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Volumn 8, Issue 3-4, 1998, Pages 229-234

Some new aspects of creatine kinase (CK): Compartmentation, structure, function and regulation for cellular and mitochondrial bioenergetics and physiology

Author keywords

Adenine nucleotide translocase (ANT); AMP activated protein kinase; Cell and neuroprotective effects of creatine; CK null mutant transgenic mice; Creatine kinase (CK); Creatine supplementation; Energetics of Ca2+ homeostasis; Intramitochondrial inclusions; Mitochondrial creatine kinase (Mi CK); Mitochondrial myopathies; Mitochondrial permeability transition; Neuromuscular diseases; Peroxynitrite; Phosphocreatine shuttle; Porin

Indexed keywords

CREATINE KINASE;

EID: 0032406769     PISSN: 09516433     EISSN: None     Source Type: Journal    
DOI: 10.1002/biof.5520080310     Document Type: Review
Times cited : (200)

References (30)
  • 1
    • 0030569305 scopus 로고    scopus 로고
    • Complexes between kinases, mitochondrial porin and adenylate translocator in rat brain resemble the permeability transition pore
    • G. Beutner, A. Rück, B. Riede, W. Weite and D. Brdiczka, Complexes between kinases, mitochondrial porin and adenylate translocator in rat brain resemble the permeability transition pore, FEBS Lett. 396 (1997), 189-195.
    • (1997) FEBS Lett. , vol.396 , pp. 189-195
    • Beutner, G.1    Rück, A.2    Riede, B.3    Weite, W.4    Brdiczka, D.5
  • 2
    • 0028034636 scopus 로고
    • In vitro complex formation between the octamer of mitochondrial creatine kinase and porin
    • D. Brdiczka, P. Kaldis and T. Wallimann, In vitro complex formation between the octamer of mitochondrial creatine kinase and porin, J. Biol. Chem. 269 (1994), 27 640-27 644.
    • (1994) J. Biol. Chem. , vol.269 , pp. 27640-27644
    • Brdiczka, D.1    Kaldis, P.2    Wallimann, T.3
  • 3
    • 0032422634 scopus 로고    scopus 로고
    • The molecular structure of mitochondrial contact sites. Their role in regulation of energy metabolism and permeability transition
    • D. Brdiczka, G. Beutner, A. Rück, M. Dolder and T. Wallimann, The molecular structure of mitochondrial contact sites. Their role in regulation of energy metabolism and permeability transition, Biofactors 8 (1998), 235-242.
    • (1998) Biofactors , vol.8 , pp. 235-242
    • Brdiczka, D.1    Beutner, G.2    Rück, A.3    Dolder, M.4    Wallimann, T.5
  • 5
    • 0031918210 scopus 로고    scopus 로고
    • Does muscle creatine phosphokinase have access to the total pool of phosphocreatine plus creatine?
    • P.W. Hochachka and M.K. Mossey, Does muscle creatine phosphokinase have access to the total pool of phosphocreatine plus creatine?, Am. J. Physiol. 274 (1998), R868-R872.
    • (1998) Am. J. Physiol. , vol.274
    • Hochachka, P.W.1    Mossey, M.K.2
  • 6
  • 8
    • 0001560058 scopus 로고    scopus 로고
    • Binding of creatine kinase to the I-band of skinned skeletal muscle fibers is mediated by glycolytic enzymes: An in situ biochemical approach
    • Th. Kraft, V. Nier, B. Brenner and T. Wallimann, Binding of creatine kinase to the I-band of skinned skeletal muscle fibers is mediated by glycolytic enzymes: an in situ biochemical approach, Biophys. J. 70 (1996), A292.
    • (1996) Biophys. J. , vol.70
    • Kraft, Th.1    Nier, V.2    Brenner, B.3    Wallimann, T.4
  • 9
    • 0031031163 scopus 로고    scopus 로고
    • Peak assignment in localized 1H MR spectra of human muscle based on oral creatine supplementation
    • R. Kreis, M. Koster, M. Kamber, H. Hoppeler and C. Boesch, Peak assignment in localized 1H MR spectra of human muscle based on oral creatine supplementation, Magn. Reson. Med. 37 (1997), 159-163.
    • (1997) Magn. Reson. Med. , vol.37 , pp. 159-163
    • Kreis, R.1    Koster, M.2    Kamber, M.3    Hoppeler, H.4    Boesch, C.5
  • 10
    • 0030816175 scopus 로고    scopus 로고
    • Kinetics of ATP to ADP β-phosphoryl conversion in contracting skeltal muscle by in vivo 31P-NMR magnetization transfer
