Phosphorylation status modulates Bcl‐2 function during glucocorticoid‐induced apoptosis in T lymphocytes
| Autor: | Se-Te J. Huang, John A. Cidlowski |
|---|---|
| Rok vydání: | 2002 |
| Předmět: |
Programmed cell death
Genotype Cell Survival T-Lymphocytes Cell Mutant Gene Expression Apoptosis DNA Fragmentation Biology Biochemistry Dexamethasone Tumor Cells Cultured Genetics medicine Animals Humans Phosphorylation Glucocorticoids Molecular Biology Cell Size Transfection Flow Cytometry Molecular biology Mitochondria medicine.anatomical_structure Proto-Oncogene Proteins c-bcl-2 Cell culture Mutation DNA fragmentation Biotechnology |
| Zdroj: | The FASEB Journal. 16:825-832 |
| ISSN: | 1530-6860 0892-6638 |
| DOI: | 10.1096/fj.01-0852com |
| Popis: | Glucocorticoids are known to induce apoptosis in lymphoid cells, and Bcl-2 overexpression can block the apoptosis-inducing action of glucocorticoids. Since phosphorylation of Bcl-2 is implicated in regulating Bcl-2 function, we considered the role of Bcl-2 phosphorylation in protecting lymphoid cells from glucocorticoid-induced cell death. Five stably transfected cell lines of WEHI 7.1 cells expressing either wild-type Bcl-2 or alanine mutants of Bcl-2 at amino acids threonine 56, serine 70, threonine 74, or serine 87 were created. Expression of the mutant Bcl-2 proteins was documented by flow cytometry and Western blot analysis. Mutation of Bcl-2 on T56 and S87 eliminated the ability of Bcl-2 to inhibit glucocorticoid-induced cell shrinkage, mitochondrial depolarization, DNA fragmentation, and cell death. Mutation of T74 only partially impaired the ability of Bcl-2 to block glucocorticoid-induced apoptosis whereas mutation of S70 in Bcl-2 did not alter its ability to block glucocorticoid-induced apoptosis. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|
Plný text