| Differential regulation of AMP-activated kinase and AKT kinase in response to oxygen availability in crucian carp (Carassius carassius). | |
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MedLine Citation:
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PMID: 18922957 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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We investigated whether two kinases critical for survival during periods of energy deficiency in anoxia-intolerant mammalian species, AMP-activated kinase (AMPK), and protein kinase B (AKT), are equally important for hypoxic/anoxic survival in the extremely anoxia-tolerant crucian carp (Carassius carassius). We report that phosphorylation of AMPK and AKT in heart and brain showed small changes after 10 days of severe hypoxia (0.3 mg O2/l at 9 degrees C). In contrast, anoxia exposure (0.01 mg O2/l at 8 degrees C) substantially increased AMPK phosphorylation but decreased AKT phosphorylation in carp heart and brain, indicating activation of AMPK and deactivation of AKT. In agreement, blocking the activity of AMPK in anoxic fish in vivo with 20 mg/kg Compound C resulted in an elevated metabolic rate (as indicated by increased ethanol production) and tended to reduce energy charge. This is the first in vivo experiment with Compound C in a nonmammalian vertebrate, and it appears that AMPK plays a role in mediating anoxic metabolic depression in crucian carp. Real-time RT-PCR analysis of the investigated AMPK subunit revealed that the most likely composition of subunits in the carp heart is alpha2, beta1B, gamma2a, whereas a more even expression of subunits was found in the brain. In the heart, expression of the regulatory gamma2-subunit increased in the heart during anoxia. In the brain, expression of the alpha1-, alpha2-, and gamma1-subunits decreased with anoxia exposure, but expression of the gamma2-subunit remained constant. Combined, our findings suggest that AMPK and AKT may play important, but opposing roles for hypoxic/anoxic survival in the anoxia-tolerant crucian carp. |
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Authors:
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Kåre-Olav Stensløkken; Stian Ellefsen; Jonathan A W Stecyk; Mai Britt Dahl; Göran E Nilsson; Jarle Vaage |
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Publication Detail:
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Type: Journal Article Date: 2008-10-15 |
Journal Detail:
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Title: American journal of physiology. Regulatory, integrative and comparative physiology Volume: 295 ISSN: 0363-6119 ISO Abbreviation: Am. J. Physiol. Regul. Integr. Comp. Physiol. Publication Date: 2008 Dec |
Date Detail:
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Created Date: 2008-12-10 Completed Date: 2009-01-22 Revised Date: 2009-11-19 |
Medline Journal Info:
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Nlm Unique ID: 100901230 Medline TA: Am J Physiol Regul Integr Comp Physiol Country: United States |
Other Details:
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Languages: eng Pagination: R1803-14 Citation Subset: IM |
Affiliation:
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Department of Surgery, Ullevål University Hospital, Oslo, Norway. k.o.stenslokken@imbv.uio.no |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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AMP-Activated Protein Kinases
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antagonists & inhibitors,
genetics,
metabolism* Adaptation, Physiological Adenine Nucleotides / metabolism Animals Anoxia / enzymology*, genetics, physiopathology Brain / drug effects, enzymology* Carps / genetics, metabolism* Energy Metabolism Ethanol / metabolism Fish Proteins / genetics, metabolism* Gene Expression Regulation, Enzymologic Myocardium / enzymology* Oxygen / metabolism* Phosphorylation Protein Kinase Inhibitors / pharmacology Protein Subunits Proto-Oncogene Proteins c-akt / metabolism* Pyrazoles / pharmacology Pyrimidines / pharmacology Time Factors |
| Chemical | |
Reg. No./Substance:
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0/(6-(4-(2-piperidin-1-ylethoxy)phenyl))-3-pyridin-4-ylpyrazolo(1,5-a)pyrimidine; 0/Adenine Nucleotides; 0/Fish Proteins; 0/Protein Kinase Inhibitors; 0/Protein Subunits; 0/Pyrazoles; 0/Pyrimidines; 64-17-5/Ethanol; 7782-44-7/Oxygen; EC 2.7.11.1/AMP-Activated Protein Kinases; EC 2.7.11.1/Proto-Oncogene Proteins c-akt |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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