    • E. LeRumeur, N. LeTallec, F. Kernec and J.D. de Certaines, Kinetics of ATP to ADP β-phosphoryl conversion in contracting skeltal muscle by in vivo 31P-NMR magnetization transfer, NMR Biomed. 10 (1997), 67-72.
    • (1997) NMR Biomed. , vol.10 , pp. 67-72
    • LeRumeur, E.1    LeTallec, N.2    Kernec, F.3    De Certaines, J.D.4
  • 11
    • 0028071988 scopus 로고
    • Activity of creatine kinase in a contracting mammalian muscle of uniform fiber type
    • E.W. McFarland, M.J. Kushmerick and T. Moerland, Activity of creatine kinase in a contracting mammalian muscle of uniform fiber type, Biophys. J. 67 (1994), 1912-1924.
    • (1994) Biophys. J. , vol.67 , pp. 1912-1924
    • McFarland, E.W.1    Kushmerick, M.J.2    Moerland, T.3
  • 12
    • 0030242226 scopus 로고    scopus 로고
    • 2+-uptake by cardiac sarcoplasmic reticulum ATPase in situ strongly depends on bound creatine kinase
    • 2+-uptake by cardiac sarcoplasmic reticulum ATPase in situ strongly depends on bound creatine kinase, Pflügers Arch. 432 (1996), 904-912.
    • (1996) Pflügers Arch. , vol.432 , pp. 904-912
    • Minajeva, A.1    Ventura-Calapier, R.2    Veksler, V.3
  • 13
    • 0030745401 scopus 로고    scopus 로고
    • Dipolar resonance frequency shifts in IH MR spectra of skeletal muscle: Confirmation in rats at 4,7 T in vivo and observation of changes postmortem
    • V. Ntziachristos, R. Kreis, C. Boesch and B. Quistorff, Dipolar resonance frequency shifts in IH MR spectra of skeletal muscle: confirmation in rats at 4,7 T in vivo and observation of changes postmortem, Magn. Reson. Med. 38 (1997), 33-39.
    • (1997) Magn. Reson. Med. , vol.38 , pp. 33-39
    • Ntziachristos, V.1    Kreis, R.2    Boesch, C.3    Quistorff, B.4
  • 14
    • 0030857659 scopus 로고    scopus 로고
    • Crystalline mitochondrial inclusion bodies isolated from creatine-depleted rat soleus muscle
    • E. O'Gorman, K.-H. Fuchs, P. Tittmann, H. Gross and T. Wallimann, Crystalline mitochondrial inclusion bodies isolated from creatine-depleted rat soleus muscle, J. Cell Sci. 110 (1997), 1403-1411.
    • (1997) J. Cell Sci. , vol.110 , pp. 1403-1411
    • O'Gorman, E.1    Fuchs, K.-H.2    Tittmann, P.3    Gross, H.4    Wallimann, T.5
  • 15
  • 16
    • 0032536774 scopus 로고    scopus 로고
    • Dual regulation of AMP-activated protein kinase provides a novel mechanism for the control of creatine kinase in skeletal muscle
    • M. Ponticos, Q.L. Lu, J.E. Morgan, D.G. Hardie, TA. Partridge and D. Carling, Dual regulation of AMP-activated protein kinase provides a novel mechanism for the control of creatine kinase in skeletal muscle, EMBO J. 17 (1998), 1688-1699.
    • (1998) EMBO J. , vol.17 , pp. 1688-1699
    • Ponticos, M.1    Lu, Q.L.2    Morgan, J.E.3    Hardie, D.G.4    Partridge, T.A.5    Carling, D.6
  • 18
    • 0031712655 scopus 로고    scopus 로고
    • Functional aspects of the X-ray structure of mitochondrial creatine kinase: A molecular physiology approach
    • U. Schlattner, N. Forstner, M. Eder, O. Stachowiak, K. Fritz-Wolf and T. Wallimann, Functional aspects of the X-ray structure of mitochondrial creatine kinase: a molecular physiology approach, Mol. Cell Biochem. 184 (1998), 125-140.
    • (1998) Mol. Cell Biochem. , vol.184 , pp. 125-140
    • Schlattner, U.1    Forstner, N.2    Eder, M.3    Stachowiak, O.4    Fritz-Wolf, K.5    Wallimann, T.6
  • 19
    • 0032479147 scopus 로고    scopus 로고
    • Mitochondrial creatine kinase is a prime target of peroxynitrite-induced modification and inactivation
    • O. Stachowiak, M. Dolder, T. Wallimann and Ch. Richter, Mitochondrial creatine kinase is a prime target of peroxynitrite-induced modification and inactivation, J. Biol. Chem. 273 (1998), 16 694-16 699.
    • (1998) J. Biol. Chem. , vol.273 , pp. 16694-16699
    • Stachowiak, O.1    Dolder, M.2    Wallimann, T.3    Richter, Ch.4
  • 20
    • 0031656932 scopus 로고    scopus 로고
