| Full text | |
| Author(s): |
Pimentel, Andre C.
;
Fuzita, Felipe J.
;
Palmisano, Giuseppe
;
Ferreira, Celia
;
Terra, Walter R.
Total Authors: 5
|
| Document type: | Journal article |
| Source: | COMPARATIVE BIOCHEMISTRY AND PHYSIOLOGY B-BIOCHEMISTRY & MOLECULAR BIOLOGY; v. 204, p. 45-52, FEB 2017. |
| Web of Science Citations: | 9 |
| Abstract | |
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 mid gut 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 Land 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. (C) 2016 Elsevier Inc. All rights reserved. (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 |