Endocytosis of pulchellin and its recombinant B-chain into K-562 cells: Binding and uptake studies

dc.contributor.authorGoto, Leandro S.
dc.contributor.authorCastilho, Priscila V.
dc.contributor.authorCominetti, Marcia R.
dc.contributor.authorSelistre-Araujo, Heloisa S.
dc.contributor.authorAraujo, Ana Paula Ulian
dc.contributor.institutionUniversidade de São Paulo (USP)
dc.contributor.institutionUniversidade Federal de São Paulo (UNIFESP)
dc.date.accessioned2016-01-24T13:49:14Z
dc.date.available2016-01-24T13:49:14Z
dc.date.issued2007-12-01
dc.description.abstractMost of the type 2 ribosome-inactivating proteins (RIPs) are toxins formed by an RNA-N-glycosidase A-chain polypeptide linked to a lectin B-chain by a single disulfide bond. Members of this protein class vary greatly in cytotoxity, correlating more with B-chain diversity rather than to A-chain differences. Pulchellin is a type 2 ribosome-inactivating protein toxin found in the seeds of Abrus pulchellus tenuiflorus. Recombinant pulchellin B-Chain (rPBC) has been previously produced as inclusion bodies in Escherichia coli and successfully refolded recovering biological activity. New approaches for using this kind of protein as a biotechnological tool require a better understanding of cell targeting, binding, uptake, intracellular routing and delivery. in this work, cell adhesion experiments were used to determine the interaction of rPBC with mammalian cells. Fluorescence and confocal microscopy revealed the intracellular localization and trafficking. Subcellular sorting of the native pulchellin could also be determined. the results support that the endosomal internalization pathway and the retrograde transport through the Golgi apparatus might be used by both native protein and rPBC. (C) 2007 Elsevier B.V. All rights reserved.en
dc.description.affiliationUniv São Paulo, Ctr Biotechnol Mol Estruct, Inst Fis Sao Carlos, Sao Carlos, SP, Brazil
dc.description.affiliationUniversidade Federal de São Paulo, Program Pos Grad Genet & Evol, Sao Carlos 13560, Brazil
dc.description.affiliationUniversidade Federal de São Paulo, Dept Ciencias Fisiol, Sao Carlos, Brazil
dc.description.affiliationUnifespUniversidade Federal de São Paulo, Program Pos Grad Genet & Evol, Sao Carlos 13560, Brazil
dc.description.affiliationUnifespUniversidade Federal de São Paulo, Dept Ciencias Fisiol, Sao Carlos, Brazil
dc.description.sourceWeb of Science
dc.format.extent1660-1666
dc.identifierhttp://dx.doi.org/10.1016/j.bbagen.2007.08.011
dc.identifier.citationBiochimica Et Biophysica Acta-general Subjects. Amsterdam: Elsevier B.V., v. 1770, n. 12, p. 1660-1666, 2007.
dc.identifier.doi10.1016/j.bbagen.2007.08.011
dc.identifier.issn0304-4165
dc.identifier.urihttp://repositorio.unifesp.br/handle/11600/30178
dc.identifier.wosWOS:000251120100009
dc.language.isoeng
dc.publisherElsevier B.V.
dc.relation.ispartofBiochimica Et Biophysica Acta-general Subjects
dc.rightsAcesso restrito
dc.rights.licensehttp://www.elsevier.com/about/open-access/open-access-policies/article-posting-policy
dc.subjectribosome-inactivating proteinen
dc.subjectpulchellinen
dc.subjectendocytosisen
dc.subjectplant toxinen
dc.titleEndocytosis of pulchellin and its recombinant B-chain into K-562 cells: Binding and uptake studiesen
dc.typeArtigo
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