| Cathepsin D-mediated yolk protein degradation is blocked by acid phosphatase inhibitors. | |
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MedLine Citation:
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PMID: 15797237 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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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. |
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Authors:
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Eliane Fialho; Angelica Nakamura; Luiz Juliano; Hatisaburo Masuda; Mário A C Silva-Neto |
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Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't |
Journal Detail:
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Title: Archives of biochemistry and biophysics Volume: 436 ISSN: 0003-9861 ISO Abbreviation: Arch. Biochem. Biophys. Publication Date: 2005 Apr |
Date Detail:
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Created Date: 2005-03-30 Completed Date: 2005-05-24 Revised Date: 2007-11-15 |
Medline Journal Info:
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Nlm Unique ID: 0372430 Medline TA: Arch Biochem Biophys Country: United States |
Other Details:
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Languages: eng Pagination: 246-53 Citation Subset: IM |
Affiliation:
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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:
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Acid Phosphatase
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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:
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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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