenocarcinoma","Animals","Butyrates","Colonic Neoplasms","Galactosyltransferases","Humans","Oligosaccharides","RNA, Messenger","Sialyltransferases","Tumor Cells, Cultured","Blotting, Northern","Gene Expression Regulation, Enzymologic","Glycosyltransferases","N-Acetylgalactosaminyltransferases","Butyric Acid","Mice"],"keywords":["Glycosyltransferase","Galactosyltransferase","Sialyltransferase","Oligosaccharide","Fucosyltransferase","Cell culture","Biology","Biochemistry","Molecular biology","Messenger RNA","Gene","Glycoprotein","Enzyme","Genetics"],"sdg_mappings":[],"linked_datasets":[],"clinical_trials":[],"software_tools":[],"database_accessions":[],"source":"live","citation_network_status":"fetched"},"created_at":"2026-07-26T17:04:59.385925Z","pmid":null,"pmcid":null,"fwci":null,"citation_percentile":null,"influential_citations":0,"oa_status":null,"license":null,"views":0,"total_file_size_bytes":0,"version_count":0,"fair_f":null,"fair_a":null,"fair_i":null,"fair_r":null,"fair_zscore":null,"fair_rationale":null,"fair_model":null,"fair_agent_version":null,"fair_fulltext_source":null,"fair_has_llm":null,"fair_computed_at":null,"clinical_trials":[],"software_tools":[],"db_accessions":[],"linked_datasets":[],"topics":[]}