Rapid In Vivo Quantification of Creatine Kinase Activity by Phosphorous-31 Magnetic Resonance Spectroscopic Fingerprinting (31P-MRSF)

2021 ◽  
pp. 597-609
Author(s):  
Charlie Wang ◽  
Kihwan Kim ◽  
Xin Yu
Keyword(s):  
Creatine Kinase ◽  
Magnetic Resonance ◽  
Kinase Activity ◽  
Creatine Kinase Activity

Adriamycin-induced changes of creatine kinase activity in vivo and in cardiomyocyte culture

Toxicology ◽  
1999 ◽  
Vol 134 (1) ◽  
pp. 51-62 ◽  
Author(s):  
S.Michael DeAtley ◽  
Michael Y. Aksenov ◽  
Marina V. Aksenova ◽  
Brad Jordan ◽  
John M. Carney ◽  
...  
Keyword(s):  
Creatine Kinase ◽  
Kinase Activity ◽  
Creatine Kinase Activity ◽  
Cardiomyocyte Culture ◽  
Induced Changes

Imaging of human brain creatine kinase activity in vivo

1989 ◽  
Vol 3 (14) ◽  
pp. 2660-2666 ◽  
Author(s):  
Thomas A. Cadoux‐Hudson ◽  
Martin J. Blackledge ◽  
George K. Radda
Keyword(s):  
Creatine Kinase ◽  
Human Brain ◽  
Kinase Activity ◽  
Creatine Kinase Activity ◽  
Brain Creatine Kinase

Maturational changes in respiratory control through creatine kinase in heart in vivo

1992 ◽  
Vol 263 (2) ◽  
pp. C453-C460 ◽  
Author(s):  
M. A. Portman ◽  
X. H. Ning
Keyword(s):  
Creatine Kinase ◽  
Oxygen Consumption ◽  
Kinase Activity ◽  
Respiratory Control ◽  
Atp Synthesis ◽  
Developmental State ◽  
Creatine Kinase Activity ◽  
Total Creatine Kinase Activity ◽  
Total Creatine

The role of creatine kinase in regulation of myocardial respiration was studied in vivo as a function of maturation. Unidirectional creatine kinase flux (JCK), phosphocreatine to gamma-ATP, was measured in newborn lambs (age 3-9 days, n = 8) and mature sheep (age 30-60 days, n = 6) using 31P saturation transfer techniques, and total creatine kinase activity was measured using standard methods. Myocardial oxygen consumption (MVO2) was measured simultaneously via an extracorporeal shunt from the coronary sinus as cardiac work was increased via epinephrine (1-3 micrograms.kg-1.min-1). Findings were as follows: 1) baseline newborn JCK was markedly lower than in mature sheep despite higher levels of MVO2, and this could be related to a decrease in total creatine kinase activity; 2) JCK was substantially higher than the rate of ATP synthesis in both groups at baseline rates of oxygen consumption; and 3) JCK decreased significantly in newborns during increases in MVO2, whereas there was no change in flux rate in the mature sheep during even larger relative changes in work and oxygen consumption. These data imply that creatine kinase does not limit oxidative phosphorylation. However, this enzyme system probably maintains at least an indirect role in respiratory control that is a function of the myocardial developmental state.

scholarly journals The Triterpenoid Betulin Protects against the Neuromuscular Effects ofBothrops jararacussuSnake VenomIn Vivo

2015 ◽  
Vol 2015 ◽  
pp. 1-10 ◽  
Author(s):  
Miriéle Cristina Ferraz ◽  
Jhones Luiz de Oliveira ◽  
Joel Reis de Oliveira Junior ◽  
José Carlos Cogo ◽  
Márcio Galdino dos Santos ◽  
...  
Keyword(s):  
Creatine Kinase ◽  
Single Dose ◽  
Tibialis Anterior ◽  
Kinase Activity ◽  
Similar Efficacy ◽  
Creatine Kinase Activity ◽  
Plasma Creatine Kinase ◽  
Partial Blockade

