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dc.contributor.authorSepponen, Kirsi
dc.date.accessioned2011-08-21T16:57:14Z
dc.date.available2011-08-21T16:57:14Z
dc.date.issued2011
dc.identifier.otheroai:jykdok.linneanet.fi:1181709
dc.identifier.urihttps://jyx.jyu.fi/handle/123456789/36565
dc.description.abstractAn important step in cancer metastasis is the ability of the cancer cells to degrade the surrounding extracellular matrix (ECM) and migrate through it. To accomplish this, invasive cancer cells generate protrusive structures called invadopodia, which are dynamic cell protrusions that secrete matrix metalloproteinases (MMPs) responsible for the degradation of the ECM. Invadopodia formation employs the actin polymerization machinery and several cell adhesion, signal transduction and matrix degradation proteins. In addition, mechanisms involving membrane deformation may play a major role in their formation. Recently, an evolutionary conserved group of proteins involved in the formation of cell protrusions was characterized. These proteins were found to contain an inverse Bin-Amphiphysin-Rvs167 (I-BAR) domain. The I-BAR domain is capable of bending the plasma membrane outwards and via accessory domains, the I-BAR proteins link this membrane bending activity to actin cytoskeleton remodeling to generate cell protrusions. In the present study, the aim was to examine the localization of I-BAR domain proteins in invasive cancer cell lines. First, I studied the expression of the members of the I-BAR gene family (ABBA, IRTKS, IRSp53) in MDA-MB-231 breast cancer cells and SNB-19 glioma cells by reverse transcription polymerase chain reaction (RT-PCR) and Western blotting. The results indicated that I-BAR domain proteins were expressed at the messenger RNA (mRNA) and protein level in both cell lines. Then, to investigate the sub-cellular localization of these proteins to invasive sites, an ECM degradation assay was set up to distinguish invadopodias from other actin-rich sub-cellular structures. Using this assay, the localization of both endogenous and green fluorescent protein (GFP)-tagged I-BAR domain proteins to invadopodia was studied by light microscopy. Endogenous I-BAR domain proteins were examined both in two dimensional (2D) and three dimensional (3D) environments, but the antibodies used in this study appeared not to be suitable for their detection. However, the intensity profiles of invadopodia showed that in cells expressing I-BAR domain proteins fused to a GFP, these proteins accumulated either on the edge or at the centre of an invadopodium. The results suggest that the I-BAR domain proteins are likely to be recruited to distinct sites of invadopodia where they can induce or stabilize plasma membrane curvature and link it to actin cytoskeleton remodeling during the formation of invasive cell protrusions.
dc.format.extent67 sivua
dc.language.isoeng
dc.rightsThis publication is copyrighted. You may download, display and print it for Your own personal use. Commercial use is prohibited.en
dc.rightsJulkaisu on tekijänoikeussäännösten alainen. Teosta voi lukea ja tulostaa henkilökohtaista käyttöä varten. Käyttö kaupallisiin tarkoituksiin on kielletty.fi
dc.titleLocalization of I-BAR domain proteins in invasive cancer cells
dc.typeBooken
dc.identifier.urnURN:NBN:fi:jyu-2011082111261
dc.type.dcmitypeTexten
dc.type.ontasotPro gradufi
dc.type.ontasotMaster’s thesisen
dc.contributor.tiedekuntaMatemaattis-luonnontieteellinen tiedekuntafi
dc.contributor.tiedekuntaFaculty of Sciencesen
dc.contributor.laitosBio- ja ympäristötieteiden laitosfi
dc.contributor.laitosDepartment of Biological and Environmental Scienceen
dc.contributor.yliopistoUniversity of Jyväskyläen
dc.contributor.yliopistoJyväskylän yliopistofi
dc.contributor.oppiaineSolu- ja molekyylibiologiafi
dc.contributor.oppiaineCell and molecular biologyen
dc.date.updated2011-08-21T16:57:14Z
dc.rights.accesslevelopenAccessfi
dc.contributor.oppiainekoodi4013
dc.subject.ysosyöpäsolut
dc.subject.ysoproteiinit


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