| Autor: |
Van Denderen, Janneke, Van Der Plas, Dorien, Meeuwsen, Toon, Zegers, Netty, Boersma, Wim, Grosveld, Gerard, Van Ewijk, Willem |
| Zdroj: |
Blood; July 1990, Vol. 76 Issue: 1 p136-141, 6p |
| Abstrakt: |
Philadelphia (Ph')-positive acute lymphoblastic leukemia (ALL) is highly associated with two forms of chimeric bcr-ablproteins: P190bcr-abland P210bcr-abl. Whereas P210bcr-ablalso occurs in chronic myeloid leukemia, P190bcr-ablis uniquely expressed in Ph'-positive ALL. As a consequence, P190bcr-ablis preeminently a tumor-specific marker in leukemic cells of ALL patients. Because P190bcr-ablis composed of the normal bcrand ablproteins, the major part of the P190bcr-ablmolecule comprises nontumor-specific determinants. The joining region between bcrand abl, newly generated during the Ph' translocation, is exclusively a tumor-specific epitope on the P190bcr-ablmolecule. Therefore, only antibodies against the bcr-abljoining region will detect the tumor-specificity of P190bcr-abl. In this study a polyclonal antiserum, termed BP-ALL, was raised against a synthetic peptide corresponding to the bcr-abljunction in P190bcr-abl. The reactivity of BP-ALL with native p190bcr-ablderived from a Ph'-positive ALL cell line (TOM-1) was tested using immunoprecipitation analysis. BP-ALL reacted highly specifically with P190bcr-ablbut not with P210bcr-ablisolated from chronic myeloid leukemia cell lines. Peptide inhibition studies further confirmed the fine specificity of BP-ALL. Our data indicate that the tumor-specific bcr-abljunction domain is exposed in an antigenic fashion on the P190bcr-ablmolecule. |
| Databáze: |
Supplemental Index |
| Externí odkaz: |
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