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dc.creatorGuardia, Carlos Manuel Alberto-
dc.creatorCaramelo, Julio Javier-
dc.creatorTrujillo, Madia-
dc.creatorMendez Huergo, Santiago Patricio-
dc.creatorRadi, Rafael-
dc.creatorEstrin, Dario Ariel-
dc.creatorRabinovich, Gabriel Adrian-
dc.date2016-07-04T17:22:04Z-
dc.date2016-07-04T17:22:04Z-
dc.date2014-05-
dc.date2016-06-15T19:12:15Z-
dc.date.accessioned2019-04-29T15:49:09Z-
dc.date.available2019-04-29T15:49:09Z-
dc.date.issued2014-05-
dc.identifierGuardia, Carlos Manuel Alberto; Caramelo, Julio Javier; Trujillo, Madia ; Mendez Huergo, Santiago Patricio; Radi, Rafael ; et al.; Structural basis of redox-dependent modulation of galectin-1 dynamics and function; Oxford University Press; Glycobiology; 24; 5; 5-2014; 428-441-
dc.identifier0959-6658-
dc.identifierhttp://hdl.handle.net/11336/6329-
dc.identifier.urihttp://rodna.bn.gov.ar:8080/jspui/handle/bnmm/302874-
dc.descriptionGalectin-1 (Gal-1), a member of a family of multifunctional lectins, plays key roles in diverse biological processes including cell signaling, immunomodulation, neuroprotection and angiogenesis. The presence of an unusual number of six cysteine residues within Gal-1 sequence prompted a detailed analysis of the impact of the redox environment on the functional activity of this lectin. We examined the role of each cysteine residue in the structure and function of Gal-1 using both experimental and computational approaches. Our results show that: (i) only three cysteine residues present in each carbohydrate recognition domain (CRD) (Cys2, Cys16 and Cys88) were important in protein oxidation, (ii) oxidation promoted the formation of the Cys16-Cys88 disulfide bond, as well as multimers through Cys2, (iii) the oxidized protein did not bind to lactose, probably due to poor interactions with Arg48 and Glu71, (iv) in vitro oxidation by air was completely reversible and (v) oxidation by hydrogen peroxide was relatively slow (1.7 ± 0.2 M(-1) s(-1) at pH 7.4 and 25°C). Finally, an analysis of key cysteines in other human galectins is also provided in order to predict their behaviour in response to redox variations. Collectively, our data provide new insights into the structural basis of Gal-1 redox regulation with critical implications in physiology and pathology.-
dc.descriptionFil: Guardia, Carlos Manuel Alberto. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química, Física de Los Materiales, Medioambiente y Energía; Argentina. Universidad de Buenos Aires; Argentina-
dc.descriptionFil: Caramelo, Julio Javier. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Química Biológica; Argentina-
dc.descriptionFil: Trujillo, Madia . Universidad de la Republica; Uruguay-
dc.descriptionFil: Mendez Huergo, Santiago Patricio. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Biología y Medicina Experimental (i); Argentina-
dc.descriptionFil: Radi, Rafael . Universidad de la Republica; Uruguay-
dc.descriptionFil: Estrin, Dario Ariel. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química, Física de Los Materiales, Medioambiente y Energía; Argentina-
dc.descriptionFil: Rabinovich, Gabriel Adrian. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Biología y Medicina Experimental (i); Argentina. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Química Biológica; Argentina-
dc.formatapplication/pdf-
dc.formatapplication/pdf-
dc.formatapplication/pdf-
dc.formatapplication/pdf-
dc.formatapplication/pdf-
dc.languageeng-
dc.publisherOxford University Press-
dc.relationinfo:eu-repo/semantics/altIdentifier/doi/10.1093/glycob/cwu008-
dc.relationinfo:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1093/glycob/cwu008-
dc.relationinfo:eu-repo/semantics/altIdentifier/url/http://glycob.oxfordjournals.org/content/24/5/428.long-
dc.relationinfo:eu-repo/semantics/altIdentifier/url/http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3976282/-
dc.relationinfo:eu-repo/semantics/altIdentifier/pmid/PMC3976282-
dc.rightsinfo:eu-repo/semantics/openAccess-
dc.rightshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/-
dc.sourcereponame:CONICET Digital (CONICET)-
dc.sourceinstname:Consejo Nacional de Investigaciones Científicas y Técnicas-
dc.sourceinstacron:CONICET-
dc.source.urihttp://hdl.handle.net/11336/11119-
dc.subjectCIRCULAR DICHROISM-
dc.subjectCYSTEINE-
dc.subjectGALECTIN-1-
dc.subjectMOLECULAR DYNAMICS-
dc.subjectOXIDATION-
dc.subjectBioquímica y Biología Molecular-
dc.subjectCiencias Biológicas-
dc.subjectCIENCIAS NATURALES Y EXACTAS-
dc.subjectBiofísica-
dc.subjectCiencias Biológicas-
dc.subjectCIENCIAS NATURALES Y EXACTAS-
dc.subjectInmunología-
dc.subjectMedicina Básica-
dc.subjectCIENCIAS MÉDICAS Y DE LA SALUD-
dc.titleStructural basis of redox-dependent modulation of galectin-1 dynamics and function-
dc.typeinfo:eu-repo/semantics/article-
dc.typeinfo:eu-repo/semantics/publishedVersion-
dc.typeinfo:ar-repo/semantics/articulo-
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