2014年10月
Degradation of acetoacetyl-CoA synthetase, a ketone body-utilizing enzyme, by legumain in the mouse kidney
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
- ,
- ,
- 巻
- 453
- 号
- 3
- 開始ページ
- 631
- 終了ページ
- 635
- 記述言語
- 英語
- 掲載種別
- 研究論文(学術雑誌)
- DOI
- 10.1016/j.bbrc.2014.09.130
- 出版者・発行元
- ACADEMIC PRESS INC ELSEVIER SCIENCE
Acetoacetyl-CoA synthetase (AACS) is a ketone body-utilizing enzyme, which is responsible for the synthesis of cholesterol and fatty acids from ketone bodies in lipogenic tissues, such as the liver and adipocytes. To explore the possibility of AACS regulation at the protein-processing level, we investigated the proteolytic degradation of AACS. Western blot analysis showed that the 75.1 kDa AACS was cleaved to form a protein of approximately 55 kDa in the kidney, which has considerable high activity of legumain, a lysosomal asparaginyl endopeptidase. Co-expression of AACS and legumain in HEK 293 cells generated the 55 kDa product from AACS. Moreover, incubation of recombinant AACS with recombinant legumain resulted in the degradation of AACS. Knockdown of legumain with short-hairpin RNA against legumain using the hydrodynamics method led to a decrease in the 55 kDa band of AACS in mouse kidney. These results suggest that legumain is involved in the processing of AACS through the lysosomal degradation pathway in the kidney. (C) 2014 Elsevier Inc. All rights reserved.
- リンク情報
- ID情報
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- DOI : 10.1016/j.bbrc.2014.09.130
- ISSN : 0006-291X
- eISSN : 1090-2104
- PubMed ID : 25301556
- Web of Science ID : WOS:000350267500057