    • Oligomeric state and membrane binding behaviour of creatine kinase isoenzymes: Implications for cellular function and mitochondrial structure
    • O. Stachowiak, U. Schlattner, M. Dolder and T. Wallimann, Oligomeric state and membrane binding behaviour of creatine kinase isoenzymes: implications for cellular function and mitochondrial structure, Mol. Cell Biochem. 184 (1998), 141-151.
    • (1998) Mol. Cell Biochem. , vol.184 , pp. 141-151
    • Stachowiak, O.1    Schlattner, U.2    Dolder, M.3    Wallimann, T.4
  • 21
    • 0030611177 scopus 로고    scopus 로고
    • 2+-response in muscles with combined mitochondrial and cytosolic creatine kinase deficiencies
    • 2+-response in muscles with combined mitochondrial and cytosolic creatine kinase deficiencies, Cell 89 (1997), 93-103.
    • (1997) Cell , vol.89 , pp. 93-103
    • Steeghs, K.1
  • 22
    • 0031781884 scopus 로고    scopus 로고
    • Myofibrillar interaction of cytosolic creatine kinase (CK) isoenzymes: Allocation of N-terminal binding epitope in MM-CK and BB-CK
    • M. Stolz and T Wallimann, Myofibrillar interaction of cytosolic creatine kinase (CK) isoenzymes: allocation of N-terminal binding epitope in MM-CK and BB-CK, J. Cell Sci. 111 (1998), 1207-1216.
    • (1998) J. Cell Sci. , vol.111 , pp. 1207-1216
    • Stolz, M.1    Wallimann, T.2
  • 23
    • 0030851631 scopus 로고    scopus 로고
    • Activation of sea urchin sperm motility is accompanied by an increase in the creatine kinase exchange flux
    • F. VanDorsten, M. Wyss, T. Wallimann and K. Nicolay, Activation of sea urchin sperm motility is accompanied by an increase in the creatine kinase exchange flux, Biochem. J. 325 (1997), 411-416.
    • (1997) Biochem. J. , vol.325 , pp. 411-416
    • VanDorsten, F.1    Wyss, M.2    Wallimann, T.3    Nicolay, K.4
  • 24
    • 0028603394 scopus 로고
    • Creatine kinase in skeletal muscle energy metabolism: A study of mouse mutants with graded reduc-tion in muscle CK expression
    • J. VanDeursen et al., Creatine kinase in skeletal muscle energy metabolism: a study of mouse mutants with graded reduc-tion in muscle CK expression, Proc. Natl. Acad. Sci. USA 91 (1994), 9091-9095.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 9091-9095
    • VanDeursen, J.1
  • 25
    • 0029665566 scopus 로고
    • 31P-NMR-measured creatine kinase reaction flux in muscle: A CAVEAT!
    • 31P-NMR-measured creatine kinase reaction flux in muscle: a CAVEAT!, J. Muscle Res. Cell Motil. 17 (1994), 177-181.
    • (1994) J. Muscle Res. Cell Motil. , vol.17 , pp. 177-181
    • Wallimann, T.1
  • 26
    • 0028050777 scopus 로고
    • Dissecting the role of creatine kinase
    • T Wallimann, Dissecting the role of creatine kinase, Curr. Biol. 1 (1994), 42-46.
    • (1994) Curr. Biol. , vol.1 , pp. 42-46
    • Wallimann, T.1
  • 27
    • 0026585611 scopus 로고
    • Intracellular compartmentation, structure and function of creatine kinase isoenzymes in tissues with high and fluctuating energy demands: The "PCr-circuit" for cellular energy homeostasis
    • T. Wallimann, M. Wyss, D. Brdiczka, K. Nicolay and H.M. Eppenberger, Intracellular compartmentation, structure and function of creatine kinase isoenzymes in tissues with high and fluctuating energy demands: the "PCr-circuit" for cellular energy homeostasis, Biochem. J. 281 (1992), 21-40.
    • (1992) Biochem. J. , vol.281 , pp. 21-40
    • Wallimann, T.1    Wyss, M.2    Brdiczka, D.3    Nicolay, K.4    Eppenberger, H.M.5
  • 29
  • 30
    • 0026698727 scopus 로고
    • Mitochondrial creatine kinase: A key enzyme of aerobic energy metabolism
    • M. Wyss, J. Smeitink, R. Wevers and T. Wallimann, Mitochondrial creatine kinase: a key enzyme of aerobic energy metabolism, Biochim. Biophys. Acta 1102 (1992), 119-166.
    • (1992) Biochim. Biophys. Acta , vol.1102 , pp. 119-166
    • Wyss, M.1    Smeitink, J.2    Wevers, R.3    Wallimann, T.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.