Difference between revisions of "WFYellow(F08) Research Proposal"

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(Allen and Jess's 20.109 Module 3 Research Proposal Resource Page)
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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:</b>  
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<b>Idea(s):</b>  
Identify proteins associated with extracellular Hsp90 (in particular HER-2/ErbB2)
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Identify proteins associated with extracellularlly-presented Hsp90 (in particular HER-2/ErbB2), which is known to be over-expressed in proliferating cancer cells.
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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>

Revision as of 09:59, 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.

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

  1. 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 | PubMed ID:18800240 | HubMed [cid08]
  2. 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 | PubMed ID:18056992 | HubMed [sidera-jcb-2008]
  3. 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 | PubMed ID:15146192 | HubMed [eustace04]
  4. 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 | PubMed ID:18469526 | HubMed [sidera08]
  5. Eustace BK and Jay DG. Extracellular roles for the molecular chaperone, hsp90. Cell Cycle. 2004 Sep;3(9):1098-100. PubMed ID:15326368 | HubMed [eustace04b]
  6. 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 | PubMed ID:17645779 | HubMed [tsutsumi07]
All Medline abstracts: PubMed | HubMed

Methods
cell fractionstion
TAP (or other)-tagging