Absorption and distribution of sodium [2-14C]barbital in tissues of normal and dystrophic mice

1978 ◽  
Vol 56 (1) ◽  
pp. 76-82
Author(s):  
Heather R. Stephens ◽  
Denis Nadeau ◽  
Edmund B. Sandborn
Keyword(s):  
Skeletal Muscle ◽  
Gastrointestinal Tract ◽  
Gastric Emptying ◽  
Oral Administration ◽  
Distribution Volume ◽  
Tissue Concentrations ◽  
Dystrophic Mouse ◽  
Rapid Absorption ◽  
Dystrophic Mice ◽  
Mutant Homozygote

The absorption and distribution of [2-14C]barbital after oral administration was studied in various tissues, including skeletal muscle, of normal and dystrophic mice. There appeared to be a more rapid gastric emptying in the mutant homozygote as reflected in lower levels of the drug recuperated from the gastrointestinal tract. This resulted in initially higher plasma and tissue concentrations of barbital in the dystrophic mice. Two hours after oral administration, this kinetic profile was reversed so that less barbital remained in the tissues of the dystrophic mouse. The tissue:plasma concentration ratios were consistently, but not significantly, higher in all tissues of the dystrophic animals. Analysis of the half-life of the drug in both groups suggests that there is an increase in the distribution volume of barbital in the dystrophic mice. The phenomenon of more rapid absorption of the barbiturate seems to be more consistent as the symptoms of the disease progress. The altered absorption and disposition of barbital in various tissues of the dystrophic mouse support the concept that a generalized multisystemic disorder may be crucial to the pathogenesis of murine muscular dystrophy, in contradistinction to a purely myogenic origin.

Biochemical changes in progressive muscular dystrophy. XIV. Skeletal muscle myosin mRNA translatability in dystrophic mice

1987 ◽  
Vol 65 (9) ◽  
pp. 833-841 ◽  
Author(s):  
U. S. Srivastava ◽  
E. A. Sugden ◽  
P. K. Majumdar ◽  
M. L. Thakur ◽  
G. M. Bhatnagar
Keyword(s):  
Skeletal Muscle ◽  
Muscular Dystrophy ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Cdna Probe ◽  
Sodium Dodecyl ◽  
Mouse Muscle ◽  
Skeletal Muscle Myosin ◽  
Dystrophic Mouse ◽  
Dystrophic Mice

Variations in the content and translatability of the poly(A)+ RNA and mRNA molecules coding for myosin (M) were studied in the hind leg muscles of genetically dystrophic mice. The poly(A)+ RNA content of total skeletal muscle failed to increase normally during progression of the disease. M mRNA, isolated from dystrophic murine muscle poly(A)+ RNA, was mostly found to be associated with the 26S RNA species. The translation of M mRNA in an in vitro heterologous wheat germ system was lower at 8 and 16 weeks in the dystrophic group as compared with the controls. Analysis of the translation products via sodium dodecyl sulfate – polyacrylamide gel electrophoresis, autoradiography, and densitometric autoradiographic tracing demonstrated the gradual disappearance of a protein band corresponding to M, the major component of skeletal muscle. cDNA was synthesized, using M mRNA that was isolated and purified from normal and dystrophic mouse muscle as a template. Total radioactivity was measured in some cDNA fractions produced from normal and dystrophic mouse muscle, while other fractions were utilized for separation and sizing of cDNA by disc gel electrophoresis. The cDNA from normal muscle was hybridized with M mRNA from normal and 16-week-old dystrophic mouse muscles. The cDNA probe, hybridization experiments, and studies involving the content and synthesis of M mRNA suggest that murine muscular dystrophy elicited a shorter species of mRNA or shorter sequences of the same species of mRNA coding for M. Not all poly(A)+ mRNA sequences coding for M, found in control mice, were present in their dystrophic counterparts. In conclusion, it appears that murine muscular dystrophy produces a shorter species of pre-M mRNA via decreased polynucleotide elongation.

