Evidence for extensive intermolecular disulfide bonds of the proteins of non-ionic detergent high-salt-resistant skeletons of normal lymphocytes, and the altered structure in leukemia
✍ Scribed by Sinan Tas; Lewis V. Rodriguez; Benjamin Drewinko; Jose M. Trujillo
- Publisher
- John Wiley and Sons
- Year
- 1984
- Tongue
- French
- Weight
- 526 KB
- Volume
- 34
- Category
- Article
- ISSN
- 0020-7136
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✦ Synopsis
Normal and leukemic lymphocytes were subjected to lysis with a non-ionic detergent and 2.0 M NaCI. The intact nuclear DNA and the associated molecules resulting from these lyses (the nucleoids) were then separated from DNAdissociated molecules and analyzed by sodium dodecyl sulfate-polyauylamide gel electrophoresis. Most of the proteins undissociable by 2.0 M NaCl from normal lymphocyte nuclear DNA or from DNA-associated molecules appear to be intermolecularly S-S linked. A distinct set of these proteins was either absent or only present in greatly decreased mounts in association with the leukemic lymphocyte nuclear DNA exposed to 2.0 M NaCI. On the other hand, the opposite relationship was found for a an MW 71 ,OOO protein with leukemic lymphocytes of every patient studied regardless of the subtype of leukemia. Conversion of normal quiescent lymphocytes to cycling cells by lectin stimulation rendered them similar to leukemic cells in some respects but not in all. Our results show an altered nuclo(cyto)skeletal structure in leukemic cells; in general the proteins involved appear to be sulfhydryl proteins whose redox states andlor DNA association properties are modified by the neoplastic transformation of lymphocytes.