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dc.contributor.advisorHulmi, Juha
dc.contributor.advisorIhalainen, Janne
dc.contributor.authorHärkönen, Jouni
dc.date.accessioned2017-07-20T09:39:57Z
dc.date.available2017-07-20T09:39:57Z
dc.date.issued2017
dc.identifier.otheroai:jykdok.linneanet.fi:1705344
dc.identifier.urihttps://jyx.jyu.fi/handle/123456789/54939
dc.description.abstractCachexia is a muscle wasting condition associated with multiple different chronic illnesses, such as cancer, diabetes and AIDS. In cancer, approximately 80% of patients with advanced disease have symptoms of muscle wasting, and around 25% of cancer mortality concerns cachexia. Elevated serum levels of different cytokines and TGF-β protein family members, such as Interleukin-6, Myostatin and Activin-A, have been observed in cachetic patients and test animals. However, the mechanistic role and the relative contribution of these molecules to muscle loss in the syndrome have not yet been fully elucidated. In this thesis, the gene-expression levels of Activin-A, Myostatin and Interleukin-6 was assessed with Reverse-Transcriptase quantitative PCR from the tumor and muscle tissue of cachetic C26-tumor-bearing mice to clarify whether they arise from the tumor or are muscle derived. Additionally, transfection of CAGA-luciferase plasmid construct was optimized for the C2C12 murine myoblast cell-line to be utilized in research concerning TGF-β mediated cancer-associated cachexia in vitro. The function of the construct was tested by administration of exogenous Activin-A, with and without its inhibitor, into the C2C12 growth media. This thesis showed a marked increase in the expression levels of Activin-A (inhibin-βA) and IL-6 mRNA in cachexia inducing tumors (C26) when compared to tumors not inducing cachexia (Lewis-Lung-Cancer) (P < 0.001). Additionally, the results show decrease in muscle-derived Activin-A (inhibin-βA) in the cachetic groups (P < 0.05). These results imply that Activin-A and Interleukin-6 are strongly induced in the tumors that produced cachexia in vivo. This work also presents a successful, optimized plasmid transfection protocol for the notoriously transfection resistant C2C12-myoblast cell line. The presented in vitro –method can partially replace animal tests in related settings, when studying the mechanistic effects of cachexia-inducing TGF-β proteins on muscle tissue.en
dc.format.extent1 verkkoaineisto (41 sivua)
dc.language.isoeng
dc.rightsJulkaisu on tekijänoikeussäännösten alainen. Teosta voi lukea ja tulostaa henkilökohtaista käyttöä varten. Käyttö kaupallisiin tarkoituksiin on kielletty.fi
dc.rightsThis publication is copyrighted. You may download, display and print it for Your own personal use. Commercial use is prohibited.en
dc.subject.otherkakeksia
dc.subject.otheraktiviini-a
dc.subject.othermyostatiini
dc.subject.otherCachexia
dc.subject.otherMyostatin
dc.subject.otherActivin-A
dc.subject.otherInterleukin-6
dc.subject.otherC2C12
dc.titleActivin-A, myostatin and interleukin-6 in cancer associated cachexia
dc.identifier.urnURN:NBN:fi:jyu-201707203334
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.updated2017-07-20T09:39:57Z
dc.rights.accesslevelopenAccessfi
dc.contributor.oppiainekoodi4013
dc.subject.ysosyöpätaudit
dc.subject.ysoproteiinit
dc.subject.ysointerleukiinit


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