We confirmed the ability of the triterpenoid betulin to protect against neurotoxicity caused byBothrops jararacussusnake venomin vitroin mouse isolated phrenic nerve-diaphragm (PND) preparations and examined its capability ofin vivoprotection using the rat external popliteal/sciatic nerve-tibialis anterior (EPSTA) preparation. Venom caused complete, irreversible blockade in PND (40 μg/mL), but only partial blockade (~30%) in EPSTA (3.6 mg/kg, i.m.) after 120 min. In PND, preincubation of venom with commercial bothropic antivenom (CBA) attenuated the venom-induced blockade, and, in EPSTA, CBA given i.v. 15 min after venom also attenuated the blockade (by ~70% in both preparations). Preincubation of venom with betulin (200 μg/mL) markedly attenuated the venom-induced blockade in PND; similarly, a single dose of betulin (20 mg, i.p., 15 min after venom) virtually abolished the venom-induced decrease in contractility. Plasma creatine kinase activity was significantly elevated 120 min after venom injection in the EPSTA but was attenuated by CBA and betulin. These results indicate that betulin given i.p. has a similar efficacy as CBA given i.v. in attenuating the neuromuscular effects ofB. jararacussuvenomin vivoand could be a useful complementary measure to antivenom therapy for treating snakebite.

Distribution of serum creatine kinase activity in young healthy persons

1999 ◽  
Vol 279 (1-2) ◽  
pp. 107-115 ◽  
Author(s):  
Eli I. Lev ◽  
Ilan Tur-Kaspa ◽  
Isaac Ashkenazy ◽  
Anat Reiner ◽  
David Faraggi ◽  
...  
Keyword(s):  
Creatine Kinase ◽  
Kinase Activity ◽  
Creatine Kinase Activity ◽  
Serum Creatine Kinase ◽  
Healthy Persons

scholarly journals Ability of adenovirus 5 E1A proteins to suppress differentiation of BC3H1 myoblasts correlates with their binding to a 300 kDa cellular protein.

1992 ◽  
Vol 3 (10) ◽  
pp. 1107-1115 ◽  
Author(s):  
J S Mymryk ◽  
R W Lee ◽  
S T Bayley
Keyword(s):  
Creatine Kinase ◽  
Kinase Activity ◽  
Cellular Protein ◽  
Creatine Kinase Activity ◽  
Cellular Proteins ◽  
Deletion Mutants ◽  
Transcriptional Enhancers ◽  
Actin Mrna ◽  
Alpha Actin ◽  
Adenovirus 5

We have used deletion mutants to define the regions in Ad5 E1A proteins necessary to suppress differentiation of mouse BC3H1 myoblasts. We examined the differentiation of cells infected at a low multiplicity with viruses containing the E1A deletions and constructed so as to produce only the smaller of the two major E1A proteins. Only four of the mutant viruses containing deletions within the N-terminal 69 residues failed to suppress differentiation as judged by changes in morphology and in levels of muscle-specific alpha-actin mRNA and creatine kinase activity. The results were confirmed by analyses of lines of cells stably transfected with representative E1A mutants. The mouse cellular proteins to which mutant E1A proteins bound were identified by immunoprecipitating E1A proteins specifically from infected BC3H1 cells and by analyzing the precipitates on denaturing gels. Bands of proteins of 300, 130, 107, 105 (the retinoblastoma product), and 60 kDa (cyclin A) were distinguished. Failure to suppress differentiation correlated with loss of binding to the 300-kDa protein but not to any of the others. The regions of E1A defined in this way have been shown to be required for several other activities, including enhancer repression and transformation. One function of the 300-kDa protein appears to be to facilitate the action of transcriptional enhancers of differentiation-specific genes.

Sign in / Sign up

Export Citation Format

Share Document