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 Blood Biomarkers of Recovery Efficiency in Soccer Players

2019 ◽  
Vol 16 (18) ◽  
pp. 3279 ◽  
Author(s):  
Anna Nowakowska ◽  
Dorota Kostrzewa-Nowak ◽  
Rafał Buryta ◽  
Robert Nowak
Keyword(s):  
Alkaline Phosphatase ◽  
Creatine Kinase ◽  
Lactate Dehydrogenase ◽  
Alanine Aminotransferase ◽  
Soccer Players ◽  
Control Group ◽  
Iron Level ◽  
Recovery Efficiency ◽  
Lactate Dehydrogenase Activity ◽  
Over Time

Physical exercise strongly affects human metabolism and causes biochemical changes. This study aimed to investigate the relationship between routine plasma biomarker levels and recovery efficiency in soccer players during an entire competitive match season. The players participating in the study were divided into a midfielder/defender group (seven midfielders and seven defenders) and a goalie/substitute group (six persons—goalkeepers and players with a short cumulative match-time). The fasting capillary blood samples were taken 17–24 h after each competitive match. The blood plasma was used to determine the creatinine, urea, alkaline phosphatase, creatine kinase, lactate dehydrogenase, aspartate and alanine aminotransferase, iron and magnesium levels of the athletes. The levels of (AST) (aspartate aminotransferase), (ALT) (alanine aminotransferase) and (Cr) creatinine were higher in the midfielder/defender group than in the control group, but only AST and Cr significantly varied over time (AST decreased, and Cr increased with time). The (LDH) (lactate dehydrogenase) activity and urea level were significantly lower in the midfielder/defender group than in the goalie/substitute group, and it significantly varied over time (LDH decreased, and urea increased with time). No differences in the (CK) creatine kinase and (ALP) alkaline phosphatase activities between the groups was found, although CK increased significantly with time in the midfielder/defender group (particularly midfielders in the spring round). In midfielders, the AST activity and the iron level were significantly lower in the spring than in the autumn round. On the contrary, ALT, CK, urea and magnesium levels were significantly higher in the spring than in autumn round. A long-term measurement of biochemical parameters in elite soccer players indicated that AST, CK, LDH and creatinine levels, when analyzed together, could constitute a useful set of markers for monitoring recovery periods.

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.

scholarly journals Standards versus Standardised Methods in Enzyme Assay

1983 ◽  
Vol 20 (1) ◽  
pp. 52-59 ◽  
Author(s):  
R T P Jansen ◽  
A P Jansen
Keyword(s):  
Quality Control ◽  
Alkaline Phosphatase ◽  
Creatine Kinase ◽  
Lactate Dehydrogenase ◽  
Alanine Aminotransferase ◽  
Enzyme Assay ◽  
Control Program ◽  
Internal Quality ◽  
Quality Control Program ◽  
Control Serum

In a trial of the Netherlands coupled external/internal quality control program a control serum and an enzyme standard were analysed over a period of eight weeks, five times each week. Five enzymes were determined: alkaline phosphatase, creatine kinase, lactate dehydrogenase, alanine aminotransferase, and γ-glutamyltransferase. The measured values in the serum were converted to the standards. Those laboratories using the recommended methods also submitted their non-transformed serum values. The following standardisation techniques have been compared: ( a) no standardisation of methodology but use of enzyme standards; ( b) standardisation of methodology; ( c) standardisation of methodology combined with use of an enzyme standard. Results were submitted to analysis of variance. Standardisation of methodology did not yield smaller interlaboratory variation than the standardisation with enzyme standards. In this trial a combination of both standardisation techniques yielded generally better results. Results for γ-glutamyltransferase indicate that standardisation of substrate may be necessary apart from the use of an enzyme standard. The preparation of stable enzyme standards is stressed.

scholarly journals STUDIES ON THE INTERMEDIARY CARBOHYDRATE METABOLISM OF AQUATIC ANIMALS

1948 ◽  
Vol 31 (4) ◽  
pp. 347-359 ◽  
Author(s):  
Kenneth P. DuBois ◽  
E. M. K. Geiling ◽  
Arthur F. McBride ◽  
John F. Thomson
Keyword(s):  
Skeletal Muscle ◽  
Body Weight ◽  
Cardiac Muscle ◽  
Enzyme Activities ◽  
Glycogen Content ◽  
Succinic Dehydrogenase ◽  
Total Body Weight ◽  
Rat Tissues ◽  
Malic Dehydrogenase ◽  
Total Body

1. Liver, kidney, brain, skeletal muscle, and cardiac muscle from one newborn and three adult long-snouted dolphins (Stenella plagiodon) were obtained for enzyme studies. 2. All of the dolphin tissues exhibited cytochrome oxidase, succinic dehydrogenase, and malic dehydrogenase activity. Considerable differences in the enzyme activities of the various tissues were noted, with cardiac muscle exhibiting the highest respiratory enzyme activity. The enzyme activities of dolphin tissues were lower than those of the corresponding rat tissues. 3. All of the dolphin tissues exhibited adenosine triphosphatase activity which was accelerated by magnesium and manganese but, in contrast to rat tissues, was only slightly activated by calcium. 4. Measurements of the distribution of acid-soluble phosphorus in dolphin tissues indicated that glycolysis in all of the tissues examined proceeded through the Emden-Meyerhof phosphorylation scheme. 5. The average glycogen content of dolphin skeletal muscle was 0.98 per cent as compared with 0.16 to 0.20 per cent for rat skeletal muscle. The high glycogen content of dolphin skeletal muscle indicates a ready source of substrate for glycolysis even during submergence when the blood supply may be differentially shunted to other organs. 6. Measurements of the organ weights of dolphins showed that the lungs occupy over three times and the liver one-half as much of the total body weight as do these organs in the rat. The heart and the thyroid gland of the dolphin are also larger in proportion to the total body weight than in the rat while the relative weights of the other tissues in the two species are about the same.

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.

scholarly journals Influence of 8-Hour Road Transportation on Selected Physiological Parameters in Horses

2012 ◽  
Vol 56 (2) ◽  
pp. 193-197 ◽  
Author(s):  
Artur Niedźwiedź ◽  
Marcin Zawadzki ◽  
Henryk Filipowski ◽  
Józef Nicpoń
Keyword(s):  
Alkaline Phosphatase ◽  
Creatine Kinase ◽  
Total Protein ◽  
Aspartate Aminotransferase ◽  
Alanine Aminotransferase ◽  
Total Bilirubin ◽  
Physiological Responses ◽  
Venous Blood ◽  
Road Transportation ◽  
Physiological Variables

Abstract The objective of this study was to assess the physiological responses in mature healthy horses prior to an 8 h transport, as well as immediately and 24 h after transportation in a horse truck, under autumn conditions typical for central Poland. The study was conducted on a group of 60 horses of different breed. Horses ranged from 4 to 10 years of age. Venous blood was taken 3 times: I - directly before loading the horses to the trailer, II - directly after unloading the horses from the trailer, III - after period of 24 h resting. There was no change in the concentrations of urea, cholesterol, creatinine, and magnesium and in the activity of alkaline phosphatase during the three subsequent samplings. Albumin, total protein, alanine aminotransferase, aspartate aminotransferase, total bilirubin, creatine kinase, and triglycerides were mostly influenced by the transport. The obtained results indicate that the transportation of horses alters concentrations of physiological variables of their metabolism.

Sign in / Sign up

Export Citation Format

Share Document