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Lupinus albus protein componentes inhibit MMP-2 and MMP-9 gelatinolytic activity in vitro and in vivo

dc.contributor.authorMota, Joana
dc.contributor.authorDireito, Rosa
dc.contributor.authorRocha, João
dc.contributor.authorFernandes, João
dc.contributor.authorSepodes, Bruno
dc.contributor.authorFigueira, Maria Eduardo
dc.contributor.authorRaymundo, Anabela
dc.contributor.authorLima, Ana
dc.contributor.authorFerreira, Ricardo Boavida
dc.date.accessioned2021-12-17T10:15:42Z
dc.date.available2021-12-17T10:15:42Z
dc.date.issued2021
dc.description.abstractMatrix metalloproteinases 2 and 9 (MMP-2 and MMP-9) are regarded as important clinical targets due to their nodal-point role in inflammatory and oncological diseases. Here, we aimed at isolating and characterizing am MMP-2 and-9 inhibitor (MMPI) from Lupinus albus and at assessing its efficacy in vitro and in vivo. The protein was isolated using chromatographic and 2-D electrophoretic procedures and sequenced by using MALDI-TOF TOF and MS/MS analysis. In vitro MMP-2 and 9 inhibitions were determined on colon adenocarcinoma (HT29) cells, as well as by measuring the expression levels of genes related to these enzymes. Inhibitory activities were also confirmed in vivo using a model of experimental TNBS-induced colitis in mice, with oral administrations of 15 mg kg􀀀1. After chromatographic and electrophoretic isolation, the L. albus MMP-9 inhibitor was found to comprise a large fragment from -conglutin and, to a lower extent, small fragments of -conglutin. In vitro studies showed that the MMPI successfully inhibited MMP-9 activity in a dose-dependent manner in colon cancer cells, with an IC50 of 10 g mL􀀀1 without impairing gene expression nor cell growth. In vivo studies showed that the MMPI maintained its bioactivities when administered orally and significantly reduced colitis symptoms, along with a very significant inhibition of MMP-2 and -9 activities. Overall, results reveal a novel type of MMPI in lupine that is edible, proteinaceous in nature and soluble in water, and effective in vivo, suggesting a high potential application as a nutraceutical or a functional food in pathologies related to abnormally high MMP-9 activity in the digestive systempt_PT
dc.description.versioninfo:eu-repo/semantics/publishedVersionpt_PT
dc.identifier.citationMota, J.; Direito, R.; Rocha, J.; Fernandes, J.; Sepodes, B.; Figueira, M.E.; Raymundo, A.; Lima, A.; Ferreira, R.B. Lupinus albus Protein Components Inhibit MMP-2 and MMP-9 Gelatinolytic Activity In Vitro and In Vivo. Int. J. Mol. Sci. 2021, 22, 13286pt_PT
dc.identifier.doihttps://doi.org/10.3390/ ijms222413286pt_PT
dc.identifier.urihttp://hdl.handle.net/10400.5/22755
dc.language.isoengpt_PT
dc.peerreviewedyespt_PT
dc.publisherMDPIpt_PT
dc.relationUID/AGR/04129/2020pt_PT
dc.relationAnti-inflammatory and anticancer activities of a protein isolated from Lupinus seeds and its application as functional foods
dc.relationLudexin, an edible anti-inflammatory and anticancer protein isolated from legume seeds
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/pt_PT
dc.subjectLupinus albus proteinpt_PT
dc.subjectMMP-9pt_PT
dc.subjectMMP-2pt_PT
dc.subjectgelatinasespt_PT
dc.subjectMMP inhibitorpt_PT
dc.subjectnutraceuticalpt_PT
dc.subjectgastrointestinal diseasespt_PT
dc.titleLupinus albus protein componentes inhibit MMP-2 and MMP-9 gelatinolytic activity in vitro and in vivopt_PT
dc.typejournal article
dspace.entity.typePublication
oaire.awardNumberPTDC/BAA-AGR/28608/2017
oaire.awardNumberSFRH/BD/132832/2017
oaire.awardTitleAnti-inflammatory and anticancer activities of a protein isolated from Lupinus seeds and its application as functional foods
oaire.awardTitleLudexin, an edible anti-inflammatory and anticancer protein isolated from legume seeds
oaire.awardURIinfo:eu-repo/grantAgreement/FCT/3599-PPCDT/PTDC%2FBAA-AGR%2F28608%2F2017/PT
oaire.awardURIinfo:eu-repo/grantAgreement/FCT/OE/SFRH%2FBD%2F132832%2F2017/PT
oaire.citation.titleInternational Journal of Molecular Sciencespt_PT
oaire.fundingStream3599-PPCDT
oaire.fundingStreamOE
person.familyNameRaymundo
person.familyNameFerreira
person.givenNameAnabela
person.givenNameRicardo Boavida
person.identifier1445512
person.identifier86030
person.identifier.ciencia-idD71D-F355-5B85
person.identifier.ciencia-id371D-28A0-4027
person.identifier.orcid0000-0001-5266-1685
person.identifier.orcid0000-0002-5027-7564
person.identifier.ridM-9260-2013
person.identifier.scopus-author-id55957162900
person.identifier.scopus-author-id8285312700
project.funder.identifierhttp://doi.org/10.13039/501100001871
project.funder.identifierhttp://doi.org/10.13039/501100001871
project.funder.nameFundação para a Ciência e a Tecnologia
project.funder.nameFundação para a Ciência e a Tecnologia
rcaap.rightsopenAccesspt_PT
rcaap.typearticlept_PT
relation.isAuthorOfPublication63f1faff-64dd-41b7-9419-2345092cf183
relation.isAuthorOfPublication0f32c437-6c87-47d7-998b-c97c4695806a
relation.isAuthorOfPublication.latestForDiscovery63f1faff-64dd-41b7-9419-2345092cf183
relation.isProjectOfPublication1443abcf-d4c7-4fad-a89c-fe502f9332e5
relation.isProjectOfPublication83416f0b-2448-4873-b231-0c31887c5a05
relation.isProjectOfPublication.latestForDiscovery1443abcf-d4c7-4fad-a89c-fe502f9332e5

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