Lipase-like 5 enzyme controls mitochondrial activity in response to starvation in Caenorhabditis elegans

Autor(es):Mostrar menos -

Macedo, Felipe ^[1] ; Martins, Gabriel Loureiro ^{[1, 2]} ; Luevano-Martinez, Luis A. ^[3] ; Viana, Gustavo Monteiro ^[1] ; Riske, Karin A. ^[4] ; Inague, Alex ^[5] ; Yoshinaga, Marcos Y. ^[5] ; Aguilaniu, Hugo ^{[6, 7]} ; Miyamoto, Sayuri ^[5] ; Glezer, Isaias ^[1] ; da Cunha, Fernanda Marques ^[1]

Afiliação do(s) autor(es)

^[1] Univ Fed Sao Paulo, Dept Bioquim, Escola Paulista Med, Rua Tres Maio 100, BR-04044020 Sao Paulo, SP - Brazil

^[2] Univ Sao Paulo, Escola Educ Fis & Esporte, Ave Prof Mello Moraes 65, BR-05508030 Sao Paulo, SP - Brazil

^[3] Univ Sao Paulo, Dept Parasitol, Inst Ciencias Biomed, Ave Prof Lineu Prestes 1374, BR-05508900 Sao Paulo, SP - Brazil

^[4] Univ Fed Sao Paulo, Escola Paulista Med, Dept Biofis, Rua Pedro Toledo, Rua Pedro Toledo 669, BR-04039032 Sao Paulo, SP - Brazil

^[5] Univ Sao Paulo, Inst Quim, Dept Bioquim, Ave Prof Lineu Prestes 748, BR-05508000 Sao Paulo, SP - Brazil

^[6] CNRS, Paris - France

^[7] Inst Serrapilheira, Rua Dias Ferreira 78 S202, BR-22431050 Rio De Janeiro, RJ - Brazil

• Tipo de documento: Artigo Científico
• Fonte: BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR AND CELL BIOLOGY OF LIPIDS; v. 1865, n. 2 FEB 2020.
• Citações Web of Science: 0

Resumo

The C. elegans lipase-like 5 (lipl-5) gene is predicted to code for a lipase homologous to the human gastric acid lipase. Its expression was previously shown to be modulated by nutritional or immune cues, but nothing is known about its impact on the lipid landscape and ensuing functional consequences. In the present work, we used mutants lacking LIPL-5 protein and found that lipl-5 is important for normal lipidome composition as well as its remodeling in response to food deprivation. Particularly, lipids with signaling functions such as ceramides and mitochondrial lipids were affected by lipl-5 silencing. In comparison with wild type worms, animals lacking LIPL-5 were enriched in cardiolipins linked to polyunsaturated C20 fatty acids and coenzyme Q-9. Differences in mitochondrial lipid composition were accompanied by differences in mitochondrial activity as mitochondria from well-fed lipl-5 mutants were significantly more able to oxidize respiratory substrates when compared with mitochondria from well-fed wild type worms. Strikingly, starvation elicited important changes in mitochondrial activity in wild type worms, but not in lipl-5 worms. This indicates that this lipase is a determinant of mitochondrial functional remodeling in response to food withdrawal. (AU)

• Processo FAPESP: 16/12999-0 - Evolução da via de síntese da cardiolipina: implicações bioquímicas na evolução do domínio Eukarya
• Beneficiário: Luis Alberto Luevano Martinez
• Modalidade de apoio: Auxílio à Pesquisa - Jovens Pesquisadores
• Processo FAPESP: 13/07937-8 - Redoxoma
• Beneficiário: Ohara Augusto
• Modalidade de apoio: Auxílio à Pesquisa - Centros de Pesquisa, Inovação e Difusão - CEPIDs
• Processo FAPESP: 15/15526-3 - Estudo do envolvimento da atividade mitocondrial na super-resposta à restrição calórica em Caenorhabditis elegans mutantes para lipl-5
• Beneficiário: Fernanda Marques da Cunha
• Modalidade de apoio: Auxílio à Pesquisa - Regular
• Processo FAPESP: 16/21778-8 - Evolução da via de síntese da cardiolipina: Implicações bioquímicas na evolução do domínio Eukarya.
• Beneficiário: Luis Alberto Luevano Martinez
• Modalidade de apoio: Bolsas no Brasil - Jovens Pesquisadores