[NMR paper] 31P NMR 2D Mapping of Creatine Kinase Forward Flux Rate in Hearts with Postinfarction Left Ventricular Remodeling in Response to Cell Therapy.
Related Articles31P NMR 2D Mapping of Creatine Kinase Forward Flux Rate in Hearts with Postinfarction Left Ventricular Remodeling in Response to Cell Therapy.
PLoS One. 2016;11(9):e0162149
Authors: Gao L, Cui W, Zhang P, Jang A, Zhu W, Zhang J
Abstract
Utilizing a fast 31P magnetic resonance spectroscopy (MRS) 2-dimensional chemical shift imaging (2D-CSI) method, this study examined the heterogeneity of creatine kinase (CK) forward flux rate of hearts with postinfarction left ventricular (LV) remodeling. Immunosuppressed Yorkshire pigs were assigned to 4 groups: 1) A sham-operated normal group (SHAM, n = 6); 2) A 60 minutes distal left anterior descending coronary artery ligation and reperfusion (MI, n = 6); 3) Open patch group; ligation injury plus open fibrin patch over the site of injury (Patch, n = 6); and 4) Cell group, hiPSCs-cardiomyocytes, -endothelial cells, and -smooth muscle cells (2 million, each) were injected into the injured myocardium pass through a fibrin patch (Cell+Patch, n = 5). At 4 weeks, the creatine phosphate (PCr)/ATP ratio, CK forward flux rate (Flux PCr->ATP), and k constant of CK forward flux rate (kPCr->ATP) were severely decreased at border zone myocardium (BZ) adjacent to MI. Cell treatment results in significantly increase of PCr/ATP ratio and improve the value of kPCr->ATP and Flux PCr->ATP in BZ myocardium. Moreover, the BZ myocardial CK total activity and protein expression of CK mitochondria isozyme and CK myocardial isozyme were significantly reduced, but recovered in response to cell treatment. Thus, cell therapy results in improvement of BZ bioenergetic abnormality in hearts with postinfarction LV remodeling, which is accompanied by significantly improvements in BZ CK activity and CK isozyme expression. The fast 2D 31P MR CSI mapping can reliably measure the heterogeneity of bioenergetics in hearts with post infarction LV remodeling.
Apparent rate constant mapping using hyperpolarized [1–13C]pyruvate
From The DNP-NMR Blog:
Apparent rate constant mapping using hyperpolarized pyruvate
Khegai, O., et al., Apparent rate constant mapping using hyperpolarized pyruvate. NMR in Biomedicine, 2014. 27(10): p. 1256-1265.
http://dx.doi.org/10.1002/nbm.3174
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NMR Structure of the HWE Kinase Associated Response Regulator Sma0114 in Its Activated State
NMR Structure of the HWE Kinase Associated Response Regulator Sma0114 in Its Activated State
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/bi401497h/aop/images/medium/bi-2013-01497h_0009.gif
Biochemistry
DOI: 10.1021/bi401497h
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01-07-2014 10:30 AM
[NMR paper] NMR Structure of the HWE-Kinase Associated Response Regulator Sma0114 in its Activated State.
NMR Structure of the HWE-Kinase Associated Response Regulator Sma0114 in its Activated State.
Related Articles NMR Structure of the HWE-Kinase Associated Response Regulator Sma0114 in its Activated State.
Biochemistry. 2013 Dec 23;
Authors: Sheftic SR, White E, Gage DJ, Alexandrescu AT
Abstract
Bacterial receiver domains modulate intracellular responses to external stimuli in two-component systems. Sma0114 is the first structurally-characterized representative from the family of receiver domains that are substrates for HWE-kinases. We...
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12-25-2013 03:39 PM
[NMR paper] Site-specific NMR mapping and time-resolved monitoring of serine and threonine phosphorylation in reconstituted kinase reactions and mammalian cell extracts.
Site-specific NMR mapping and time-resolved monitoring of serine and threonine phosphorylation in reconstituted kinase reactions and mammalian cell extracts.
Site-specific NMR mapping and time-resolved monitoring of serine and threonine phosphorylation in reconstituted kinase reactions and mammalian cell extracts.
Nat Protoc. 2013 Jun 27;8(7):1416-1432
Authors: Theillet FX, Rose HM, Liokatis S, Binolfi A, Thongwichian R, Stuiver M, Selenko P
Abstract
We outline NMR protocols for site-specific mapping and time-resolved monitoring of...
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[NMR paper] Cytosine deaminase and thymidine kinase gene therapy in a Dunning rat prostate tumour
Cytosine deaminase and thymidine kinase gene therapy in a Dunning rat prostate tumour model: absence of bystander effects and characterisation of 5-fluorocytosine metabolism with 19F-NMR spectroscopy.
Related Articles Cytosine deaminase and thymidine kinase gene therapy in a Dunning rat prostate tumour model: absence of bystander effects and characterisation of 5-fluorocytosine metabolism with 19F-NMR spectroscopy.
Gene Ther. 2002 Dec;9(23):1564-75
Authors: Corban-Wilhelm H, Hull WE, Becker G, Bauder-Wüst U, Greulich D, Debus J
The rat...
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11-24-2010 08:58 PM
[NMR paper] 13C NMR evidence for pyruvate kinase flux attenuation underlying suppressed acid form
13C NMR evidence for pyruvate kinase flux attenuation underlying suppressed acid formation in Bacillus subtilis.
Related Articles 13C NMR evidence for pyruvate kinase flux attenuation underlying suppressed acid formation in Bacillus subtilis.
Biotechnol Prog. 2000 Mar-Apr;16(2):169-75
Authors: Phalakornkule C, Fry B, Zhu T, Kopesel R, Ataai MM, Domach MM
When batch and continuous Bacillus subtilis cultures are provided with a small amount of citrate, acid production ceases, carbon yield increases by more than 2-fold, and the productivity of...
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[NMR paper] NMR detection of creatine kinase expressed in liver of transgenic mice: determination
NMR detection of creatine kinase expressed in liver of transgenic mice: determination of free ADP levels.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles NMR detection of creatine kinase expressed in liver of transgenic mice: determination of free ADP levels.
Proc Natl Acad Sci U S A. 1990 Apr;87(8):3112-6
Authors: Koretsky AP, Brosnan MJ, Chen LH, Chen JD, Van Dyke T
To use the equilibrium established by creatine kinase (CK) to determine hepatic free ADP...
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08-21-2010 10:48 PM
Mapping structural interactions using in-cell NMR spectroscopy (STINT-NMR)
Mapping structural interactions using in-cell NMR spectroscopy (STINT-NMR)
David S Burz, Kaushik Dutta, David Cowburn & Alexander Shekhtman
We describe a high-throughput in-cell nuclear magnetic resonance (NMR)-based method for mapping the structural changes that accompany protein-protein interactions (STINT-NMR). The method entails sequentially expressing two (or more) proteins within a single bacterial cell in a time-controlled manner and monitoring the protein interactions using in-cell NMR spectroscopy. The resulting spectra provide a complete titration of the interaction and define...
31P NMR 2D Mapping of Creatine Kinase Forward Flux Rate in Hearts with Postinfarction Left Ventricular Remodeling in Response to Cell Therapy.
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