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A proteomic approach to identify digestive enzymes, their exocytic and microapocrine secretory routes and their compartmentalization in the midgut of Spodoptera frugiperda.
Fuzita, Felipe J; Palmisano, Giuseppe; Pimenta, Daniel C; Terra, Walter R; Ferreira, Clélia.
Afiliação
  • Fuzita FJ; Departamento de Bioquímica, Instituto de Química, Universidade de São Paulo, Avenida Professor Lineu Prestes, 748, São Paulo 05508-000, Brazil.
  • Palmisano G; Departamento de Parasitologia, Instituto de Ciências Biomédicas, Universidade de São Paulo, 05508-000 São Paulo, Brazil.
  • Pimenta DC; Laboratório de Bioquímica e Biofísica, Instituto Butantan, Avenida Vital Brasil, 1500, São Paulo 05503-900, Brazil.
  • Terra WR; Departamento de Bioquímica, Instituto de Química, Universidade de São Paulo, Avenida Professor Lineu Prestes, 748, São Paulo 05508-000, Brazil.
  • Ferreira C; Departamento de Bioquímica, Instituto de Química, Universidade de São Paulo, Avenida Professor Lineu Prestes, 748, São Paulo 05508-000, Brazil. Electronic address: clfterra@iq.usp.br.
Comp Biochem Physiol B Biochem Mol Biol ; 257: 110670, 2022 Jan.
Article em En | MEDLINE | ID: mdl-34438074
A proteomic approach was used to identify the digestive enzymes secreted by exocytosis and by microapocrine vesicles and enzyme midgut compartmentalization in Spodoptera frugiperda larvae. For this, proteomic analyses were performed in isolated midgut enterocyte microvillar membrane, in a fraction enriched in microapocrine vesicles (separated in soluble and membrane fractions), in the washings of the peritrophic membrane to isolate its loosely- and tightly-bound proteins, and in the peritrophic membrane contents. PM washings correspond to proteins extracted from the mucus layer surrounding PM. Serine endopeptidases (trypsins, chymotrypsins and serine endopeptidase homologs that have substitutions in the catalytic residues) and lipases are mainly secreted by exocytosis. Aminopeptidases are mainly microvillar enzymes and some are secreted membrane-bound to microapocrine vesicles, whereas carboxypeptidase isoforms follow different secretory routes. The results also showed that most polymer hydrolases (such as amylase and endopeptidases) are not retained in the ectoperitrophic fluid (found in PM washings but absent from PM contents). On the contrary, most enzymes involved in intermediate digestion (exemplified by carboxypeptidase and aminopeptidase) do not pass through the peritrophic membrane. Finally, the data revealed that the protein composition of PM includes peritrophins classified as peritrophic membrane proteins, PMP, and chitin deacetylase.
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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Proteínas de Insetos / Proteômica Limite: Animals Idioma: En Revista: Comp Biochem Physiol B Biochem Mol Biol Assunto da revista: BIOLOGIA MOLECULAR / BIOQUIMICA Ano de publicação: 2022 Tipo de documento: Article País de afiliação: Brasil País de publicação: Reino Unido
Texto completo
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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Proteínas de Insetos / Proteômica Limite: Animals Idioma: En Revista: Comp Biochem Physiol B Biochem Mol Biol Assunto da revista: BIOLOGIA MOLECULAR / BIOQUIMICA Ano de publicação: 2022 Tipo de documento: Article País de afiliação: Brasil País de publicação: Reino Unido