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Bacterial and Arachnid Sphingomyelinases D: Comparison of Biophysical and Pathological Activities.
Mariutti, Ricardo Barros; Chaves-Moreira, Daniele; Vuitika, Larissa; Caruso, Ícaro Putinhon; Coronado, Monika A; Azevedo, Vasco A; Murakami, Mario T; Veiga, Silvio Sanches; Arni, Raghuvir K.
Afiliação
  • Mariutti RB; Department of Physics, Multiuser Center for Biomolecular Innovation, UNESP, São José do Rio Preto, SP, Brazil.
  • Chaves-Moreira D; Department of Cell Biology, UFPR, Curitiba, PR, Brazil.
  • Vuitika L; Department of Cell Biology, UFPR, Curitiba, PR, Brazil.
  • Caruso ÍP; Department of Physics, Multiuser Center for Biomolecular Innovation, UNESP, São José do Rio Preto, SP, Brazil.
  • Coronado MA; Department of Physics, Multiuser Center for Biomolecular Innovation, UNESP, São José do Rio Preto, SP, Brazil.
  • Azevedo VA; Institute of Biological Sciences, UFMG, Belo Horizonte, MG, Brazil.
  • Murakami MT; Brazilian Biosciences National Laboratory, LNBio, Campinas, SP, Brazil.
  • Veiga SS; Department of Cell Biology, UFPR, Curitiba, PR, Brazil.
  • Arni RK; Department of Physics, Multiuser Center for Biomolecular Innovation, UNESP, São José do Rio Preto, SP, Brazil.
J Cell Biochem ; 118(8): 2053-2063, 2017 08.
Article em En | MEDLINE | ID: mdl-27808444
ABSTRACT
Sphingomyelinases 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. 1182053-2063, 2017. © 2016 Wiley Periodicals, Inc.
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Texto completo: 1 Base de dados: MEDLINE Assunto principal: Aranhas / Proteínas de Bactérias / Permeabilidade Capilar / Corynebacterium pseudotuberculosis / Diester Fosfórico Hidrolases / Proteínas de Artrópodes Tipo de estudo: Prognostic_studies Limite: Animals / Humans Idioma: En Ano de publicação: 2017 Tipo de documento: Article

Texto completo: 1 Base de dados: MEDLINE Assunto principal: Aranhas / Proteínas de Bactérias / Permeabilidade Capilar / Corynebacterium pseudotuberculosis / Diester Fosfórico Hidrolases / Proteínas de Artrópodes Tipo de estudo: Prognostic_studies Limite: Animals / Humans Idioma: En Ano de publicação: 2017 Tipo de documento: Article