Presentation of insulin and insulin A chain peptides to mouse T cells: involvement of cysteine residues
Autor: | Margot Meyer-Delius, Dimitrij Plachov, Gernot Gradehandt, Hans-Gregor Gattner, Johannes Hampl, Hubert Kalbacher, Wolfgang Voelter, Erwin Rüde |
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Rok vydání: | 1991 |
Předmět: |
Swine
medicine.medical_treatment T-Lymphocytes Immunology Antigen presentation Receptors Antigen T-Cell Antigen-Presenting Cells Peptide Mice Inbred Strains In Vitro Techniques Cell Line Epitopes Mice Antigen medicine Animals Insulin Cysteine Antigen-presenting cell Molecular Biology chemistry.chemical_classification Chemistry T-cell receptor Histocompatibility Antigens Class II Chloroquine Amino acid Biochemistry Cattle Interleukin-3 Peptides |
Zdroj: | Molecular immunology. 28(4-5) |
ISSN: | 0161-5890 |
Popis: | The requirements for insulin presentation and recognition by A alpha b A beta b- and A alpha b A beta k-restricted mouse T cells were studied using a variety of derivatives of the insulin A chain. It was found that A chain peptides with irreversibly blocked Cys residues are non-stimulatory for the T cells. This suggests that at least one of the Cys residues is essential for recognition. On the other hand, all A chain peptides containing Cys residues modified in a way reversible by reaction with thiols are stimulatory yet differ in antigenic potency. All these A chain derivatives including a 14 amino acid fragment require uptake by antigen presenting cells (APC) for efficient presentation. Differences in stimulatory potency between the A chain peptides derived from the same insulin appear to be mainly due to the efficiency of uptake and/or processing by APC. Based on these findings we propose that processing in the case of insulin and its A chain derivatives involves the reductive deblocking of Cys residues or the rearrangement of disulfide bonds apart from a possible proteolytic cleavage. The same may apply to other proteins if Cys residues in the presented peptides are important for the interaction with Ia or the T cell receptor. |
Databáze: | OpenAIRE |
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