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Non-Mammalian Prdx6 Enzymes (Proteins with 1-Cys Prdx Mechanism) Display PLA(2) Activity Similar to the Human Orthologue

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Autor(es):
Bannitz-Fernandes, Renata [1] ; Aleixo-Silva, Rogerio [1] ; Silva, Joao Paulo [1] ; Dodia, Chandra [2] ; Vazquez-Medina, Jose Pablo [3, 2] ; Tao, Jian-Qin [2] ; Fisher, Aron [2] ; Netto, Luis [1]
Número total de Autores: 8
Afiliação do(s) autor(es):
[1] Univ Sao Paulo, Inst Biociencias, Dept Genet & Biol Evolut, BR-05508090 Sao Paulo, SP - Brazil
[2] Univ Penn, Perelman Sch Med, Inst Environm Med, Dept Physiol, Philadelphia, PA 19104 - USA
[3] Univ Calif Berkeley, Dept Integrat Biol, Berkeley, CA 94720 - USA
Número total de Afiliações: 3
Tipo de documento: Artigo Científico
Fonte: ANTIOXIDANTS; v. 8, n. 3 MAR 1 2019.
Citações Web of Science: 1
Resumo

Mammalian peroxiredoxin class 6 (Prdx6) are bifunctional enzymes. Non-mammalian Prdx6 enzymes display Cys-based peroxidase activity, but to date their putative phospholipase A(2) (PLA(2) activities) has not been experimentally investigated. Initially, we observed that five non-mammalian Prdx6 enzymes (enzymes from Arabidopsis thaliana (AtPER1), Triticum aestivum (TaPER1), Pseudomonas aeruginosa (PaLsfA) and Aspergillus fumigatus (AfPrx1 and AfPrxC)) present features compatible with PLA(2) activities in mammalian Prdx6 by amino acid sequences alignment and tertiary structure modeling. Employing unilamellar liposomes with tracer amounts of {[}H-3]-1,2-Dipalmitoyl-sn-glycero-3-phosphocholine (DPPC) and thin layer chromatography, all the tested non-mammalian Prdx6 enzymes displayed PLA(2) activities, with values ranging from 3.4 to 6.1 nmol/min/mg protein. It was previously shown that Thr177 phosphorylation of human Prdx6 increases its PLA(2) activity, especially at neutral pH. Therefore, we investigated if human Erk2 kinase could also phosphorylate homologous Thr residues in non-mammalian Prdx6 proteins. We observed phosphorylation of the conserved Thr in three out of the five non-mammalian Prdx enzymes by mass spectrometry. In the case of the mitochondrial Prdx6 from A. fumigatus (AfPrxC), we also observed phosphorylation by western blot, and as a consequence, the PLA(2) activity was increased in acidic and neutral conditions by the human Erk2 kinase treatment. The possible physiological meanings of these PLA(2) activities described open new fields for future research. (AU)

Processo FAPESP: 16/12248-5 - Identificação e caracterização da atividade de fosfolipase A2 independente de Ca2 (aiPLA2) de três peroxirredoxinas do fungo patógeno humano Aspergillus fumigatus
Beneficiário:Renata Bannitz Fernandes
Linha de fomento: Bolsas no Exterior - Estágio de Pesquisa - Doutorado Direto
Processo FAPESP: 13/07937-8 - Redoxoma
Beneficiário:Ohara Augusto
Linha de fomento: Auxílio à Pesquisa - Centros de Pesquisa, Inovação e Difusão - CEPIDs