Literature DB >> 10330278

Identification of an alpha2,6-sialyltransferase induced early after lymphocyte activation.

M Kaufmann1, C Blaser, S Takashima, R Schwartz-Albiez, S Tsuji, H Pircher.   

Abstract

We have used mRNA differential display PCR to search for genes induced in activated T cells and we identified a gene encoding an alpha2,6-sialyltransferase (ST6GalNAc IV) that is rapidly induced in lymphocytes after antigen or mitogen stimulation. The 3.6 kb full-length cDNA clone (MK45) obtained contained a single open reading frame encoding a 302 amino acid protein and a 2.5 kb 3' untranslated region. MK45 expression in in vivo-activated CD8 T cells reached the highest level 4 h after antigen triggering and then declined rapidly to nearly base levels within 45 h. Northern blot analysis further revealed that MK45 expression was also induced in LPS-activated B cells and antigen-triggered CD4 T cells in vitro. MK45 expression was low or undetectable in most other mouse tissues examined, when compared to activated lymphocytes. Importantly, the mRNA expression level of other sialyltransferases remained largely unchanged during the early stage of lymphocyte activation. Finally, increased ecto-sialyltransferase activity and an altered sialylation pattern were demonstrated on the cell surface of early activated CD8 T cells. Our report identifies a candidate sialyltransferase gene that is involved in the early alteration of the sialylation pattern of cell surface molecules in activated lymphocytes.

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Year:  1999        PMID: 10330278     DOI: 10.1093/intimm/11.5.731

Source DB:  PubMed          Journal:  Int Immunol        ISSN: 0953-8178            Impact factor:   4.823


  8 in total

1.  Post-conversion sialylation of prions in lymphoid tissues.

Authors:  Saurabh Srivastava; Natallia Makarava; Elizaveta Katorcha; Regina Savtchenko; Reinhard Brossmer; Ilia V Baskakov
Journal:  Proc Natl Acad Sci U S A       Date:  2015-11-16       Impact factor: 11.205

Review 2.  Role of sialylation of N-linked glycans in prion pathogenesis.

Authors:  Natallia Makarava; Ilia V Baskakov
Journal:  Cell Tissue Res       Date:  2022-01-28       Impact factor: 4.051

3.  Expression of sialyltransferase activity on intact human neutrophils.

Authors:  Salahaldin Rifat; Tae Jin Kang; Dean Mann; Lei Zhang; Adam C Puche; Nicholas M Stamatos; Simeon E Goldblum; Reinhard Brossmer; Alan S Cross
Journal:  J Leukoc Biol       Date:  2008-07-29       Impact factor: 4.962

4.  Differential sialylation modulates voltage-gated Na+ channel gating throughout the developing myocardium.

Authors:  Patrick J Stocker; Eric S Bennett
Journal:  J Gen Physiol       Date:  2006-02-13       Impact factor: 4.086

5.  Sialylation of Glycosylphosphatidylinositol (GPI) Anchors of Mammalian Prions Is Regulated in a Host-, Tissue-, and Cell-specific Manner.

Authors:  Elizaveta Katorcha; Saurabh Srivastava; Nina Klimova; Ilia V Baskakov
Journal:  J Biol Chem       Date:  2016-06-17       Impact factor: 5.157

6.  Mutation in ST6GALNAC5 identified in family with coronary artery disease.

Authors:  Kolsoum InanlooRahatloo; Amir Farhang Zand Parsa; Klaus Huse; Paniz Rasooli; Saeid Davaran; Matthias Platzer; Marcel Kramer; Jian-Bing Fan; Casey Turk; Sasan Amini; Frank Steemers; Kevin Gunderson; Mostafa Ronaghi; Elahe Elahi
Journal:  Sci Rep       Date:  2014-01-08       Impact factor: 4.379

Review 7.  Multifaceted Role of Sialylation in Prion Diseases.

Authors:  Ilia V Baskakov; Elizaveta Katorcha
Journal:  Front Neurosci       Date:  2016-08-08       Impact factor: 4.677

8.  Amaranthus leucocarpus lectin recognizes a moesin-like O-glycoprotein and costimulates murine CD3-activated CD4(+) T cells.

Authors:  Maria Arenas-Del Ángel; Martha Legorreta-Herrera; Guillermo Mendoza-Hernández; Yonathan Garfias; Raul Chávez; Edgar Zenteno; Ricardo Lascurain
Journal:  Immun Inflamm Dis       Date:  2015-06-05
  8 in total

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