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(Reference retrieved automatically from Web of Science through information on FAPESP grant and its corresponding number as mentioned in the publication by the authors.)

A proteomic approach to identify digestive enzymes, their exocytic and microapocrine secretory routes and their compartmentalization in the midgut of Spodoptera frugiperda

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Author(s):
Fuzita, Felipe J. [1] ; Palmisano, Giuseppe [2] ; Pimenta, Daniel C. [3] ; Terra, Walter R. [1] ; Ferreira, Clelia [1]
Total Authors: 5
Affiliation:
[1] Univ Sao Paulo, Inst Quim, Dept Bioquim, Ave Prof Lineu Prestes 748, BR-05508000 Sao Paulo - Brazil
[2] Univ Sao Paulo, Inst Ciencias Biomed, Dept Parasitol, BR-05508000 Sao Paulo - Brazil
[3] Inst Butantan, Lab Bioquim & Biofis, Ave Vital Brasil 1500, BR-05503900 Sao Paulo - Brazil
Total Affiliations: 3
Document type: Journal article
Source: COMPARATIVE BIOCHEMISTRY AND PHYSIOLOGY B-BIOCHEMISTRY & MOLECULAR BIOLOGY; v. 257, JAN 2022.
Web of Science Citations: 0
Abstract

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. (AU)

FAPESP's process: 14/06863-3 - Post-translational modifications in cancer and parasite infection diagnosis: methodological approaches and biological implications
Grantee:Giuseppe Palmisano
Support Opportunities: Research Grants - Young Investigators Grants
FAPESP's process: 17/08103-4 - Insect digestion: a molecular, cellular, physiological and evolutionary approach
Grantee:Walter Ribeiro Terra
Support Opportunities: Research Projects - Thematic Grants
FAPESP's process: 14/14183-2 - Intestinal microvillar membranes and their secretory vesicles in Lepidoptera Spodoptera frugiperda and Diptera Musca domestica
Grantee:Felipe Jun Fuzita
Support Opportunities: Scholarships in Brazil - Post-Doctoral