Role of cathepsins D in the midgut of Dysdercus peruvianus
| Autor: | Felipe J. Fuzita, Giuseppe Palmisano, Clélia Ferreira, Walter R. Terra, André C. Pimentel |
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| Rok vydání: | 2017 |
| Předmět: |
0301 basic medicine
Physiology Cathepsin L Cathepsin D Biochemistry Cathepsin A Gene Expression Regulation Enzymologic Cathepsin B Cathepsin C Heteroptera 03 medical and health sciences Cathepsin O Animals Computer Simulation Amino Acid Sequence Molecular Biology Cathepsin Gossypium 030102 biochemistry & molecular biology biology Plant Extracts fungi Midgut ENZIMAS 030104 developmental biology Proteolysis Seeds biology.protein Digestive System |
| Zdroj: | Repositório Institucional da USP (Biblioteca Digital da Produção Intelectual) Universidade de São Paulo (USP) instacron:USP |
| ISSN: | 1096-4959 |
| Popis: | Hemipteran ancestors probably lost their digestive serine peptidases on adapting to a plant sap diet. On returning to protein ingestion, these insects start using cathepsin (lysosomal) peptidases as digestive enzymes, from which the less known is cathepsin D. Nine of the ten cathepsin D transcribing genes found in Dysdercus peruvianus midgut are expressed exclusively in this tissue and only DpCatD10 is also expressed in other tissues. The main action of cathepsins D is in the first (V1) (from three, V1-3) midgut regions, where 40% of the total proteolytic activity was assigned to aspartic peptidases with an optimum pH of 3.5. The most expressed cathepsins D were identified in the midgut luminal contents by proteomics. The data indicate that D. peruvianus have kept a lysosomal gene expressed in all tissues and evolved another set of genes with a digestive function restricted to midgut. Digestive cathepsins D apparently complement the action of digestive cathepsin L and they are arguably responsible for the hydrolysis of cysteine peptidase inhibitors known to be present in the cotton seeds eaten by the insect, before they meet cathepsin L. |
| Databáze: | OpenAIRE |
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