Accumulation and translation of ferritin heavy chain transcripts following anoxia exposure in a marine invertebrate
Author:
Larade Kevin1, Storey Kenneth B.1
Affiliation:
1. Institute of Biochemistry and Department of Biology, Carleton University, 1125 Colonel By Drive, Ottawa, Ontario, Canada, K1S 5B6
Abstract
SUMMARYDifferential screening of a Littorina littorea (the common periwinkle) cDNA library identified ferritin heavy chain as an anoxia-induced gene in hepatopancreas. Northern blots showed that ferritin heavy chain transcript levels were elevated twofold during anoxia exposure, although nuclear run-off assays demonstrated that ferritin heavy chain mRNAs were not transcriptionally upregulated during anoxia. Polysome analysis indicated that existing ferritin transcripts were actively translated during the anoxic period. This result was confirmed via western blotting, which demonstrated a twofold increase in ferritin heavy chain protein levels during anoxia, with a subsequent decrease to control levels during normoxic recovery. Organ culture experiments using hepatopancreas slices demonstrated a >50%increase in ferritin heavy chain transcript levels in vitro under conditions of anoxia and freezing, as well as after incubation with the second messenger cGMP. Taken together, these results suggest that ferritin heavy chain is actively regulated during anoxia exposure in the marine snail, L. littorea.
Publisher
The Company of Biologists
Subject
Insect Science,Molecular Biology,Animal Science and Zoology,Aquatic Science,Physiology,Ecology, Evolution, Behavior and Systematics
Reference33 articles.
1. Addess, K. J., Basilion, J. P., Klausner, R. D., Rouault, T. A. and Pardi, A. (1997). Structure and dynamics of the iron responsive element RNA: implications for binding of the RNA by iron regulatory binding proteins. J. Mol. Biol.274, 72-83. 2. Ai, L. S. and Chau, L. Y. (1999). Post-transcriptional regulation of H-ferritin mRNA. J. Biol. Chem.274,30209-30214. 3. Anderson, O., Dehli, A., Standal, H., Giskegjerde, T. A.,Karstensen, R. and Rorvik, K. A. (1995). Two ferritin subunits of Atlantic salmon (Salmo salar): cloning of the liver cDNAs and antibody preparation. Mol. Mar. Biol. Biotechnol.4, 164-170. 4. Berberat, P. O., Katori, M., Kaczmarek, E., Anselmo, D.,Lassman, C., Ke, B., Shen, X., Busuttil, R. W., Yamashita, K.,Csizmadia, E. et al. (2003). Heavy chain ferritin acts as an anti-apoptotic gene that protects livers from ischemia-reperfusion injury. FASEB J.17,1724-1726. 5. Charlesworth, A., Georgieva, T., Gospodov, I., Law, J. H.,Dunkov, B. C., Ralcheva, N., Barillas-Mury, C., Ralchev, K. and Karatos, F. C. (1997). Isolation and properties of Drosophila melanogaster ferritin: Molecular cloning of a cDNA that encodes one subunit, and localization of the gene on the third chromosome. Eur. J. Biochem.247,470-475.
Cited by
77 articles.
订阅此论文施引文献
订阅此论文施引文献,注册后可以免费订阅5篇论文的施引文献,订阅后可以查看论文全部施引文献
|
|