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VASP and Profilin-1 Interaction in Cell Migration

Gau, David Martin (2011) VASP and Profilin-1 Interaction in Cell Migration. Undergraduate Thesis, University of Pittsburgh.

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    Abstract

    Profilins belong to a family of G-actin binding proteins which are thought to facilitate actinpolymerization at the leading edge of migrating cells via its polyproline interactions with majoractin nucleating and F-actin elongating proteins. The two major goals of this study are i) tospatially resolve profilins-1's (the only ubiquitously expressed member of profilin family)interaction with Ena (enabled)/VASP (vasodilator stimulated phosphoprotein) family of F-actinelongating protein, and ii) determine whether Ena/VASP regulates cell migration through itsinteraction with profilin-1. This study demonstrates the feasibility of GFP (green fluorescence protein)-based florescence resonance energy transfer (FRET) to identify profilin-1 and VASP interaction. Through acceptor photobleaching FRET (fluorescence resonance energy transfer) inMDA-MB-231 human breast cancer cells, we show that VASP and profilin-1 interaction at themembrane ruffles near the leading edge. We further show that VASP overexpression in breastcancer cells results in slower random cell motility; however VASP-induced suppression of cellmotility is partly rescued when VASP:profilin-1 interaction is downregulated These data suggestVASP utilizes profilin-1 to regulate breast cancer cell migration.


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    Item Type: University of Pittsburgh ETD
    Creators/Authors:
    CreatorsEmailORCID
    Gau, David Martindmg40@pitt.edu
    ETD Committee:
    ETD Committee TypeCommittee MemberEmailORCID
    Committee ChairRoy, Parthapar19@pitt.edu
    Committee MemberBaty, Catherinecjb16@pitt.edu
    Committee MemberGertler, Frankfgertler@mit.edu
    Committee MemberShroff, Sanjeevsshroff@pitt.edu
    Title: VASP and Profilin-1 Interaction in Cell Migration
    Status: Unpublished
    Abstract: Profilins belong to a family of G-actin binding proteins which are thought to facilitate actinpolymerization at the leading edge of migrating cells via its polyproline interactions with majoractin nucleating and F-actin elongating proteins. The two major goals of this study are i) tospatially resolve profilins-1's (the only ubiquitously expressed member of profilin family)interaction with Ena (enabled)/VASP (vasodilator stimulated phosphoprotein) family of F-actinelongating protein, and ii) determine whether Ena/VASP regulates cell migration through itsinteraction with profilin-1. This study demonstrates the feasibility of GFP (green fluorescence protein)-based florescence resonance energy transfer (FRET) to identify profilin-1 and VASP interaction. Through acceptor photobleaching FRET (fluorescence resonance energy transfer) inMDA-MB-231 human breast cancer cells, we show that VASP and profilin-1 interaction at themembrane ruffles near the leading edge. We further show that VASP overexpression in breastcancer cells results in slower random cell motility; however VASP-induced suppression of cellmotility is partly rescued when VASP:profilin-1 interaction is downregulated These data suggestVASP utilizes profilin-1 to regulate breast cancer cell migration.
    Date: 02 May 2011
    Date Type: Completion
    Defense Date: 15 April 2011
    Approval Date: 02 May 2011
    Submission Date: 20 April 2011
    Access Restriction: 5 year -- Restrict access to University of Pittsburgh for a period of 5 years.
    Patent pending: No
    Institution: University of Pittsburgh
    Thesis Type: Undergraduate Thesis
    Refereed: Yes
    Degree: BS - Bachelor of Science
    URN: etd-04202011-103456
    Uncontrolled Keywords: Cell Migration; Ena/VASP; FRET; MDA-MB-231; Profilin-1
    Schools and Programs: Swanson School of Engineering > Bioengineering
    University Honors College
    Date Deposited: 10 Nov 2011 14:39
    Last Modified: 23 May 2012 15:43
    Other ID: http://etd.library.pitt.edu/ETD/available/etd-04202011-103456/, etd-04202011-103456

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