Abstract
| Originalsprog | Engelsk |
|---|---|
| Tidsskrift | European Journal of Immunology |
| Vol/bind | 31 |
| Udgave nummer | 11 |
| Sider (fra-til) | 3197-206 |
| Antal sider | 9 |
| ISSN | 0014-2980 |
| DOI | |
| Status | Udgivet - 2001 |
Bibliografisk note
Keywords: Cell Line; Glycopeptides; Histocompatibility Antigens Class II; Humans; Hybridomas; Interleukin-2; Membrane Proteins; Phosphorylation; Polysaccharides; Protein-Tyrosine Kinases; Receptors, Antigen, T-Cell; Signal Transduction; Structure-Activity Relationship; T-Lymphocytes; Tyrosine; ZAP-70 Protein-Tyrosine KinaseAdgang til dokumentet
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I: European Journal of Immunology, Bind 31, Nr. 11, 2001, s. 3197-206.
Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › peer review
}
TY - JOUR
T1 - Radically altered T cell receptor signaling in glycopeptide-specific T cell hybridoma induced by antigen with minimal differences in the glycan group
AU - Jensen, T
AU - Nielsen, M
AU - Gad, Monika
AU - Hansen, P
AU - Komba, S
AU - Meldal, M
AU - Ødum, N
AU - Werdelin, Ole
N1 - Keywords: Cell Line; Glycopeptides; Histocompatibility Antigens Class II; Humans; Hybridomas; Interleukin-2; Membrane Proteins; Phosphorylation; Polysaccharides; Protein-Tyrosine Kinases; Receptors, Antigen, T-Cell; Signal Transduction; Structure-Activity Relationship; T-Lymphocytes; Tyrosine; ZAP-70 Protein-Tyrosine Kinase
PY - 2001
Y1 - 2001
N2 - A T cell hybridoma raised against the synthetic glycopeptide T(72)(Tn) was used to study whether the initial TCR signaling events are markedly different when the hybridoma is stimulated with glycopeptides closely related to the cognate glycopeptide antigen. T(72)(Tn) has an alpha-D-GalNAc group O-linked to the central threonine in the decapeptide VITAFTEGLK, and the hybridoma is known to be highly specific for this carbohydrate group. T(72)(Tn)-pulsed APC induced tyrosine phosphorylation of the TCR-zeta 21- and 23-kDa proteins and the downstream p42/44 MAP kinase and strong IL-2 secretion. APC pulsed with T(72)(alpha-D-GlcNAc), which differs from T(72)(Tn) solely by the orientation of a hydroxy group in the carbohydrate structure, completely failed to induce detectable tyrosine phosphorylation and IL-2 secretion. APC pulsed with S(72)(Tn), which differs from T(72)(Tn) by not having a methyl group in the serine amino acid side chain to which the glycan is attached, induced partial tyrosine phosphorylation of the TCR-zeta 21-kDa protein, no tyrosine phosphorylation of the MAP kinases and no IL-2 production. Molecular modeling of the MHC/glycopeptide complex revealed that the dramatic difference between the stimulatory power of T(72)(Tn) and T(72)(alpha-D-GlcNAc) is mainly due to very small differences in the TCR exposed carbohydrate structure.
AB - A T cell hybridoma raised against the synthetic glycopeptide T(72)(Tn) was used to study whether the initial TCR signaling events are markedly different when the hybridoma is stimulated with glycopeptides closely related to the cognate glycopeptide antigen. T(72)(Tn) has an alpha-D-GalNAc group O-linked to the central threonine in the decapeptide VITAFTEGLK, and the hybridoma is known to be highly specific for this carbohydrate group. T(72)(Tn)-pulsed APC induced tyrosine phosphorylation of the TCR-zeta 21- and 23-kDa proteins and the downstream p42/44 MAP kinase and strong IL-2 secretion. APC pulsed with T(72)(alpha-D-GlcNAc), which differs from T(72)(Tn) solely by the orientation of a hydroxy group in the carbohydrate structure, completely failed to induce detectable tyrosine phosphorylation and IL-2 secretion. APC pulsed with S(72)(Tn), which differs from T(72)(Tn) by not having a methyl group in the serine amino acid side chain to which the glycan is attached, induced partial tyrosine phosphorylation of the TCR-zeta 21-kDa protein, no tyrosine phosphorylation of the MAP kinases and no IL-2 production. Molecular modeling of the MHC/glycopeptide complex revealed that the dramatic difference between the stimulatory power of T(72)(Tn) and T(72)(alpha-D-GlcNAc) is mainly due to very small differences in the TCR exposed carbohydrate structure.
U2 - 10.1002/1521-4141(200111)31:11<3197::AID-IMMU3197>3.0.CO;2-5
DO - 10.1002/1521-4141(200111)31:11<3197::AID-IMMU3197>3.0.CO;2-5
M3 - Journal article
C2 - 11745336
SN - 0014-2980
VL - 31
SP - 3197
EP - 3206
JO - European Journal of Immunology
JF - European Journal of Immunology
IS - 11
ER -