Skip Navigation


Journal of Biochemistry Advance Access originally published online on August 30, 2007
Journal of Biochemistry 2007 142(4):453-458; doi:10.1093/jb/mvm159
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow All Versions of this Article:
142/4/453    most recent
mvm159v1
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrow Request Permissions
Google Scholar
Right arrow Articles by Yoshino, K.
Right arrow Articles by Ogishima, T.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Yoshino, K.
Right arrow Articles by Ogishima, T.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

© 2007 The Japanese Biochemical Society.

Haeme-regulated Degradation of {delta}-Aminolevulinate Synthase 1 in Rat Liver Mitochondria

Kazuhisa Yoshino1, Hiroshi Munakata2, Osamu Kuge1, Akio Ito1 and Tadashi Ogishima1,*

1Department of Chemistry, Faculty of Science, Kyushu University, Fukuoka, 812-8581, Japan; and 2Department of Biochemistry, School of Medicine, Kinki University, 377-2 Ohno-Higashi, Osaka-Sayama, 589-8511, Japan

*To whom correspondence should be addressed. Tel: +81-92-642-2601, Fax: +81-91-642-2607, E-mail: taogiscc{at}mbox.nc.kyushu-u.ac.jp

Received May 2, 2007; Accepted June 26, 2007


  Abstract

Protein turnover, which occurs at various rates, is critical for the homeostasis of cellular protein levels. However, the proteolysis systems that determine the turnover rate of mitochondrial proteins are largely unknown. Delta-aminolevulinic acid synthase (ALAS) 1, a rate-limiting enzyme in the haeme biosynthesis, is one of the mitochondrial proteins that have a very short lifetime. In this study, to reveal the regulatory mechanisms for ALAS1 degradation, we examined the turnover rates of ALAS1 in rat liver under several conditions. In primary rat hepatocytes, the degradation of ALAS1 was stimulated by haeme, and suppressed by inhibition of haeme biosynthesis. Furthermore, the haeme-stimulated degradation of ALAS1 was observed in the isolated mitochondria. These results suggested that, in mitochondria, there exists an ALAS1 degradation system that is regulated by cellular haeme level and plays a crucial role in the regulation of haeme biosynthesis.

Key Words: ALAS1, haeme and metabolism, metabolic regulation, mitochondria, protein degradation

Abbreviations: ALAS, {delta}-aminolevulinic acid synthase; Bt2cAMP, dibutyryladenosine 3',5'-cyclic monophosphate; CHI, cycloheximide; DDC, 3,5-dicarbethoxy-1,4-dihydrocollidine; MSH, mannitol–sucrose–Hepes; PB, phenobarbital; SA, succinylacetone; TOM40, translocase of outer membrane


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?


This article has been cited by other articles:


Home page
 J. Biol. Chem.Home page
L. Yi, P. M. Jenkins, L. I. Leichert, U. Jakob, J. R. Martens, and S. W. Ragsdale
Heme Regulatory Motifs in Heme Oxygenase-2 Form a Thiol/Disulfide Redox Switch That Responds to the Cellular Redox State
J. Biol. Chem., July 31, 2009; 284(31): 20556 - 20561.
[Abstract] [Full Text] [PDF]


Disclaimer: Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.