Brain creatine kinase

Nguyen thi Man, Cartwright, A J., Osborne, M., and Morris, G E (1991) Structural changes in the C-terminal region of human brain creatine kinase studied with monoclonal antibodies Biochim Biophys. Acta 1076, 245-251. 

Morris, G. E and Nguyen thi Man (1992) Changes at the N-termmus of human brain creatine kinase during a transition between inactive folding intermediate and active enzyme Biochim. Biophys. Acta 1120,233-238. 

Cadoux-Hudson, T.A., Blackledge, M.J., Radda, G.K. (1989). Imaging of human brain creatine kinase activity in vivo. FASEB J. 3,2660-2666. 

C19. Coolen, R. B., Herbstman, R., and Hermann, P., Spurious brain creatine kinase in serum from patients with renal disease. Clin. Chem. (Winston-Salem, N.C.) 24, 1636-1638 (1978). 

Creatine kinase, creatine kinase myocardial band Creatine kinase (CK) enzymes are found in many isoforms, with varying concentrations depending on the type of tissue. Creatine kinase is a general term used to describe the nonspecific total release of all types of CK, including that found in skeletal muscle (MM), brain (BB) and heart (MB). CK MB is released into the blood from necrotic myocytes in response to infarction and is a useful laboratory test for diagnosing myocardial infarction. If the total CK is elevated, then the relative index (RI), or fraction of the total that is composed of CK MB, is calculated as follows RI = (CK MB/CK total) x 100. An RI greater than 2 is typically diagnostic of infarction. 

Jost, C. R., Van Der Zee, C. E., In t Zandt, H. J. etal. Creatine kinase B-driven energy transfer in the brain is important for habituation and spatial learning behaviour, mossy fibre field size and determination of seizure susceptibility. Eur. J. Neurosci. 15 692-706, 2002. 

The enzyme creatine kinase (CK) is formed of two subunits that can either be of the brain (B) type or the muscle (M) type, and different combinations of these types lead to isozymes that predominate in the brain (BB), skeletal muscle (MM), and heart muscle (MB). 

Measurement of creatine kinase reaction rate in human brain using magnetization transfer image-selected in vivo spectroscopy (MT-ISIS) and a volume radiofre-... 

Wyss, M. Schlegel, J. James, P. Eppenberger, H.M. Wallimann, T. Mitochondrial creatine kinase from chicken brain. Purification, biophysical characterization, and generation of heterodimeric and heterooctameric molecules with subunits of other creatine kinase isoenzymes. J. Biol. Chem., 265, 15900-15908 (1990)... 

H.M. Wallimann, T, Perriard, J.-C. Distinct tissue specific mitochondrial creatine kinases from chicken brain and striated muscle with a conserved CK framework. Biochem. Biophys. Res. Commun., 151, 408-416 (1988)... 

Buist, R. Kroeker, S. Peeling, J. Temperature dependence of the creatine kinase reaction measured in rat brain in vivo by 31P NMR saturation transfer. Can. J. Chem., 77, 1887-1891 (1999)... 

Kanemitsu, E Mizushima, J. Kageoka, T. Okigaki, T. Taketa, K. Kira, S. Characterization of two types of mitochondrial creatine kinase isolated from normal human cardiac muscle and brain tissue. Electrophoresis, 21, 266-270 (2000)... 

K. Crystal structure of brain-type creatine kinase at 1.41 A resolution. Protein Sci., 8, 2258-2269 (1999)... 

Phosphocreatine (Fig. 13-5), also called creatine phosphate, serves as a ready source of phosphoryl groups for the quick synthesis of ATP from ADP. The phosphocreatine (PCr) concentration in skeletal muscle is approximately 30 nra, nearly ten times the concentration of ATP, and in other tissues such as smooth muscle, brain, and kidney [PCr] is 5 to 10 mM. The enzyme creatine kinase catalyzes the reversible reaction... 

Creatine kinase sequences are known for many different species and iso-forms, so species-specificity of MAbs can often be used for refining the details of epitope mapping. Natural variants that prevent MAb binding are likely to involve contact residues, because the overall protein structures (and enzyme activity) are likely to be retained. The CK-2A7 MAb in Fig. IB binds between Met-29 and Cys-73. It recognizes rabbit and Torpedo CKs, as well as chick CK, but it fails to bind to either rat muscle CK or rabbit brain CK. This suggests that Lys-39 is required for CK-2A7 binding, since it is replaced by Asn m rat muscle CK and by Ala in rabbit brain CK (7), and is the only amino acid change consistent with the observed CK-2A7 specificity. 

W. M., Booze, R., Markesbery, W. R., Butterfield, D. A. Proteomic identification of oxidatively modified proteins in Alzheimer s disease brain. Part I creatine kinase BB, glutamine synthase, and ubiq-uitin carboxy-terminal hydrolase L-l. Free Radical Biol. Med. 2002, 33 562-571. 

Creatine kinase (CK) is a dimeric enzyme with two subunits, M (muscle type) and B (brain type). Three isozymes are distinguished CK 1-BB (brain), CK 2-MB (heart), and CK 3-MM (skeletal muscle). The total CK activity found in skeletal muscle is almost entirely of the CK 3 type, that in heart muscle is 15-20% CK 2 and the remainder CK 3, and that in brain is all CK 1. In the human being, the only significant source of blood CK 2 is the heart muscle. Because the intact blood-brain barrier appears to be impermeable to CK, the occurrence of CK 1 in blood is unlikely. The total serum CK activity in healthy individuals is almost exclusively that of CK 3. 

The patient, a 63-year-old Caucasian female, was hospitalized on 4 April 2002 though 10 April 2002 for a non-ST segment elevation myocardial infarction (non-Q-wave MI per chart documentation). She had a negative adenosine stress test after the initial event. Her serum cardiac-specific troponin I (cTnl) concentration 24 hours after her onset of chest pain was 1.4 pg/L (upper limit of normal is 0.3 ng/mL), and her creatine kinase (CK) MB level was 12.5 pg/L (upper limit of normal 6.0 ng/mL). Three days post-event her cTnl level was 0.5 pg/L and her CK-MB level was 4.5 pg/L (Fig. 5-1). MB refers to one of the isoenzyme forms of CK found in serum. The form of the enzyme that occurs in brain (BB) does not usually get past the blood-brain barrier and therefore is not normally present in the serum. The MM and MB forms account for almost all of the CK in serum. Skeletal muscle contains mainly MM, with less than 2% of its CK in the MB form. MM is also the predominant myocardial creatine kinase and MB accounts for 10%-20% of creatine kinase in heart muscle. 

Creatine kinase (CK) occurs in high concentrations in the brain, cardiac and skeletal muscle and is elevated in the blood with muscle damage. A rise in CK is seen in acute myocardial infarction but also in other conditions. A more specific marker is creatine kinase MB (CK-MB), which is an isoenzyme of creatine kinase that is more specific for cardiac muscle damage. CK or CK-MB will rise approximately 4 hours after an acute cardiac event and will reach a peak after approximately 24 hours and will remain raised for 3-4 days. 

Creatine kinase (CK) catalyzes the phosphorylation of creatine by adenosine triphosphate. CK is a dimer consisting of two subunits, M (muscle) and B (brain). There are three isoenzymes, CKl (BB), CK2 (MB), and CK3 (MM). CKl is present in the brain, prostate gland, gastrointestinal tract, lung, bladder, uterus, and placenta. Cardiac muscle has the highest concentration of CK2 (= 20%). CK3 is present in skeletal and cardiac muscles. 

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