Comparative enzymology of AMP deaminase, adenylate kinase, and creatine kinase in vertebrate heart and skeletal muscle: the characteristic AMP deaminase levels of skeletal versus cardiac muscle are reversed in the North American toad

1993 ◽  
Vol 163 (3) ◽  
Author(s):  
W.N. Fishbein ◽  
J.I. Davis ◽  
J.W. Foellmer
Keyword(s):  
Skeletal Muscle ◽  
Creatine Kinase ◽  
Cardiac Muscle ◽  
North American ◽  
Adenylate Kinase ◽  
Amp Deaminase ◽  
American Toad ◽  
The North ◽  
Comparative Enzymology

scholarly journals Different regulatory sequences control creatine kinase-M gene expression in directly injected skeletal and cardiac muscle.

1993 ◽  
Vol 13 (2) ◽  
pp. 1264-1272 ◽  
Author(s):  
C K Vincent ◽  
A Gualberto ◽  
C V Patel ◽  
K Walsh
Keyword(s):  
Gene Expression ◽  
Skeletal Muscle ◽  
Creatine Kinase ◽  
Cardiac Muscle ◽  
Serum Response Factor ◽  
Sequence Motif ◽  
Regulatory Sequences ◽  
Response Factor ◽  
Specific Expression ◽  
Serum Response

Regulatory sequences of the M isozyme of the creatine kinase (MCK) gene have been extensively mapped in skeletal muscle, but little is known about the sequences that control cardiac-specific expression. The promoter and enhancer sequences required for MCK gene expression were assayed by the direct injection of plasmid DNA constructs into adult rat cardiac and skeletal muscle. A 700-nucleotide fragment containing the enhancer and promoter of the rabbit MCK gene activated the expression of a downstream reporter gene in both muscle tissues. Deletion of the enhancer significantly decreased expression in skeletal muscle but had no detectable effect on expression in cardiac muscle. Further deletions revealed a CArG sequence motif at position -179 within the promoter that was essential for cardiac-specific expression. The CArG element of the MCK promoter bound to the recombinant serum response factor and YY1, transcription factors which control expression from structurally similar elements in the skeletal actin and c-fos promoters. MCK-CArG-binding activities that were similar or identical to serum response factor and YY1 were also detected in extracts from adult cardiac muscle. These data suggest that the MCK gene is controlled by different regulatory programs in adult cardiac and skeletal muscle.

SKELETAL MUSCLE CREATINE KINASE DEFICIENCY (MCK-D) INDUCES HIGH AFFINITY AMP DEAMINASE KINETICS 1307

1997 ◽  
Vol 29 (Supplement) ◽  
pp. 228
Author(s):  
J. W.E. Rush ◽  
P. C. Tullson ◽  
B. Wieringa ◽  
R. L. Terjung
Keyword(s):  
Skeletal Muscle ◽  
Creatine Kinase ◽  
Amp Deaminase ◽  
Muscle Creatine Kinase ◽  
High Affinity ◽  
Muscle Creatine

Plasma and tissue enzyme activities of banded water snakes (Nerodia fasciata) and diamondback water snakes (Nerodia rhombifer)

2022 ◽  
pp. 1-10
Author(s):  
Alexandra K. Mason ◽  
Sean M. Perry ◽  
Mark A. Mitchell
Keyword(s):  
Skeletal Muscle ◽  
Alkaline Phosphatase ◽  
Creatine Kinase ◽  
Cardiac Muscle ◽  
Enzyme Activities ◽  
Alanine Aminotransferase ◽  
Mixed Model ◽  
Linear Mixed Model ◽  
Nerodia Fasciata ◽  
Water Snakes

