Identification of a core sequence, c1i 260 269, that is critical for signal transduction in t cells in responsive to type II collagen

B. Tang, L. K. Myer, E. K. Rosloniec, K. B. Whiltingtont, J. M. Sliiart, Andrew Kang

Research output: Contribution to journalArticle

Abstract

Collagen-induced arthritis (CIA) is an experimental arthrtis that can he induced in susceptible strains of animals by immunization with type II collagen (CII). We previously have identified a syntheiic peptide representing sequences of type II collagen, (CII 245-270), that has ability to induce tolerance and suppress arthritis in DBA/1 mice. To determine the role of individual residues of CII 245-270 in T cell signal transduction. we compared prolein-tyrosine phosphorylation patterns of TCR-zeta chains in CH-specific T-ceII hybridomas and a T cell line following stimulation with CII 245-270 and several analog peptides. Based on the use of the analog peptides, seven residues within CII 245-270 were found to be critical for tyrosine phosphorylation of the TCR-zeta chain and phosphorylation of ZAP70, a downstream molecule in the TCR-zeta signaling pathway. Substitutions at residues 260, 261, 263, 264, 266 and 267 completely abrogated the ability of the peptide to induce phosphorylation of the TCRzeta chain. In contrast, substitution of residue 269 only partially reduced the phosphorylation of the TCR-zeta chain. Previously we have described a substituted peptide A9, that inhibits the development of CIA. When this A9 peptide, containing substitutions at the residues 260, 261 and 263, was analyzed by antigen-competition assays, it did not affect the abilities of CII 245-270 to induce phosphorylation of TCR-zeta chain. These data indicate that the ability of the A9 peptide to inhibit the elicitation of CI A is not due to a partial signaling event via the TCR zeta chain.

Original languageEnglish (US)
JournalFASEB Journal
Volume11
Issue number9
StatePublished - Dec 1 1997

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Signal transduction
Collagen Type II
Phosphorylation
Signal Transduction
Peptides
Experimental Arthritis
Substitution reactions
T-cells
Tyrosine
Collagen
Immunization
T-Lymphocytes
Inbred DBA Mouse
Hybridomas
Arthritis
Assays
Animals
zeta chain antigen T cell receptors
Antigens
Cell Line

All Science Journal Classification (ASJC) codes

  • Biotechnology
  • Biochemistry
  • Molecular Biology
  • Genetics

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Identification of a core sequence, c1i 260 269, that is critical for signal transduction in t cells in responsive to type II collagen. / Tang, B.; Myer, L. K.; Rosloniec, E. K.; Whiltingtont, K. B.; Sliiart, J. M.; Kang, Andrew.

In: FASEB Journal, Vol. 11, No. 9, 01.12.1997.

Research output: Contribution to journalArticle

Tang, B. ; Myer, L. K. ; Rosloniec, E. K. ; Whiltingtont, K. B. ; Sliiart, J. M. ; Kang, Andrew. / Identification of a core sequence, c1i 260 269, that is critical for signal transduction in t cells in responsive to type II collagen. In: FASEB Journal. 1997 ; Vol. 11, No. 9.
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abstract = "Collagen-induced arthritis (CIA) is an experimental arthrtis that can he induced in susceptible strains of animals by immunization with type II collagen (CII). We previously have identified a syntheiic peptide representing sequences of type II collagen, (CII 245-270), that has ability to induce tolerance and suppress arthritis in DBA/1 mice. To determine the role of individual residues of CII 245-270 in T cell signal transduction. we compared prolein-tyrosine phosphorylation patterns of TCR-zeta chains in CH-specific T-ceII hybridomas and a T cell line following stimulation with CII 245-270 and several analog peptides. Based on the use of the analog peptides, seven residues within CII 245-270 were found to be critical for tyrosine phosphorylation of the TCR-zeta chain and phosphorylation of ZAP70, a downstream molecule in the TCR-zeta signaling pathway. Substitutions at residues 260, 261, 263, 264, 266 and 267 completely abrogated the ability of the peptide to induce phosphorylation of the TCRzeta chain. In contrast, substitution of residue 269 only partially reduced the phosphorylation of the TCR-zeta chain. Previously we have described a substituted peptide A9, that inhibits the development of CIA. When this A9 peptide, containing substitutions at the residues 260, 261 and 263, was analyzed by antigen-competition assays, it did not affect the abilities of CII 245-270 to induce phosphorylation of TCR-zeta chain. These data indicate that the ability of the A9 peptide to inhibit the elicitation of CI A is not due to a partial signaling event via the TCR zeta chain.",
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