Document Detail


ATP production rate via creatine kinase or ATP synthase in vivo: a novel superfast magnetization saturation transfer method.
MedLine Citation:
PMID:  21293002     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
RATIONALE: ³¹P magnetization saturation transfer (MST) experiment is the most widely used method to study ATP metabolism kinetics. However, its lengthy data acquisition time greatly limits the wide biomedical applications in vivo, especially for studies requiring high spatial and temporal resolutions.
OBJECTIVE: We aimed to develop a novel superfast MST method that can accurately quantify ATP production rate constants (k(f)) through creatine kinase (CK) or ATP synthase (ATPase) with 2 spectra.
METHODS AND RESULTS: The T₁(nom) (T₁ nominal) method uses a correction factor to compensate the partially relaxed MST experiments, thus allowing measurement of enzyme kinetics with an arbitrary repetition time and flip angle, which consequently reduces the data acquisition time of a transmurally differentiated CK k(f) measurement by 91% as compared with the conventional method with spatial localization. The novel T₁(nom) method is validated theoretically with numeric simulation, and further verified with in vivo swine hearts, as well as CK and ATPase activities in rat brain at 9.4 Tesla. Importantly, the in vivo data from swine hearts demonstrate, for the first time, that within an observation window of 30 minutes, the inhibition of CK activity by iodoacetamide does not limit left ventricular chamber contractile function.
CONCLUSIONS: A novel MST method for superfast examination of enzyme kinetics in vivo has been developed and verified theoretically and experimentally. In the in vivo normal heart, redundant multiple supporting systems of myocardial ATP production, transportation, and utilization exist, such that inhibition of one mechanism does not impair the normal left ventricular contractile performance.
Authors:
Qiang Xiong; Fei Du; Xiaohong Zhu; Pengyuan Zhang; Piradeep Suntharalingam; Joseph Ippolito; Forum D Kamdar; Wei Chen; Jianyi Zhang
Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't     Date:  2011-02-03
Journal Detail:
Title:  Circulation research     Volume:  108     ISSN:  1524-4571     ISO Abbreviation:  Circ. Res.     Publication Date:  2011 Mar 
Date Detail:
Created Date:  2011-03-18     Completed Date:  2011-05-23     Revised Date:  2013-06-30    
Medline Journal Info:
Nlm Unique ID:  0047103     Medline TA:  Circ Res     Country:  United States    
Other Details:
Languages:  eng     Pagination:  653-63     Citation Subset:  IM    
Affiliation:
Cardiovascular Division, Department of Medicine, University of Minnesota, Minneapolis, USA.
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MeSH Terms
Descriptor/Qualifier:
Adenosine Triphosphate / biosynthesis*
Animals
Creatine Kinase / antagonists & inhibitors,  metabolism*
Energy Metabolism
Female
Hemodynamics
Kinetics
Magnetic Resonance Imaging
Magnetic Resonance Spectroscopy / methods*
Male
Models, Biological
Myocardium / metabolism
Phosphorus Isotopes
Proton-Translocating ATPases / metabolism*
Rats
Rats, Sprague-Dawley
Swine
Time Factors
Grant Support
ID/Acronym/Agency:
HL 100407/HL/NHLBI NIH HHS; HL 67828/HL/NHLBI NIH HHS; HL 95077/HL/NHLBI NIH HHS; HL50470/HL/NHLBI NIH HHS; NS041262/NS/NINDS NIH HHS; NS057560/NS/NINDS NIH HHS; NS070839/NS/NINDS NIH HHS; P30 NS057091/NS/NINDS NIH HHS; P41 RR008079/RR/NCRR NIH HHS; R01 HL050470-08/HL/NHLBI NIH HHS; R01 HL067828-09/HL/NHLBI NIH HHS; R01 HL095077-03/HL/NHLBI NIH HHS; U01 HL100407/HL/NHLBI NIH HHS
Chemical
Reg. No./Substance:
0/Phosphorus Isotopes; 56-65-5/Adenosine Triphosphate; EC 2.7.3.2/Creatine Kinase; EC 3.6.3.14/Proton-Translocating ATPases
Comments/Corrections

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