Regulation of cancer cell metastatic properties by Akt = Akt 인산화 효소에 의한 암세포 전이 기능의 조절

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The Akt serine/threonine kinase is well known as an important mediator of multiple cell survival signaling pathways. Here, I demonstrate for the first time a major role of Akt in the metastatic properties of the highly metastatic cell line, HT1080. Using live confocal microscopic analyses, I found Akt to be localized in the leading edge membrane area of migrating HT1080 cells. This localization was phosphoinositide-3 kinase (PI3K)-dependent and required the lipid binding ability of the phosphoinositides-binding pleckstrin homology (PH) domain of Akt. I examined the possible function of Akt in HT1080 invasion. Surprisingly, Akt potently promoted HT1080 invasion, by increasing cell motility and matrix metalloproteinase-9 production, in a manner highly dependent on its kinase activity and membrane-translocating ability. The increase in matrix metalloproteinase-9 (MMP-9) production was mediated by activation of NF-$\kappa$B transcriptional activity by Akt. However, Akt did not affect the cell-cell or cell-matrix adhesion properties of HT1080. Collectively, my findings establish Akt as a major factor in the metastatic abilities of cancer cells.
Advisors
Chung, Jong-Kyeongresearcher정종경researcher
Description
한국과학기술원 : 생물과학과,
Publisher
한국과학기술원
Issue Date
2001
Identifier
169411/325007 / 000993070
Language
eng
Description

학위논문(석사) - 한국과학기술원 : 생물과학과, 2001.8, [ iv, 66 p. ]

Keywords

PI3 kinase; metastasis; invasion; Akt; metalloproteinase; metalloproteinase; 인지질 인산화 효소; 전이; 침투; 인산화 효소 Akt

URI
http://hdl.handle.net/10203/27943
Link
http://library.kaist.ac.kr/search/detail/view.do?bibCtrlNo=169411&flag=dissertation
Appears in Collection
BS-Theses_Master(석사논문)
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