Document Detail


Cathepsin D-mediated yolk protein degradation is blocked by acid phosphatase inhibitors.
MedLine Citation:
PMID:  15797237     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Vitellin (VT) is a lipoglycophosphoprotein stored inside the eggs of every oviparous organism during oogenesis. In the blood-sucking bug Rhodnius prolixus, VT is deposited inside growing oocytes together with two acid hydrolases: acid phosphatase (AP) and cathepsin D (CD). Egg fertilization triggers AP activity and VT proteolysis in vivo [Insect Biochem. Mol. Biol. 2002 (32) 847]. Here, we show that CD is the main protease targeting VT proteolysis during egg development. CD activity in total egg homogenates is blocked by the classical aspartyl protease inhibitor, pepstatin A. Surprisingly, AP inhibitors such as NaF, Na+/K+ tartrate, and inorganic phosphate also block VT proteolysis, whereas this effect is not observed when tyrosine phosphatase inhibitors such as vanadate and phenylarsine oxide or an inhibitor of alkaline phosphatases such as levamisole are used in a VT proteolysis assay. NaF concentrations that block isolated AP activity do not affect the activity of partially purified CD. Therefore, a specific repressor of VT proteolysis must be dephosphorylated by AP in vivo. In conclusion, these results demonstrate for the first time that acid hydrolases act cooperatively to promote yolk degradation during egg development in arthropods.
Authors:
Eliane Fialho; Angelica Nakamura; Luiz Juliano; Hatisaburo Masuda; Mário A C Silva-Neto
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Archives of biochemistry and biophysics     Volume:  436     ISSN:  0003-9861     ISO Abbreviation:  Arch. Biochem. Biophys.     Publication Date:  2005 Apr 
Date Detail:
Created Date:  2005-03-30     Completed Date:  2005-05-24     Revised Date:  2007-11-15    
Medline Journal Info:
Nlm Unique ID:  0372430     Medline TA:  Arch Biochem Biophys     Country:  United States    
Other Details:
Languages:  eng     Pagination:  246-53     Citation Subset:  IM    
Affiliation:
Instituto de Bioquímica Médica, Centro de Ciências da Saúde, Universidade Federal do Rio de Janeiro, UFRJ, P.O. Box 68041, Cidade Universitária, Rio de Janeiro, CEP 21941-590, RJ, Brazil.
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MeSH Terms
Descriptor/Qualifier:
Acid Phosphatase / antagonists & inhibitors,  chemistry,  metabolism
Alkaline Phosphatase / metabolism
Animals
Cathepsin D / chemistry,  metabolism*
Cathepsins / chemistry
Egg Proteins / metabolism*
Electrophoresis, Polyacrylamide Gel
Hydrogen-Ion Concentration
Hydrolases / chemistry
Insects / metabolism
Oocytes / metabolism
Oogenesis
Phosphoproteins / chemistry
Phosphoric Monoester Hydrolases / chemistry
Phosphorylation
Protein Tyrosine Phosphatases / chemistry,  metabolism
Rhodnius / metabolism
Sodium / chemistry
Tartrates / chemistry
Temperature
Time Factors
Vitellins / chemistry
Chemical
Reg. No./Substance:
0/Egg Proteins; 0/Phosphoproteins; 0/Tartrates; 0/Vitellins; 526-83-0/tartaric acid; 7440-23-5/Sodium; EC 3.-/Hydrolases; EC 3.1.3.-/Phosphoric Monoester Hydrolases; EC 3.1.3.1/Alkaline Phosphatase; EC 3.1.3.2/Acid Phosphatase; EC 3.1.3.48/Protein Tyrosine Phosphatases; EC 3.4.-/Cathepsins; EC 3.4.23.5/Cathepsin D

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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