Pharmacokinetics and urinary excretion of orally administered diiodotyrosine

1987 ◽  
Vol 116 (3) ◽  
pp. 395-398
Author(s):  
H. Meinhold ◽  
R. Finke ◽  
U. Bogner ◽  
H. Schleusener
Keyword(s):  
Gastrointestinal Tract ◽  
Oral Administration ◽  
Urinary Excretion ◽  
Normal Subjects ◽  
Serum Levels ◽  
Time Interval ◽  
Rapid Absorption ◽  
Metabolic Degradation ◽  
Excretion Rates

Abstract. Serum levels of diiodotyrosine (DIT) and urinary excretion rates of DIT and iodine were measured in 10 normal subjects after oral administration of 1.57 μmol of DIT corresponding to 400 μg of iodine. Serum DIT concentrations rose promptly from a mean endogenous basal level of 0.23 nmol/l to maximum values between 6.0 and 20 nmol/l within 30 min to 1 h after DIT ingestion. Decreasing DIT levels were found in all subjects 2 h after DIT intake. Urinary excretion of intact DIT was low, being less than 1% of the administered dose of exogenous DIT within 2 days. In contrast, 52% of the iodine administered in the form of DIT was excreted in the urine in the same time interval. The rapid absorption of DIT from the gastrointestinal tract combined with rapid and almost complete metabolic degradation by deiodination make orally applied DIT seem a suitable iodine carrier compound for therapeutic purposes.

Enzyme studies of skeletal muscle in mice with hereditary muscular dystrophy

1963 ◽  
Vol 205 (5) ◽  
pp. 897-901 ◽  
Author(s):  
Marilyn W. McCaman
Keyword(s):  
Skeletal Muscle ◽  
Muscular Dystrophy ◽  
Glutathione Reductase ◽  
Enzyme Activities ◽  
Lactic Dehydrogenase ◽  
Normal Muscle ◽  
Dystrophic Muscle ◽  
Nerve Section ◽  
Mouse Muscle ◽  
Dystrophic Mouse

The activities of 20 enzymes in normal, heterozygous, and dystrophic mouse muscle were studied by means of quantitative microchemical methods. Enzyme activities in normal and heterozygous muscle were essentially the same. In dystrophic muscle glucose-6-P dehydrogenase, 6-P-gluconic dehydrogenase, glutathione reductase, peptidase, ß-glucuronidase, and glucokinase activities were significantly higher than in normal muscle, while α-glycero-P dehydrogenase and lactic dehydrogenase activities were significantly lower. The pattern of enzyme activities found in normal gastrocnemius denervated by nerve section was strikingly similar to that in dystrophic muscle.

CYTOCHROME c CONCENTRATIONS DURING RAT AND GUINEA PIG DEVELOPMENT

PEDIATRICS ◽  
1964 ◽  
Vol 33 (1) ◽  
pp. 106-110
Author(s):  
Peter R. Dallman ◽  
Herbert C. Schwartz
Keyword(s):  
Skeletal Muscle ◽  
Cytochrome C ◽  
Guinea Pig ◽  
Mammalian Species ◽  
Fetal Tissue ◽  
Developmental Pattern ◽  
Newborn Rat ◽  
Tissue Concentrations ◽  
Functional Changes

Cytochrome c concentrations were determined in tissues of the rat and the guinea pig, two mammalian species of contrasting developmental pattern. The relatively mature newborn guinea pig had approached adult concentrations of cytochrome c by one day of age. The less mature newborn rat did not attain comparable values until later in its development. The increase from the low fetal tissue concentrations to adult values occurred in the following sequence: heart concentrations increased earliest, followed by brain, skeletal muscle, and liver. Renal concentrations were the last to rise. Changes in cytochrome c concentration could be related to functional changes within these tissues as well as the over-all pattern of maturation represented by each of these species.

Oral administration of MSG increases expression of glutamate receptors and transporters in the gastrointestinal tract of young piglets

Amino Acids ◽  
2013 ◽  
Vol 45 (5) ◽  
pp. 1169-1177 ◽  
Author(s):  
Jun Zhang ◽  
Yulong Yin ◽  
Xu Gang Shu ◽  
Tiejun Li ◽  
Fengna Li ◽  
...  
Keyword(s):  
Gastrointestinal Tract ◽  
Oral Administration ◽  
Glutamate Receptors

Influence of diet on transamidinase activity in dystrophic mice

1960 ◽  
Vol 199 (5) ◽  
pp. 927-930 ◽  
Author(s):  
D. L. Coleman ◽  
M. E. Ashworth
Keyword(s):  
Dystrophic Mouse ◽  
Dystrophic Mice

The activities of the enzymes involved in creatine synthesis were studied in normal and dystrophic mice maintained on two commercial mouse chows. Kidney transamidinase activity in the dystrophic mouse was found to vary from 150 to –50% of the normal depending on the diet fed while the activity of the enzyme in the control mice remained unaltered. Addition of protein or glycine to the diet normally causing the lower transamidinase values resulted in increased enzyme levels equal to those found in animals maintained on the diet normally producing the higher enzyme levels.

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