The extracellular matrix protein EMILIN1 silences the RAS-ERK pathway via α4β1 integrin and decreases tumor cell growth
Identifieur interne : 000099 ( Main/Exploration ); précédent : 000098; suivant : 000100The extracellular matrix protein EMILIN1 silences the RAS-ERK pathway via α4β1 integrin and decreases tumor cell growth
Auteurs : Teresa Maria Elisa Modica [Italie] ; Orlando Maiorani [Italie] ; Giulio Sartori [Italie] ; Eliana Pivetta [Italie] ; Roberto Doliana [Italie] ; Alessandra Capuano [Italie] ; Alfonso Colombatti [Italie] ; Paola Spessotto [Italie]Source :
- Oncotarget [ 1949-2553 ] ; 2017.
Abstract
The extracellular matrix plays a fundamental role in physiological and pathological proliferation. It exerts its function through a signal cascade starting from the integrins that take direct contact with matrix constituents most of which behave as pro-proliferative clues. On the contrary, EMILIN1, a glycoprotein interacting with the α4β1 integrin through its gC1q domain, plays a paradigmatic anti-proliferative role. Here, we demonstrate that the EMILIN1-α4 interaction de-activates the MAPK pathway through HRas. Epithelial cells expressing endogenous α4 integrin and persistently plated on gC1q inhibited pERK1/2 increasing HRasGTP and especially the HRasGTP ubiquitinated form (HRasGTP-Ub). The drug salirasib reversed this effect. In addition, only the gC1q-ligated α4 integrin chain co-immunoprecipitated the ubiquitinated HRas. Only epithelial cells transfected with the wild type form of the α4 integrin chain showed the EMILIN1/α4β1/HRas/pERK1/2 link, whereas cells transfected with a α4 integrin chain carrying a truncated cytoplasmic tail had no effect. In this study we unveiled the pathway activated by the gC1q domain of EMILIN1 through α4β1 integrin engagement and leading to the decrease of proliferation in an epithelial system.
Url:
DOI: 10.18632/oncotarget.15067
PubMed: 28177903
PubMed Central: 5432316
Affiliations:
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Italy</nlm:aff><country xml:lang="fr">Italie</country><wicri:regionArea> Department of Translational Research, Experimental Oncology 2 Division, CRO Aviano, National Cancer Institute, Aviano, PN 33081</wicri:regionArea><wicri:noRegion>PN 33081</wicri:noRegion></affiliation></author><author><name sortKey="Pivetta, Eliana" sort="Pivetta, Eliana" uniqKey="Pivetta E" first="Eliana" last="Pivetta">Eliana Pivetta</name><affiliation wicri:level="1"><nlm:aff id="A1"> Department of Translational Research, Experimental Oncology 2 Division, CRO Aviano, National Cancer Institute, Aviano, PN 33081, Italy</nlm:aff><country xml:lang="fr">Italie</country><wicri:regionArea> Department of Translational Research, Experimental Oncology 2 Division, CRO Aviano, National Cancer Institute, Aviano, PN 33081</wicri:regionArea><wicri:noRegion>PN 33081</wicri:noRegion></affiliation></author><author><name sortKey="Doliana, Roberto" sort="Doliana, Roberto" uniqKey="Doliana R" first="Roberto" last="Doliana">Roberto Doliana</name><affiliation wicri:level="1"><nlm:aff id="A1"> Department of Translational Research, Experimental Oncology 2 Division, CRO Aviano, National Cancer Institute, Aviano, PN 33081, Italy</nlm:aff><country xml:lang="fr">Italie</country><wicri:regionArea> Department of Translational Research, Experimental Oncology 2 Division, CRO Aviano, National Cancer Institute, Aviano, PN 33081</wicri:regionArea><wicri:noRegion>PN 33081</wicri:noRegion></affiliation></author><author><name sortKey="Capuano, Alessandra" sort="Capuano, Alessandra" uniqKey="Capuano A" first="Alessandra" last="Capuano">Alessandra Capuano</name><affiliation wicri:level="1"><nlm:aff id="A1"> Department of Translational Research, Experimental Oncology 2 Division, CRO Aviano, National Cancer Institute, Aviano, PN 33081, Italy</nlm:aff><country xml:lang="fr">Italie</country><wicri:regionArea> Department of Translational Research, Experimental Oncology 2 Division, CRO Aviano, National Cancer Institute, Aviano, PN 33081</wicri:regionArea><wicri:noRegion>PN 33081</wicri:noRegion></affiliation></author><author><name sortKey="Colombatti, Alfonso" sort="Colombatti, Alfonso" uniqKey="Colombatti A" first="Alfonso" last="Colombatti">Alfonso Colombatti</name><affiliation wicri:level="1"><nlm:aff id="A1"> Department of Translational Research, Experimental Oncology 2 Division, CRO Aviano, National Cancer Institute, Aviano, PN 33081, Italy</nlm:aff><country xml:lang="fr">Italie</country><wicri:regionArea> Department of Translational Research, Experimental Oncology 2 Division, CRO Aviano, National Cancer Institute, Aviano, PN 33081</wicri:regionArea><wicri:noRegion>PN 33081</wicri:noRegion></affiliation></author><author><name sortKey="Spessotto, Paola" sort="Spessotto, Paola" uniqKey="Spessotto