Homocysteine modification of HLA antigens and its immunological consequences.
Homocysteine-treated cells can be specifically lysed by cytotoxic T lymphocytes (CTL) identifiable in patients with ankylosing spondylitis and reactive arthritis. Sensitization of target cells involves disulfide bonding and the interaction between homocysteine and HLA antigens occurs in a pre-Golgi...
| Main Authors: | , , , , , , |
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| Format: | Journal article |
| Language: | English |
| Published: |
1996
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| _version_ | 1797073952456048640 |
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| author | Gao, X Wordsworth, P Mcmichael, A Kyaw, M Seifert, M Rees, D Dougan, G |
| author_facet | Gao, X Wordsworth, P Mcmichael, A Kyaw, M Seifert, M Rees, D Dougan, G |
| author_sort | Gao, X |
| collection | OXFORD |
| description | Homocysteine-treated cells can be specifically lysed by cytotoxic T lymphocytes (CTL) identifiable in patients with ankylosing spondylitis and reactive arthritis. Sensitization of target cells involves disulfide bonding and the interaction between homocysteine and HLA antigens occurs in a pre-Golgi compartment in the cells. Salmonella-infected B cells are also lysed by homocysteine-specific CTL, suggesting that intracellular invading microorganisms may provide homocysteine which would gain access to the newly synthesized intracellular HLA molecules and modify them inside the cells. Two different mechanisms for homocysteine modification of HLA antigens are proposed: homocysteine could bind directly to the unpaired cysteine residues in HLA antigens, or it could bind indirectly to HLA antigens through cysteine-containing peptides bound to them. Thus, HLA antigens containing unpaired cysteine residues (e.g. HLA B27) could be modified by homocysteine directly or indirectly, while HLA antigens without unpaired cysteine residues (e.g. HLA A68) could only be modified indirectly. The results are discussed in relation to the potential involvement of homocysteine-specific CTL in ankylosing spondylitis and reactive arthritis, both of which are related to bacterial infections, associated with HLA B27, and considered to be autoimmune diseases. |
| first_indexed | 2024-03-06T23:29:18Z |
| format | Journal article |
| id | oxford-uuid:6b76432e-91da-4f74-a131-029e1c2df259 |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-06T23:29:18Z |
| publishDate | 1996 |
| record_format | dspace |
| spelling | oxford-uuid:6b76432e-91da-4f74-a131-029e1c2df2592022-03-26T19:04:14ZHomocysteine modification of HLA antigens and its immunological consequences.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:6b76432e-91da-4f74-a131-029e1c2df259EnglishSymplectic Elements at Oxford1996Gao, XWordsworth, PMcmichael, AKyaw, MSeifert, MRees, DDougan, GHomocysteine-treated cells can be specifically lysed by cytotoxic T lymphocytes (CTL) identifiable in patients with ankylosing spondylitis and reactive arthritis. Sensitization of target cells involves disulfide bonding and the interaction between homocysteine and HLA antigens occurs in a pre-Golgi compartment in the cells. Salmonella-infected B cells are also lysed by homocysteine-specific CTL, suggesting that intracellular invading microorganisms may provide homocysteine which would gain access to the newly synthesized intracellular HLA molecules and modify them inside the cells. Two different mechanisms for homocysteine modification of HLA antigens are proposed: homocysteine could bind directly to the unpaired cysteine residues in HLA antigens, or it could bind indirectly to HLA antigens through cysteine-containing peptides bound to them. Thus, HLA antigens containing unpaired cysteine residues (e.g. HLA B27) could be modified by homocysteine directly or indirectly, while HLA antigens without unpaired cysteine residues (e.g. HLA A68) could only be modified indirectly. The results are discussed in relation to the potential involvement of homocysteine-specific CTL in ankylosing spondylitis and reactive arthritis, both of which are related to bacterial infections, associated with HLA B27, and considered to be autoimmune diseases. |
| spellingShingle | Gao, X Wordsworth, P Mcmichael, A Kyaw, M Seifert, M Rees, D Dougan, G Homocysteine modification of HLA antigens and its immunological consequences. |
| title | Homocysteine modification of HLA antigens and its immunological consequences. |
| title_full | Homocysteine modification of HLA antigens and its immunological consequences. |
| title_fullStr | Homocysteine modification of HLA antigens and its immunological consequences. |
| title_full_unstemmed | Homocysteine modification of HLA antigens and its immunological consequences. |
| title_short | Homocysteine modification of HLA antigens and its immunological consequences. |
| title_sort | homocysteine modification of hla antigens and its immunological consequences |
| work_keys_str_mv | AT gaox homocysteinemodificationofhlaantigensanditsimmunologicalconsequences AT wordsworthp homocysteinemodificationofhlaantigensanditsimmunologicalconsequences AT mcmichaela homocysteinemodificationofhlaantigensanditsimmunologicalconsequences AT kyawm homocysteinemodificationofhlaantigensanditsimmunologicalconsequences AT seifertm homocysteinemodificationofhlaantigensanditsimmunologicalconsequences AT reesd homocysteinemodificationofhlaantigensanditsimmunologicalconsequences AT dougang homocysteinemodificationofhlaantigensanditsimmunologicalconsequences |