Eimre 2008 Biochim Biophys Acta: Difference between revisions
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|authors=Eimre M, Paju K, Pelloux S, Beraud N, Roosimaa M, Kadaja L, Gruno M, Peet N, Orlova E, Remmelkoor R, Piirsoo A, Saks V, Seppet E | |authors=Eimre M, Paju K, Pelloux S, Beraud N, Roosimaa M, Kadaja L, Gruno M, Peet N, Orlova E, Remmelkoor R, Piirsoo A, Saks V, Seppet E | ||
|year=2008 | |year=2008 | ||
|journal=Biochim | |journal=Biochim Biophys Acta | ||
|abstract=Expression and function of creatine kinase (CK), adenylate kinase (AK) and hexokinase (HK) isoforms in relation to their roles in regulation of oxidative phosphorylation (OXPHOS) and intracellular energy transfer were assessed in beating (B) and non-beating (NB) cardiac HL-l cell lines and adult rat cardiomyocytes or myocardium. In both types of HL-1 cells, the ''AK2, CKB, HK1'' and ''HK2'' genes were expressed at higher levels than the ''CKM, CKMT2'' and ''AK1'' genes. Contrary to the saponin-permeabilized cardiomyocytes the OXPHOS was coupled to mitochondrial AK and HK but not to mitochondrial CK, and neither direct transfer of adenine nucleotides between CaMgATPases and mitochondria nor functional coupling between CK-MM and CaMgATPases was observed in permeabilized HL-1 cells. The HL-1 cells also exhibited deficient complex I of the respiratory chain. In conclusion, contrary to cardiomyocytes where mitochondria and CaMgATPases are organized into tight complexes which ensure effective energy transfer and feedback signaling between these structures via specialized pathways mediated by CK and AK isoforms and direct adenine nucleotide channeling, these complexes do not exist in HL-1 cells due to less organized energy metabolism. | |abstract=Expression and function of creatine kinase (CK), adenylate kinase (AK) and hexokinase (HK) isoforms in relation to their roles in regulation of oxidative phosphorylation (OXPHOS) and intracellular energy transfer were assessed in beating (B) and non-beating (NB) cardiac HL-l cell lines and adult rat cardiomyocytes or myocardium. In both types of HL-1 cells, the ''AK2, CKB, HK1'' and ''HK2'' genes were expressed at higher levels than the ''CKM, CKMT2'' and ''AK1'' genes. Contrary to the saponin-permeabilized cardiomyocytes the OXPHOS was coupled to mitochondrial AK and HK but not to mitochondrial CK, and neither direct transfer of adenine nucleotides between CaMgATPases and mitochondria nor functional coupling between CK-MM and CaMgATPases was observed in permeabilized HL-1 cells. The HL-1 cells also exhibited deficient complex I of the respiratory chain. In conclusion, contrary to cardiomyocytes where mitochondria and CaMgATPases are organized into tight complexes which ensure effective energy transfer and feedback signaling between these structures via specialized pathways mediated by CK and AK isoforms and direct adenine nucleotide channeling, these complexes do not exist in HL-1 cells due to less organized energy metabolism. | ||
|keywords=HL-1 cell, Heart, Energy transfer, Kinase, Gene expression | |keywords=HL-1 cell, Heart, Energy transfer, Kinase, Gene expression | ||
| Line 14: | Line 14: | ||
|injuries=Genetic Defect; Knockdown; Overexpression | |injuries=Genetic Defect; Knockdown; Overexpression | ||
|organism=Rat | |organism=Rat | ||
|tissues=Cardiac | |tissues=Cardiac muscle | ||
|preparations=Intact Cell; Cultured; Primary, Enzyme | |preparations=Intact Cell; Cultured; Primary, Enzyme | ||
|enzymes=Complex I, Complex II; Succinate Dehydrogenase, Complex III, Complex IV; Cytochrome c Oxidase, Complex V; ATP Synthase, Marker Enzyme | |enzymes=Complex I, Complex II; Succinate Dehydrogenase, Complex III, Complex IV; Cytochrome c Oxidase, Complex V; ATP Synthase, Marker Enzyme | ||
Revision as of 04:41, 5 April 2012
| Eimre M, Paju K, Pelloux S, Beraud N, Roosimaa M, Kadaja L, Gruno M, Peet N, Orlova E, Remmelkoor R, Piirsoo A, Saks V, Seppet E (2008) Distinct organization of energy metabolism in HL-1 cardiac cell line and cardiomyocytes. Biochim Biophys Acta 1777: 514-524. |
» [[Has info::PMID: 18423391]]
Eimre M, Paju K, Pelloux S, Beraud N, Roosimaa M, Kadaja L, Gruno M, Peet N, Orlova E, Remmelkoor R, Piirsoo A, Saks V, Seppet E (2008) Biochim Biophys Acta
Abstract: Expression and function of creatine kinase (CK), adenylate kinase (AK) and hexokinase (HK) isoforms in relation to their roles in regulation of oxidative phosphorylation (OXPHOS) and intracellular energy transfer were assessed in beating (B) and non-beating (NB) cardiac HL-l cell lines and adult rat cardiomyocytes or myocardium. In both types of HL-1 cells, the AK2, CKB, HK1 and HK2 genes were expressed at higher levels than the CKM, CKMT2 and AK1 genes. Contrary to the saponin-permeabilized cardiomyocytes the OXPHOS was coupled to mitochondrial AK and HK but not to mitochondrial CK, and neither direct transfer of adenine nucleotides between CaMgATPases and mitochondria nor functional coupling between CK-MM and CaMgATPases was observed in permeabilized HL-1 cells. The HL-1 cells also exhibited deficient complex I of the respiratory chain. In conclusion, contrary to cardiomyocytes where mitochondria and CaMgATPases are organized into tight complexes which ensure effective energy transfer and feedback signaling between these structures via specialized pathways mediated by CK and AK isoforms and direct adenine nucleotide channeling, these complexes do not exist in HL-1 cells due to less organized energy metabolism. • Keywords: HL-1 cell, Heart, Energy transfer, Kinase, Gene expression
• O2k-Network Lab: EE_Tallinn_Saks VA, FR_Grenoble_Saks VA, EE_Tartu_Seppet EK
Labels:
Stress:Genetic Defect; Knockdown; Overexpression Organism: Rat Tissue;cell: Cardiac muscle Preparation: Intact Cell; Cultured; Primary, Enzyme Enzyme: Complex I, Complex II; Succinate Dehydrogenase, Complex III, Complex IV; Cytochrome c Oxidase, Complex V; ATP Synthase, Marker Enzyme Regulation: Respiration; OXPHOS; ETS Capacity
HRR: Oxygraph-2k