P" first="Paola" last="Spessotto">Paola Spessotto</name><affiliation wicri:level="1"><nlm:aff id="A1"> Department of Translational Research, Experimental Oncology 2 Division, CRO Aviano, National Cancer Institute, Aviano, PN 33081, Italy</nlm:aff><country xml:lang="fr">Italie</country><wicri:regionArea> Department of Translational Research, Experimental Oncology 2 Division, CRO Aviano, National Cancer Institute, Aviano, PN 33081</wicri:regionArea><wicri:noRegion>PN 33081</wicri:noRegion></affiliation></author></analytic><series><title level="j">Oncotarget</title><idno type="eISSN">1949-2553</idno><imprint><date when="2017">2017</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p>The extracellular matrix plays a fundamental role in physiological and pathological proliferation. It exerts its function through a signal cascade starting from the integrins that take direct contact with matrix constituents most of which behave as pro-proliferative clues. On the contrary, EMILIN1, a glycoprotein interacting with the α4β1 integrin through its gC1q domain, plays a paradigmatic anti-proliferative role. Here, we demonstrate that the EMILIN1-α4 interaction de-activates the MAPK pathway through HRas. Epithelial cells expressing endogenous α4 integrin and persistently plated on gC1q inhibited pERK1/2 increasing HRasGTP and especially the HRasGTP ubiquitinated form (HRasGTP-Ub). The drug salirasib reversed this effect. In addition, only the gC1q-ligated α4 integrin chain co-immunoprecipitated the ubiquitinated HRas. Only epithelial cells transfected with the wild type form of the α4 integrin chain showed the EMILIN1/α4β1/HRas/pERK1/2 link, whereas cells transfected with a α4 integrin chain carrying a truncated cytoplasmic tail had no effect. In this study we unveiled the pathway activated by the gC1q domain of EMILIN1 through α4β1 integrin engagement and leading to the decrease of proliferation in an epithelial system.</p></div></front><back><div1 type="bibliography"><listBibl><biblStruct><analytic><author><name sortKey="Moreno Layseca, P" uniqKey="Moreno Layseca P">P Moreno-Layseca</name></author><author><name sortKey="Streuli, Ch" uniqKey="Streuli C">CH Streuli</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Sjaastad, Md" uniqKey="Sjaastad M">MD Sjaastad</name></author><author><name sortKey="Lewis, Rs" uniqKey="Lewis R">RS Lewis</name></author><author><name sortKey="Nelson, Wj" uniqKey="Nelson W">WJ Nelson</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Illario, M" uniqKey="Illario M">M Illario</name></author><author><name sortKey="Cavallo, Al" uniqKey="Cavallo A">AL Cavallo</name></author><author><name sortKey="Bayer, Ku" uniqKey="Bayer K">KU 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Gabos</name></author><author><name sortKey="Sun, Xj" uniqKey="Sun X">XJ Sun</name></author><author><name sortKey="Wang, Xb" uniqKey="Wang X">XB Wang</name></author><author><name sortKey="Xu, X" uniqKey="Xu X">X Xu</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Spessotto, P" uniqKey="Spessotto P">P Spessotto</name></author><author><name sortKey="Lacrima, K" uniqKey="Lacrima K">K Lacrima</name></author><author><name sortKey="Nicolosi, Pa" uniqKey="Nicolosi P">PA Nicolosi</name></author><author><name sortKey="Pivetta, E" uniqKey="Pivetta E">E Pivetta</name></author><author><name sortKey="Scapolan, M" uniqKey="Scapolan M">M Scapolan</name></author><author><name sortKey="Perris, R" uniqKey="Perris R">R Perris</name></author></analytic></biblStruct></listBibl></div1></back></TEI><affiliations><list><country><li>Italie</li></country></list><tree><country name="Italie"><noRegion><name sortKey="Modica, Teresa Maria Elisa" sort="Modica, Teresa Maria Elisa" uniqKey="Modica T" first="Teresa Maria Elisa" last="Modica">Teresa Maria Elisa Modica</name></noRegion><name sortKey="Capuano, Alessandra" sort="Capuano, Alessandra" uniqKey="Capuano A" first="Alessandra" last="Capuano">Alessandra Capuano</name><name sortKey="Colombatti, Alfonso" sort="Colombatti, Alfonso" uniqKey="Colombatti A" first="Alfonso" last="Colombatti">Alfonso Colombatti</name><name sortKey="Doliana, Roberto" sort="Doliana, Roberto" uniqKey="Doliana R" first="Roberto" last="Doliana">Roberto Doliana</name><name sortKey="Maiorani, Orlando" sort="Maiorani, Orlando" uniqKey="Maiorani O" first="Orlando" last="Maiorani">Orlando Maiorani</name><name sortKey="Pivetta, Eliana" sort="Pivetta, Eliana" uniqKey="Pivetta E" first="Eliana" last="Pivetta">Eliana Pivetta</name><name sortKey="Sartori, Giulio" sort="Sartori, Giulio" uniqKey="Sartori G" first="Giulio" last="Sartori">Giulio Sartori</name><name sortKey="Spessotto, Paola" sort="Spessotto, Paola" uniqKey="Spessotto P" first="Paola" 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