WFYellow(F08) Research Proposal: Difference between revisions
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==[[User:Allen Lin | Allen]] and [[User:Jessho | Jess's]] 20.109 Module 3 Research Proposal Resource Page== | ==[[User:Allen Lin | Allen]] and [[User:Jessho | Jess's]] 20.109 Module 3 Research Proposal Resource Page== | ||
<b>Idea(s):</b> | <b>Idea(s):</b> | ||
Identify proteins associated with extracellularlly-presented Hsp90 (in particular HER-2/ErbB2), which is known to be over-expressed in proliferating cancer cells. | ##Identify proteins associated with extracellularlly-presented Hsp90 (in particular HER-2/ErbB2), which is known to be over-expressed in proliferating cancer cells. | ||
##Identify the membrane targeting sequence of Hsp90, produce interfering RNA, and observe phenotypic changes. | |||
High membrane-bound Hsp90 expression also correlates with the rounded morphology of proliferative cancer. One potential research idea is to study the induction of flat vs. rounded morphology pathways and observe whether or not return of flattened morphology reduces cell proliferation, metastasis, and tissue invasion. | ##High membrane-bound Hsp90 expression also correlates with the rounded morphology of proliferative cancer. One potential research idea is to study the induction of flat vs. rounded morphology pathways and observe whether or not return of flattened morphology reduces cell proliferation, metastasis, and tissue invasion. | ||
<b>Links to papers</b> | <b>Links to papers</b> | ||
| Line 17: | Line 17: | ||
<b>Methods</b> | <b>Methods</b> | ||
<br>cell | <br>cell fractionation | ||
<br>TAP (or other)-tagging | <br>TAP (or other)-tagging | ||
<br>immunofluorescence | |||
Revision as of 11:01, 19 November 2008
Allen and Jess's 20.109 Module 3 Research Proposal Resource Page
Idea(s):
- Identify proteins associated with extracellularlly-presented Hsp90 (in particular HER-2/ErbB2), which is known to be over-expressed in proliferating cancer cells.
- Identify the membrane targeting sequence of Hsp90, produce interfering RNA, and observe phenotypic changes.
- High membrane-bound Hsp90 expression also correlates with the rounded morphology of proliferative cancer. One potential research idea is to study the induction of flat vs. rounded morphology pathways and observe whether or not return of flattened morphology reduces cell proliferation, metastasis, and tissue invasion.
Links to papers
- Cid C, Regidor I, Poveda PD, and Alcazar A. Expression of heat shock protein 90 at the cell surface in human neuroblastoma cells. Cell Stress Chaperones. 2009 May;14(3):321-7. DOI:10.1007/s12192-008-0076-7 |
- Sidera K, Gaitanou M, Stellas D, Matsas R, and Patsavoudi E. A critical role for HSP90 in cancer cell invasion involves interaction with the extracellular domain of HER-2. J Biol Chem. 2008 Jan 25;283(4):2031-41. DOI:10.1074/jbc.M701803200 |
- Eustace BK, Sakurai T, Stewart JK, Yimlamai D, Unger C, Zehetmeier C, Lain B, Torella C, Henning SW, Beste G, Scroggins BT, Neckers L, Ilag LL, and Jay DG. Functional proteomic screens reveal an essential extracellular role for hsp90 alpha in cancer cell invasiveness. Nat Cell Biol. 2004 Jun;6(6):507-14. DOI:10.1038/ncb1131 |
- Sidera K and Patsavoudi E. Extracellular HSP90: conquering the cell surface. Cell Cycle. 2008 Jun 1;7(11):1564-8. DOI:10.4161/cc.7.11.6054 |
- Eustace BK and Jay DG. Extracellular roles for the molecular chaperone, hsp90. Cell Cycle. 2004 Sep;3(9):1098-100.
- Tsutsumi S and Neckers L. Extracellular heat shock protein 90: a role for a molecular chaperone in cell motility and cancer metastasis. Cancer Sci. 2007 Oct;98(10):1536-9. DOI:10.1111/j.1349-7006.2007.00561.x |
Methods
cell fractionation
TAP (or other)-tagging
immunofluorescence
