- 作者: Shun-Chun Yang; Chian-Hoang Huang; Nien-Jung Chen; Cheng-Kung Chou; Chi-Hung Lin
- 作者服務機構: Institute of Microbiology and Immunology, and Institute of Genetice, National Yang-Ming University; Department of Medical Research, Veterans General Hospital, Taipei, and Department of Medical Research, Chi-Mei Foundation Hospital, Tainan, Taiwan, ROC
- 中文摘要: --
- 英文摘要: Protein phosphorylation is involved in many biologicalactivities and plays important roles in cell cycle progres-sion. In the present study, we identified a serine/threo-nine kinase, hAIK, from human hepatic cells using de-generated polymerase chain reactions with a pair ofprimers derived from the highly conserved sequence inthe catalytic domain of kinases. The full-length hAIKcDNA was then obtained, which contained 403 aminoacids and was homologous to Drosophila Aurora2 andyeast lpl1 proteins. Northern blotting analysis revealedthat hAIK was highly expressed in the testis but not inother tissues. Expressions of hAIK drastically increasedin cancer tissues/cell lines but not in fibroblasts or nontu-morigenic cell lines. The recombinant hAIK protein phos-phorylated itself and histone H1; this phosphorylationactivity was totally abolished after a point mutation at thecatalytic domain (hAIKm). During the interphase cell,hAIK was found mainly in the cytoplasm: during mitosishAIK accumulated at the centrosomes. In addition, over-expression of hAIK in cancer cell lines (HEK293T andHeLa) appeared to inhibit cell cycle progression. None ofthese phenomena were observed in hAIKm whose ki-nase activity was rendered inactive. Our results suggestthat hAIK protein/activity might modulate cell cycle pro-gression by interacting with the centrosomes and/or pro-teins associated with these structures.
- 中文關鍵字: --
- 英文關鍵字: --