Publicação:
Bacterial and Arachnid Sphingomyelinases D: Comparison of Biophysical and Pathological Activities

dc.contributor.authorMariutti, Ricardo Barros [UNESP]
dc.contributor.authorChaves-Moreira, Daniele
dc.contributor.authorVuitika, Larissa
dc.contributor.authorCaruso, Ícaro Putinhon [UNESP]
dc.contributor.authorCoronado, Monika A. [UNESP]
dc.contributor.authorAzevedo, Vasco A.
dc.contributor.authorMurakami, Mario T.
dc.contributor.authorVeiga, Silvio Sanches
dc.contributor.authorArni, Raghuvir K. [UNESP]
dc.contributor.institutionUniversidade Estadual Paulista (Unesp)
dc.contributor.institutionUniversidade Federal do Paraná (UFPR)
dc.contributor.institutionUniversidade Federal de Minas Gerais (UFMG)
dc.contributor.institutionLNBio
dc.date.accessioned2018-12-11T16:47:11Z
dc.date.available2018-12-11T16:47:11Z
dc.date.issued2017-08-01
dc.description.abstractSphingomyelinases D have only been identified in arachnid venoms, Corynebacteria, Arcanobacterium, Photobacterium and in the fungi Aspergillus and Coccidioides. The arachnid and bacterial enzymes share very low sequence identity and do not contain the HKD sequence motif characteristic of the phospholipase D superfamily, however, molecular modeling and circular dichroism of SMases D from Loxosceles intermedia and Corynebacterium pseudotuberculosis indicate similar folds. The phospholipase, hemolytic and necrotic activities and mice vessel permeabilities were compared and both enzymes possess the ability to hydrolyze phospholipids and also promote similar pathological reactions in the host suggesting the existence of a common underlying mechanism in tissue disruption. J. Cell. Biochem. 118:2053–2063, 2017. © 2016 Wiley Periodicals, Inc.en
dc.description.affiliationDepartment of Physics Multiuser Center for Biomolecular Innovation UNESP
dc.description.affiliationDepartment of Cell Biology UFPR
dc.description.affiliationInstitute of Biological Sciences UFMG
dc.description.affiliationBrazilian Biosciences National Laboratory LNBio
dc.description.affiliationUnespDepartment of Physics Multiuser Center for Biomolecular Innovation UNESP
dc.description.sponsorshipCoordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)
dc.description.sponsorshipConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
dc.description.sponsorshipFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
dc.description.sponsorshipFinanciadora de Estudos e Projetos
dc.description.sponsorshipFundação Araucária
dc.format.extent2053-2063
dc.identifierhttp://dx.doi.org/10.1002/jcb.25781
dc.identifier.citationJournal of Cellular Biochemistry, v. 118, n. 8, p. 2053-2063, 2017.
dc.identifier.doi10.1002/jcb.25781
dc.identifier.issn1097-4644
dc.identifier.issn0730-2312
dc.identifier.lattes9162508978945887
dc.identifier.orcid0000-0003-2460-1145
dc.identifier.scopus2-s2.0-85018800378
dc.identifier.urihttp://hdl.handle.net/11449/169688
dc.language.isoeng
dc.relation.ispartofJournal of Cellular Biochemistry
dc.relation.ispartofsjr1,209
dc.relation.ispartofsjr1,209
dc.rights.accessRightsAcesso restrito
dc.sourceScopus
dc.subjectCATALYSIS
dc.subjectDERMONECROSIS
dc.subjectHEMOLYSIS
dc.subjectSPHINGOMYELINASE D
dc.titleBacterial and Arachnid Sphingomyelinases D: Comparison of Biophysical and Pathological Activitiesen
dc.typeArtigo
dspace.entity.typePublication
unesp.author.lattes9162508978945887[9]
unesp.author.orcid0000-0003-2460-1145[9]

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