Difference between revisions of "Monge 2008 Mol Cell Biochem"
Beno Marija (talk | contribs) |
|||
| (10 intermediate revisions by 5 users not shown) | |||
| Line 1: | Line 1: | ||
{{Publication | {{Publication | ||
|title=Monge C, Beraud N, Kuznetsov | |title=Monge C, Beraud N, Kuznetsov AV, Rostovtseva T, Sackett D, Schlattner U, Vendelin M, Saks V (2008) Regulation of respiration in brain mitochondria and synaptosomes: restrictions of ADP diffusion in situ, roles of tubulin, and mitochondrial creatine kinase. Mol Cell Biochem 318:147-65. | ||
|authors=Monge C, Beraud N, Kuznetsov | |info=[http://www.ncbi.nlm.nih.gov/pubmed/18629616 PMID: 18629616] | ||
|authors=Monge C, Beraud N, Kuznetsov AV, Rostovtseva T, Sackett D, Schlattner U, Vendelin M, Saks VA | |||
|year=2008 | |year=2008 | ||
|journal=Mol | |journal=Mol Cell Biochem | ||
|abstract=The role of ubiquitous mitochondrial creatine | |abstract=The role of ubiquitous mitochondrial creatine kinase (uMtCK) reaction in regulation of mitochondrial respiration was studied in purified preparations of rat brain synaptosomes and mitochondria. In permeabilized synaptosomes, apparent Km for exogenous ADP, Km (ADP), in regulation of respiration in situ was rather high (110 ± 11lM) in comparison with isolated brain mitochondria | ||
kinase (uMtCK) reaction in regulation of mitochondrial respiration | (9 ± 1 lM). This apparent Km for ADP observed in isolated mitochondria ''in vitro'' dramatically increased to 169 ± 52lM after their incubation with 1 lM of dimeric tubulin showing that in rat brain, particularly in synaptosomes, | ||
was studied in purified preparations of rat brain | mitochondrial outer membrane permeability for ADP, and ATP may be restricted by tubulin binding to voltage dependent anion channel (VDAC). On the other hand, in | ||
synaptosomes and mitochondria. In permeabilized synaptosomes, | synaptosomes apparent Km (ADP) decreased to 25 ± 1 lM in the presence of 20 mM creatine. To fully understand this effect of creatine on kinetics of respiration regulation, complete kinetic analysis of uMtCK reaction in isolated brain mitochondria was carried out. This showed that oxidative phosphorylation specifically altered only the dissociation constants for MgATP, by decreasing that from ternary complex MtCK.Cr.MgATP (Ka) from 0.13 ± 0.02 to 0.018 ± | ||
apparent Km for exogenous ADP, Km (ADP), in | 0.007 mMand that frombinary complexMtCK.MgATP (Kia) from 1.1 ± 0.29 mM to 0.17 ± 0.07 mM. Apparent decrease of dissociation constants for MgATP reflects effective cycling of ATP and ADP between uMtCK and adenine nucleotide translocase (ANT). These results emphasize important role and various pathophysiological implications of the phosphocreatine–creatine kinase systemin energy transfer in brain cells, including synaptosomes. | ||
regulation of respiration in situ was rather high (110 ± | |||
11lM) in comparison with isolated brain mitochondria | |||
(9 ± 1 lM). This apparent Km for ADP observed in isolated | |||
mitochondria in vitro dramatically increased to 169 ± | |||
52lM after their incubation with 1 lM of dimeric tubulin | |||
showing that in rat brain, particularly in synaptosomes, | |||
mitochondrial outer membrane permeability for ADP, and | |||
ATP may be restricted by tubulin binding to voltage dependent | |||
anion channel (VDAC). On the other hand, in | |||
synaptosomes apparent Km (ADP) decreased to 25 ± 1 lM | |||
in the presence of 20 mM creatine. To fully understand this | |||
effect of creatine on kinetics of respiration regulation, complete | |||
kinetic analysis of uMtCK reaction in isolated brain | |||
mitochondria was carried out. This showed that oxidative | |||
