A tyrosine protein kinase activity has been detected in the mitochondrial fraction purified from human fibroblasts. By enzymatic and sedimentation analysis this activity appeared to be localized in the mitochondrial outer membrane. Mitochondrial tyrosine phosphorylation was strictly dependent on the
Enhanced activity of cyclin A-associated kinase in immortalized human fibroblasts
β Scribed by Ryuichiro Ohashi; Masahiro Miyazaki; Kazuo Fushimi; Toshiya Tsuji; Yusuke Inoue; Nobuyoshi Shimizu; Masayoshi Namba
- Publisher
- John Wiley and Sons
- Year
- 1999
- Tongue
- French
- Weight
- 164 KB
- Volume
- 82
- Category
- Article
- ISSN
- 0020-7136
No coin nor oath required. For personal study only.
β¦ Synopsis
Deregulation of cell cycle regulatory mechanisms leads to disruption of normal control of cell growth and may be associated with neoplastic transformation. To determine whether immortalized human cells have alterations in their cell cycle regulatory mechanisms, we analyzed cell cycle regulatory proteins in 2 immortalized human fibroblast cell lines, KMST-6 and OUMS-24/P6X, established by repeated irradiation with 60 Co gamma rays alone or mutant p53 gene transfection plus X-ray irradiation, respectively. Both the immortalized cell lines had markedly enhanced activity of cyclin A-associated kinase as compared with their normal counterparts. The high activity of cyclin A-associated kinase was well correlated with the increased expression of cyclin A mRNA and its protein. In addition, the immortalized cell lines showed significantly reduced amounts of p21 Cip1/Waf1/Sdi1 , a potent inhibitor of cyclin dependent kinases. Furthermore, among the pRb family of proteins, p107 and p130, were hyperphosphorylated in both the immortalized cell lines, suggesting possible participation in upregulation of cyclin A associated kinase activity. These changes represent some important characteristics of immortalized cells. Int.
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