Abstract OBJECTIVE To measure plasma and tissue activities of alkaline phosphatase, alanine aminotransferase, aspartate aminotransferase (AST), creatine kinase, and γ-glutamyltransferase in 2 snake species. ANIMALS 6 banded water snakes (Nerodia fasciata) and 6 diamondback water snakes (Nerodia rhombifer). PROCEDURES Blood was collected via the ventral tail vein to measure plasma enzyme activities. Animals were then euthanized, and samples of 9 tissues were collected from each snake: skeletal muscle, cardiac muscle, liver, spleen, lung, kidney, testicle, pancreas, and gallbladder. Tissues were frozen for 30 days, then homogenized and processed. Supernatants were collected and analyzed within 24 hours of processing. A linear mixed model was used to determine differences in enzyme activity between tissues and species and assess interactions between tissues and species. RESULTS Activities of all enzymes were found to differ significantly among tissues. There were also significant differences between species for all enzyme activities, except AST activity. The kidney had the highest alanine aminotransferase and γ-glutamyltransferase activities. Alkaline phosphatase activity was significantly highest in liver and kidney tissues than in other tissue. Creatine kinase activity was highest in skeletal muscle, followed by cardiac muscle and kidney. AST activity was present in all tissues evaluated, but was highest in liver, kidney, and cardiac muscle in both species. CLINICAL RELEVANCE Results reinforced the importance of characterizing the origin of tissue enzymes in reptiles to improve our understanding of biochemistry results and highlighted the differences that can exist in tissue enzyme activities between closely related species.

scholarly journals Suppression of Creatine Kinase-catalyzed Phosphotransfer Results in Increased Phosphoryl Transfer by Adenylate Kinase in Intact Skeletal Muscle

1996 ◽  
Vol 271 (22) ◽  
pp. 12847-12851 ◽  
Author(s):  
Petras P. Dzeja ◽  
Robert J. Zeleznikar ◽  
Nelson D. Goldberg
Keyword(s):  
Skeletal Muscle ◽  
Creatine Kinase ◽  
Adenylate Kinase ◽  
Phosphoryl Transfer

scholarly journals Analysis of muscle creatine kinase gene regulatory elements in skeletal and cardiac muscles of transgenic mice.

1996 ◽  
Vol 16 (4) ◽  
pp. 1649-1658 ◽  
Author(s):  
D B Donoviel ◽  
M A Shield ◽  
J N Buskin ◽  
H S Haugen ◽  
C H Clegg ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Creatine Kinase ◽  
Transgenic Mice ◽  
Cardiac Muscle ◽  
Muscle Cells ◽  
Regulatory Elements ◽  
Muscle Creatine Kinase ◽  
Regulatory Regions ◽  
Mouse Muscle ◽  
Muscle Creatine

Regulatory regions of the mouse muscle creatine kinase (MCK) gene, previously discovered by analysis in cultured muscle cells, were analyzed in transgenic mice. The 206-bp MCK enhancer at nt-1256 was required for high-level expression of MCK-chloramphenicol acetyltransferase fusion genes in skeletal and cardiac muscle; however, unlike its behavior in cell culture, inclusion of the 1-kb region of DNA between the enhancer and the basal promoter produced a 100-fold increase in skeletal muscle activity. Analysis of enhancer control elements also indicated major differences between their properties in transgenic muscles and in cultured muscle cells. Transgenes in which the enhancer right E box or CArG element were mutated exhibited expression levels that were indistinguishable from the wild-type transgene. Mutation of three conserved E boxes in the MCK 1,256-bp 5' region also had no effect on transgene expression in thigh skeletal muscle expression. All these mutations significantly reduced activity in cultured skeletal myocytes. However, the enhancer AT-rich element at nt - 1195 was critical for expression in transgenic skeletal muscle. Mutation of this site reduced skeletal muscle expression to the same level as transgenes lacking the 206-bp enhancer, although mutation of the AT-rich site did not affect cardiac muscle expression. These results demonstrate clear differences between the activity of MCK regulatory regions in cultured muscles cells and in whole adult transgenic muscle. This suggests that there are alternative mechanism of regulating the MCK gene in skeletal and cardiac muscle under different physiological states.

scholarly journals Muscle creatine kinase sequence elements regulating skeletal and cardiac muscle expression in transgenic mice.

