Creatine kinase activity in the assessment of muscle injuries following lateral  recumbency and standing restraint positions for rumenotomy in Kano-Brown Goats

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.

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Skeletal muscle collagen content in humans after high-force eccentric contractions

Journal of Applied Physiology ◽

10.1152/japplphysiol.01174.2003 ◽

2004 ◽

Vol 97 (1) ◽

pp. 197-203 ◽

Cited By ~ 66

Author(s):

Abigail L. Mackey ◽

Alan E. Donnelly ◽

Taina Turpeenniemi-Hujanen ◽

Helen P. Roper

Keyword(s):

Creatine Kinase ◽

Kinase Activity ◽

Staining Intensity ◽

Creatine Kinase Activity ◽

Serum Creatine Kinase ◽

Muscle Contractions ◽

Tissue Inhibitors Of Metalloproteinases ◽

Eccentric Contractions ◽

Knee Extensors ◽

Type Iv

The purpose of this study was to investigate the effects of high-force eccentric muscle contractions on collagen remodeling and on circulating levels of matrix metalloproteinases (MMP) and tissue inhibitors of metalloproteinases (TIMP) in humans. Nine volunteers [5 men and 4 women, mean age 23 (SD 4) yr] each performed a bout of 100 maximum voluntary eccentric contractions of the knee extensors. Muscle biopsies were taken before exercise and on days 4 and 22 afterward. Image analysis of stained tissue sections was used to quantify endomysial collagen staining intensity. Maximum voluntary contractile isometric force was recorded preexercise and on days 1, 2, 3, 4, 8, 11, and 14 postexercise. Venipuncture blood samples were also drawn on these days for measurement of serum creatine kinase activity and concentrations of MMP-9, TIMP-1, TIMP-2, and the MMP-2/TIMP-2 complex. Maximum voluntary contractile force declined by 39 ± 23% (mean ± SD) on day 2 postexercise and recovered thereafter. Serum creatine kinase activity peaked on day 4 postexercise ( P < 0.01). Collagen type IV staining intensity increased significantly on day 22 postexercise to 126 ± 29% (mean ± SD) of preexercise values ( P < 0.05). Serum MMP-9 levels increased on day 8 postexercise ( P < 0.01), and serum TIMP-1 was also significantly elevated on days 1, 2, 3, 4, and 14 postexercise ( P < 0.05). These results suggest that a single bout of eccentric muscle contractions results in remodeling of endomysial type IV collagen, possibly via the MMP pathway.

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Inhibition of creatine kinase activity by lysine in rat cerebral cortex

Metabolic Brain Disease ◽

10.1007/s11011-009-9131-z ◽

2009 ◽

Vol 24 (2) ◽

pp. 349-360 ◽

Cited By ~ 9

Author(s):

Anelise Miotti Tonin ◽

Gustavo Costa Ferreira ◽

Patrícia Fernanda Schuck ◽

Carolina Maso Viegas ◽

Ângela Zanatta ◽

...

Keyword(s):

Creatine Kinase ◽

Cerebral Cortex ◽

Kinase Activity ◽

Creatine Kinase Activity ◽

Rat Cerebral Cortex

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A "Reagentless" Fluorometric Method for Creatine Kinase Activity in Serum

Clinical Chemistry ◽

10.1093/clinchem/19.9.1045 ◽

1973 ◽

Vol 19 (9) ◽

pp. 1045-1048 ◽

Cited By ~ 10

Author(s):

Herbert K Y Lau ◽

George G Guilbault

Keyword(s):

Creatine Kinase ◽

Silicone Rubber ◽

Kinase Activity ◽

Creatine Kinase Activity ◽

Serum Creatine Kinase ◽

Fluorometric Method ◽

Nadh Fluorescence

Abstract A "reagentless" fluorometric method is described for the analysis of serum creatine kinase (CK) activity. The method is based on the use of silicone rubber pads, upon which are placed all the reagents for assay of CK. The rate of formation of NADH fluorescence at 460 nm is measured and equated to CK activity. The method is simple, rapid, inexpensive, and as little as 3 µl of serum is needed.

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