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Difference between revisions of "Kunz 1993 FEBS Lett"

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{{Publication
{{Publication
|title=Kunz WS, Kuznetsov AV, Gellerich FN (1993) Mitochondrial oxidative phosphorylation in saponin-skinned human muscle fibers is stimulated by caffeine. FEBS Lett. 323: 188-190.
|title=Kunz WS, Kuznetsov AV, Gellerich FN (1993) Mitochondrial oxidative phosphorylation in saponin-skinned human muscle fibers is stimulated by caffeine. FEBS Lett 323:188-90.
|info=[http://www.ncbi.nlm.nih.gov/pubmed/8495738 PMID: 8495738 Open Access]
|authors=Kunz WS, Kuznetsov AV, Gellerich FN
|authors=Kunz WS, Kuznetsov AV, Gellerich FN
|year=1993
|year=1993
|journal=FEBS Lett.
|journal=FEBS Lett
|abstract=The addition of 15 mM caffeine to saponin-skinned human muscle fibers from M. vastus lateralis caused in the presence of 2 mM ATP an approx. 2-fold stimulation of respiration with glutamate + malate. This effect can be abolished by either the addition of the Ca2+ chelator EGTA, the inhibitor of Ca2+Β  transport Ruthenium red and the inhibitor of the myosin ATPase vanadate. The caffeine concentration dependency of respiration of fibers coincided with the caffeine-caused stimulation of myosin ATPase activity. The activation of oxidative phosphorylation in saponin-skinned human muscle fibers by caffeine can be explained by a stimulation of myosin ATPase caused by Ca2+ release from sarcoplasmic reticulum.
|abstract=The addition of 15 mM caffeine to saponin-skinned human muscle fibers from M. vastus lateralis caused in the presence of 2 mM ATP an approx. 2-fold stimulation of respiration with glutamate + malate. This effect can be abolished by either the addition of the Ca<sup>2+</sup> chelator EGTA, the inhibitor of Ca<sup>2+</sup> transport Ruthenium red and the inhibitor of the myosin ATPase vanadate. The caffeine concentration dependency of respiration of fibers coincided with the caffeine-caused stimulation of myosin ATPase activity. The activation of oxidative phosphorylation in saponin-skinned human muscle fibers by caffeine can be explained by a stimulation of myosin ATPase caused by Ca<sup>2+</sup> release from sarcoplasmic reticulum.
|keywords=Saponin-skinned muscle fiber, Human skeletal muscle, Oxidative phosphorylation, Caffeine
|keywords=Saponin-skinned muscle fiber, Human skeletal muscle, Oxidative phosphorylation, Caffeine
|info=[http://www.ncbi.nlm.nih.gov/pubmed/8495738 PMID: 8495738]
|mipnetlab=DE Magdeburg Gellerich FN
}}
}}
{{Labeling
{{Labeling
|organism=Human
|organism=Human
|topics=Respiration; OXPHOS; ETS Capacity
|tissues=Skeletal muscle
|preparations=Permeabilized tissue
|couplingstates=OXPHOS
|instruments=Oxygraph-2k
|instruments=Oxygraph-2k
}}
}}

Latest revision as of 11:00, 27 March 2018

Publications in the MiPMap
Kunz WS, Kuznetsov AV, Gellerich FN (1993) Mitochondrial oxidative phosphorylation in saponin-skinned human muscle fibers is stimulated by caffeine. FEBS Lett 323:188-90.

Β» PMID: 8495738 Open Access

Kunz WS, Kuznetsov AV, Gellerich FN (1993) FEBS Lett

Abstract: The addition of 15 mM caffeine to saponin-skinned human muscle fibers from M. vastus lateralis caused in the presence of 2 mM ATP an approx. 2-fold stimulation of respiration with glutamate + malate. This effect can be abolished by either the addition of the Ca2+ chelator EGTA, the inhibitor of Ca2+ transport Ruthenium red and the inhibitor of the myosin ATPase vanadate. The caffeine concentration dependency of respiration of fibers coincided with the caffeine-caused stimulation of myosin ATPase activity. The activation of oxidative phosphorylation in saponin-skinned human muscle fibers by caffeine can be explained by a stimulation of myosin ATPase caused by Ca2+ release from sarcoplasmic reticulum. β€’ Keywords: Saponin-skinned muscle fiber, Human skeletal muscle, Oxidative phosphorylation, Caffeine

β€’ O2k-Network Lab: DE Magdeburg Gellerich FN


Labels:


Organism: Human  Tissue;cell: Skeletal muscle  Preparation: Permeabilized tissue 


Coupling state: OXPHOS 

HRR: Oxygraph-2k