1989 ◽  
Vol 9 (8) ◽  
pp. 3393-3399 ◽  
Author(s):  
J E Johnson ◽  
B J Wold ◽  
S D Hauschka
Keyword(s):  
Skeletal Muscle ◽  
Creatine Kinase ◽  
Transgenic Mice ◽  
Cardiac Muscle ◽  
Fusion Gene ◽  
Proximal Promoter ◽  
Muscle Creatine Kinase ◽  
Specific Expression ◽  
Muscle Creatine

Muscle creatine kinase (MCK) is expressed at high levels only in skeletal and cardiac muscle tissues. Previous in vitro transfection studies of skeletal muscle myoblasts and fibroblasts had identified two MCK enhancer elements and one proximal promoter element, each of which exhibited expression only in differentiated skeletal muscle. In this study, we have identified several regions of the mouse MCK gene that are responsible for tissue-specific expression in transgenic mice. A fusion gene containing 3,300 nucleotides of MCK 5' sequence exhibited chloramphenicol acetyltransferase activity levels that were more than 10(4)-fold higher in skeletal muscle than in other, nonmuscle tissues such as kidney, liver, and spleen. Expression in cardiac muscle was also greater than in these nonmuscle tissues by 2 to 3 orders of magnitude. Progressive 5' deletions from nucleotide -3300 resulted in reduced expression of the transgene, and one of these resulted in a preferential decrease in expression in cardiac tissue relative to that in skeletal muscle. Of the two enhancer sequences analyzed, only one directed high-level expression in both skeletal and cardiac muscle. The other enhancer activated expression only in skeletal muscle. These data reveal a complex set of cis-acting sequences that have differential effects on MCK expression in skeletal and cardiac muscle.

scholarly journals Muscle creatine kinase sequence elements regulating skeletal and cardiac muscle expression in transgenic mice

1989 ◽  
Vol 9 (8) ◽  
pp. 3393-3399
Author(s):  
J E Johnson ◽  
B J Wold ◽  
S D Hauschka
Keyword(s):  
Skeletal Muscle ◽  
Creatine Kinase ◽  
Transgenic Mice ◽  
Cardiac Muscle ◽  
Fusion Gene ◽  
Proximal Promoter ◽  
Muscle Creatine Kinase ◽  
Specific Expression ◽  
Muscle Creatine

Muscle creatine kinase (MCK) is expressed at high levels only in skeletal and cardiac muscle tissues. Previous in vitro transfection studies of skeletal muscle myoblasts and fibroblasts had identified two MCK enhancer elements and one proximal promoter element, each of which exhibited expression only in differentiated skeletal muscle. In this study, we have identified several regions of the mouse MCK gene that are responsible for tissue-specific expression in transgenic mice. A fusion gene containing 3,300 nucleotides of MCK 5' sequence exhibited chloramphenicol acetyltransferase activity levels that were more than 10(4)-fold higher in skeletal muscle than in other, nonmuscle tissues such as kidney, liver, and spleen. Expression in cardiac muscle was also greater than in these nonmuscle tissues by 2 to 3 orders of magnitude. Progressive 5' deletions from nucleotide -3300 resulted in reduced expression of the transgene, and one of these resulted in a preferential decrease in expression in cardiac tissue relative to that in skeletal muscle. Of the two enhancer sequences analyzed, only one directed high-level expression in both skeletal and cardiac muscle. The other enhancer activated expression only in skeletal muscle. These data reveal a complex set of cis-acting sequences that have differential effects on MCK expression in skeletal and cardiac muscle.