phosphorylation specifically altered only the dissociation | |||
constants for MgATP, by decreasing that from ternary complex | |||
MtCK.Cr.MgATP (Ka) from 0.13 ± 0.02 to 0.018 ± | |||
0.007 mMand that frombinary complexMtCK.MgATP (Kia) | |||
from 1.1 ± 0.29 mM to 0.17 ± 0.07 mM. Apparent | |||
decrease of dissociation constants for MgATP reflects effective | |||
cycling of ATP and ADP between uMtCK and adenine | |||
nucleotide translocase (ANT). These results emphasize | |||
important role and various pathophysiological implications of | |||
the phosphocreatine–creatine kinase systemin energy transfer | |||
in brain cells, including synaptosomes. | |||
|keywords=Brain, Creatine kinase, Functional coupling, Mitochondria, Synaptosomes, Tubulin | |keywords=Brain, Creatine kinase, Functional coupling, Mitochondria, Synaptosomes, Tubulin | ||
| | |mipnetlab=EE Tallinn Saks VA, FR Grenoble Saks VA, FR Grenoble Schlattner U, EE Tallinn Kaambre T | ||
}} | }} | ||
{{Labeling | {{Labeling | ||
|injuries=Mitochondrial | |area=Respiration | ||
|organism= | |injuries=Mitochondrial disease | ||
|tissues= | |organism=Rat | ||
| | |tissues=Nervous system | ||
|preparations=Isolated mitochondria | |||
|instruments=Oxygraph-2k | |instruments=Oxygraph-2k | ||
}} | }} | ||
Latest revision as of 15:20, 26 March 2018
| Monge C, Beraud N, Kuznetsov AV, Rostovtseva T, Sackett D, Schlattner U, Vendelin M, Saks V (2008) Regulation of respiration in brain mitochondria and synaptosomes: restrictions of ADP diffusion in situ, roles of tubulin, and mitochondrial creatine kinase. Mol Cell Biochem 318:147-65. |
Monge C, Beraud N, Kuznetsov AV, Rostovtseva T, Sackett D, Schlattner U, Vendelin M, Saks VA (2008) Mol Cell Biochem
Abstract: The role of ubiquitous mitochondrial creatine kinase (uMtCK) reaction in regulation of mitochondrial respiration was studied in purified preparations of rat brain synaptosomes and mitochondria. In permeabilized synaptosomes, apparent Km for exogenous ADP, Km (ADP), in regulation of respiration in situ was rather high (110 ± 11lM) in comparison with isolated brain mitochondria (9 ± 1 lM). This apparent Km for ADP observed in isolated mitochondria in vitro dramatically increased to 169 ± 52lM after their incubation with 1 lM of dimeric tubulin showing that in rat brain, particularly in synaptosomes, mitochondrial outer membrane permeability for ADP, and ATP may be restricted by tubulin binding to voltage dependent anion channel (VDAC). On the other hand, in synaptosomes apparent Km (ADP) decreased to 25 ± 1 lM in the presence of 20 mM creatine. To fully understand this effect of creatine on kinetics of respiration regulation, complete kinetic analysis of uMtCK reaction in isolated brain mitochondria was carried out. This showed that oxidative phosphorylation specifically altered only the dissociation constants for MgATP, by decreasing that from ternary complex MtCK.Cr.MgATP (Ka) from 0.13 ± 0.02 to 0.018 ± 0.007 mMand that frombinary complexMtCK.MgATP (Kia) from 1.1 ± 0.29 mM to 0.17 ± 0.07 mM. Apparent decrease of dissociation constants for MgATP reflects effective cycling of ATP and ADP between uMtCK and adenine nucleotide translocase (ANT). These results emphasize important role and various pathophysiological implications of the phosphocreatine–creatine kinase systemin energy transfer in brain cells, including synaptosomes. • Keywords: Brain, Creatine kinase, Functional coupling, Mitochondria, Synaptosomes, Tubulin
• O2k-Network Lab: EE Tallinn Saks VA, FR Grenoble Saks VA, FR Grenoble Schlattner U, EE Tallinn Kaambre T
Labels: MiParea: Respiration
Stress:Mitochondrial disease Organism: Rat Tissue;cell: Nervous system Preparation: Isolated mitochondria
HRR: Oxygraph-2k
