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 | |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. | ||
|info=[http://www.ncbi.nlm.nih.gov/pubmed/8495738 PMID: 8495738] | |info=[http://www.ncbi.nlm.nih.gov/pubmed/8495738 PMID: 8495738] | ||
|authors=Kunz WS, Kuznetsov AV, Gellerich FN | |authors=Kunz WS, Kuznetsov AV, Gellerich FN | ||
|year=1993 | |year=1993 | ||
|journal=FEBS | |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 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. | |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 | ||
Revision as of 08:55, 2 July 2013
| 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. |
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. • Keywords: Saponin-skinned muscle fiber, Human skeletal muscle, Oxidative phosphorylation, Caffeine
Labels:
Organism: Human
Tissue;cell: Skeletal muscle
Preparation: Permeabilized tissue
Coupling state: OXPHOS
HRR: Oxygraph-2k