Macro Creatine Kinase (macro CK) in Clinical Practice

2018 ◽  
Vol 69 (8) ◽  
pp. 2107-2109
Author(s):  
Mihai Bojinca ◽  
Violeta Claudia Bojinca ◽  
Andra Rodica Balanescu ◽  
Serban Mihai Balanescu
Keyword(s):  
Skeletal Muscle ◽  
Creatine Kinase ◽  
Cardiac Muscle ◽  
Type B ◽  
Dimeric Molecule ◽  
The Brain ◽  
Persistent Elevation ◽  
Important Enzyme

Creatine kinase (CK) is an important enzyme involved in energy metabolism. CK is found in the cytosol and mitochondria of various tissues, mainly those with increased energy necessities as skeletal muscle, cardiac muscle and brain, but also in visceral tissues. CK is a dimeric molecule composed of two identical or different subunits, type M - muscular and type B - brain. The combination of M and B subunits leads to formation of three isozymes: CK - MM found mainly in the skeletal muscle, CK - BB found mainly in the brain and CK - MB found mainly in the cardiac muscle, but also in small quantities in the skeletal muscle. The serum increase of different isozymes of CK is a consequence of cell disruption in various clinical situations like physical training, rhabdomyolysis, myositis, muscular dystrophy, myocardial infarction and others, CK being an important biomarker for this diseases. Macro CK is a complex of CK and immunoglobulin (macro CK type 1) or a polymer of mitochondrial CK (macro CK type 2) that induces false and persistent elevation of CK levels that could mislead the clinician. We present a review of the literature concerning the appearance and clinical significance of macro CK.

North American Malignant Hyperthermia Population

2001 ◽  
Vol 95 (3) ◽  
pp. 594-599 ◽  
Author(s):  
Nyamkhishig Sambuughin ◽  
Yoshitatsu Sei ◽  
Kathleen L. Gallagher ◽  
Hadley W. Wyre ◽  
Daniel Madsen ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Restriction Fragment Length Polymorphism ◽  
Length Polymorphism ◽  
North American ◽  
Fragment Length Polymorphism ◽  
Single Strand Conformation Polymorphism ◽  
Ryr1 Gene ◽  
The North ◽  
Conformation Polymorphism ◽  
Restriction Fragment Length

Background Malignant hyperthermia (MH) is a disorder of skeletal muscle manifested as a life-threatening hypermetabolic crisis in susceptible individuals after exposure to inhalational anesthetics and depolarizing muscle relaxants. Mutations in the gene encoding the skeletal muscle ryanodine receptor (RYR1) are considered a common cause of the disorder, and, to date, more than 20 RYR1 mutations have been reported in European and Canadian families. Some studies suggest that differences may exist in the frequencies and distribution of mutations in the RYR1 gene between European and North American MH families the frequency and distribution of mutations in the RYR1 gene. Methods Skeletal muscle samples from 73 unrelated individuals diagnosed as MH susceptible according to the North American MH caffeine-halothane contracture test were studied. Genomic DNA of MH-susceptible patients was investigated by polymerase chain reaction-based restriction fragment length polymorphism, single-strand conformation polymorphism, and sequencing analysis. The majority of known RYR1 mutations were analyzed using the restriction fragment length polymorphism method, whereas new mutations were searched by single-strand conformation polymorphism in exons 12, 15, 39, 40, 44, 45, and 46 of the gene. Results Seven known RYR1 mutations (Arg163Cys, Gly248Arg, Arg614Cys, Val2168Met, Thr2206Met, Gly2434Arg, and Arg2454His) were detected at frequencies of 2.7, 1.4, 1.4, 1.4, 1.4, 5.5, and 4.1%, respectively. In addition, three novel amino acid substitutions (Val2214Ile, Ala2367Thr, and Asp2431Asn) were detected at frequency of 1.4% each. These 10 mutations account for 21.9% of the North American MH-susceptible population. Conclusion Three novel candidate mutations in the RYR1 gene were identified in these MH patients. The frequency and distribution of RYR1 mutations observed in this North American MH population was markedly different from that previously identified in Europe. Larger-scale studies are necessary to clarify the type and frequency of mutations in RYR1 associated with MH in North American families.

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