BDM drives protein dephosphorylation and inhibits adenine nucleotide exchange in cardiomyocytes
Contractile dysfunction plays a key role in injury sustained by ischemic myocardium at reperfusion, whereas interventions that impede hypercontracture enhance recovery. In permeabilized adult rat cardiomyocytes, the negative inotrope 2,3-butanedione monoxime (BDM; 10-50 mM) inhibited rigor at low Mg...
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| Veröffentlicht in: | American journal of physiology. Heart and circulatory physiology 1998-10, Vol.44 (4), p.H1260-H1266 |
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| container_end_page | H1266 |
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| container_issue | 4 |
| container_start_page | H1260 |
| container_title | American journal of physiology. Heart and circulatory physiology |
| container_volume | 44 |
| creator | STAPLETON, M. T FUCHSBAUER, C. M ALLSHIRE, A. P |
| description | Contractile dysfunction plays a key role in injury sustained by ischemic myocardium at reperfusion, whereas interventions that impede hypercontracture enhance recovery. In permeabilized adult rat cardiomyocytes, the negative inotrope 2,3-butanedione monoxime (BDM; 10-50 mM) inhibited rigor at low MgATP concentration but stimulated net ATP hydrolysis. |
| format | Article |
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| identifier | ISSN: 0363-6135 |
| ispartof | American journal of physiology. Heart and circulatory physiology, 1998-10, Vol.44 (4), p.H1260-H1266 |
| issn | 0363-6135 1522-1539 |
| language | eng |
| recordid | cdi_proquest_journals_229677757 |
| source | American Physiological Society; EZB-FREE-00999 freely available EZB journals |
| subjects | Biological and medical sciences Cardiology Drug therapy Fundamental and applied biological sciences. Psychology Heart Metabolism Pharmacology Proteins Vertebrates: cardiovascular system |
| title | BDM drives protein dephosphorylation and inhibits adenine nucleotide exchange in cardiomyocytes |
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