| Autor: |
Tsitsiloni, O.E. Heimer, E. Felix, A. Yialouris, P.P. Vamvoukakis, J. Voelter, W. Haritos, A.A. |
| Jazyk: |
angličtina |
| Rok vydání: |
1994 |
| Předmět: |
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| Popis: |
A radioimmunoassay specific for the C-terminus of human prothymosin α was developed using the synthetic peptide[Cys-Aca°]-human prothymosin α (90-109)-OH coupled to KLH as antigen and the analogue [Tyr-Aca°]-human prothymosin α (90-109)-OH labelled with 125I as tracer. The radioimmunoassay measured intact prothymosin α, in the range of 2-100 pmol and does not cross-react with the partly homologous polypeptide parathymosin α. A major epitope was located in the segment 95-107. A radioimmunoassay specific for the N-terminus of human parathymosin α, also measuring intact parathymosin α in the range of 1-20 pmol and not cross-reacting with prothymosin α, was developed using the synthetic peptide [Cys-Aca°]-human parathymosin α (1-30)-OH as antigen coupled to KLH and the analogue [Tyr-Aca°]-human parathymosin α (1-10)-OH labelled with 125I as tracer. A major epitope was located in the segment 1-10. These radioimmunoassays, together with a previously established radioimmunoassay for the N-terminus of prothymosin α, permitted the identification of the molecular forms of the cross-reactive materials in both normal and neoplastic breast tissue extracts as intact prothymosin α and parathymosin α. It was also possible to reveal significantly higher levels of both α-thymosins in breast cancer tissue compared to the nearby healthy tissue - the mean of 14 samples was over 14-fold higher - suggesting a role of both prothymosin α and parathymosin α in cell proliferation. The reported radioimmunoassays are expected to facilitate the search for prognostic and/or diagnostic applications of these polypeptides in human cancer. © 1994. |
| Databáze: |
OpenAIRE |
| Externí odkaz: |
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