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PubMed1999

Variation in subcutaneous adipose tissue distribution associated with age, sex, and maturation.

Age-, sex-, and maturity-associated variation in subcutaneous adipose tissue (SAT) distribution is reviewed and then considered longitudinally in a sample of Polish youth. Current study of adipose tissue distribution places considerable emphasis on abdominal adiposity, specifically intra-abdominal or visceral adipose tissue (VAT). Most studies of children and adolescents do not include an abdominal skinfold, and when it is available, the skinfold is grouped with others as a sum of skinfolds. Correlations between abdominal VAT and SAT based on computerized tomography in non-obese children are moderate to high, and those between the suprailiac and abdominal skinfolds and abdominal VAT are moderately high. Changes in three individual skinfolds (triceps, subscapular, abdominal) and ratios of the skinfolds were considered by chronological age and relative to the timing of peak height velocity (PHV), and in children of contrasting maturity status in participants of the Wroclaw Growth Study, 193 boys and 197 girls, who were followed longitudinally from 8 to 18 years of age. Individual skinfolds behave differently during childhood and adolescence, and the changes are influenced by the timing of the adolescent growth spurt. Sex differences in estimated velocities are negligible up to about 2 years before PHV; then velocities tend to be higher in girls. The velocity of the triceps skinfold is negative in boys just before and after PHV; estimated velocities for the trunk skinfolds are positive through the growth spurt in both sexes, and are somewhat greater after PHV, especially in girls. The individuality of changes in individual skinfolds during the adolescent spurt contributes to changes in the relative distribution of SAT at this time. The timing of the adolescent growth spurt is an important factor influencing the distribution of SAT both in the total sample and in youth classified as early and late maturing. Am. J. Hum. Biol. 11:189-200, 1999. Copyright 1999 Wiley-Liss, Inc.

Journal Article↗

PubMed1987

A comparison of plasma, white blood cell, red blood cell, and tissue distribution of amiodarone and desethylamiodarone in anesthetized dogs.

Desethylamiodarone (DA) is a major metabolite of amiodarone (AM), a Class III antiarrhythmic drug. The plasma pharmacokinetics and tissue distribution of AM and DA (10 mg/kg i.v.) were compared in anesthetized dogs. Plasma, white blood cell (WBC), red blood cell (RBC), liver, and skeletal muscle samples were obtained at frequent intervals up to 6 h after a single i.v. bolus of the two drugs. Drug concentrations in these and other tissues, i.e., lung, kidney, heart (right and left atrium, right and left ventricle, Purkinje fibers, and AV node), and femoral nerve were measured by a highly sensitive and specific high-pressure liquid chromatographic technique developed in our laboratory. Four different patterns of AM and DA uptake and washout could be identified in these experiments. The first pattern is biexponential decline in plasma drug levels with a rapid distribution phase (t1/2 alpha = 5.1 +/- 2.1 min for AM and 5.5 +/- 1.2 min for DA, respectively) and a slower elimination phase (t1/2 beta = 3.7 +/- 1.3 h for AM and 4.96 +/- 0.8 h for DA, respectively). The volume of distribution of DA was significantly larger than that of AM. The second pattern is that both WBCs and RBCs showed an initial uptake within 5 min followed by a biexponential decrease in drug levels, with t1/2 alpha similar to that in plasma but t1/2 beta significantly longer than in plasma. In both these types of cells, the elimination half-life for DA was significantly longer than that of AM. The third pattern is that in the liver there was a rapid uptake of both drugs with peak concentrations at 15 min; the decline in hepatic levels of AM was biexponential, but that of DA appeared to be monoexponential. In addition, in dogs given AM alone, the metabolite (DA) was easily detected in the liver from the earliest time of measurement, suggesting that the parent drug is rapidly metabolized to DA. In the experiments where DA was injected, two new peaks were also identified in the liver suggesting that DA was metabolized further in the liver. The fourth pattern was in the skeletal muscle, where AM uptake was relatively slow, reaching peak concentrations between 1.5-2 h followed by a monoexponential decline; however, DA was rapidly taken up by skeletal muscle, but the rate of decline appeared to be slower as compared to that of AM.(ABSTRACT TRUNCATED AT 400 WORDS)

Amiodarone↗

PubMed2000

Tissue distribution and excretion of CDRI-81/470 in rats.

Methyl-N[5 [[4-(2-pyridinyl)-1-piperazinyl]carbonyl]- 1H-benzimidazol-2-yl] carbamate (CDRI-81/470) is a broad spectrum anthelmintic agent, effective against both intestinal and systemic parasitism. Tissue distribution and excretion of CDR1-81/470 were studied in rats after a single oral dose of 100 mg kg(-1) CDRI-81/470. One of the metabolites was identified in pilot studies as its N-decarboxylate derivative and characterized by synthesis. HPLC assay methods for the simultaneous estimation of CDRI-81/470 and its N-decarboxylate derivative in tissues, bile, urine, and faeces were developed and validated. The parent compound was quantitated in all major tissues and organs up to 48 h post-dose. Among the tissues other than serum, the highest concentrations of CDRI-81/470 were found in liver, whereas only trace levels were found in brain. Approximately 3% of the administered dose was excreted unchanged in urine at 120 h postdose, whereas approximately 7% was recovered in faeces. The contribution of the biliary route for the excretion of parent compound was less than 0.5%. The N-decarboxylate derivative was quantitated in faeces (1-4%) and bile ( < 0.1%) but was absent in serum, tissues, and urine. An additional metabolite was isolated from bile and characterized as the pyridinyl-5-hydroxy derivative of CDRI-81/470. CDRI-81/470 showed rapid absorption and distribution into all major organs and tissues, and underwent extensive metabolism in rats. Two metabolites in bile were identified and characterized by synthesis.

Animals↗

PubMed1999

Complementary DNA cloning, tissue distribution, and synthesis of canine brain natriuretic peptide.

OBJECTIVE: To determine complimentary DNA (cDNA) sequence and tissue distribution of canine brain natriuretic peptide (BNP), and to investigate whether synthesis of canine BNP increases in association with cardiovascular dysfunction. ANIMALS: 5 healthy adult mixed-breed dogs and 3 healthy adult Beagles. PROCEDURE: Total RNA was extracted from normal canine hearts and was used in a reverse transcription-polymerase chain reaction (RT-PCR) procedure to isolate canine BNP cDNA. Sequence of the isolated cDNA was analyzed. Gene expression of canine BNP in various tissues from 2 mixed-breed dogs was investigated, using RT-PCR and northern blot analyses. Moreover, messenger RNA (mRNA) expression of canine BNP, using northern blot analysis, was compared between grossly normal hearts from 3 Beagles and hearts from 3 mixed-breed dogs with acute myocardial infarction created by surgical ligation. RESULTS: The cDNA sequence and deduced amino acid residues of canine BNP precursor were 420 base pairs and 140 residues, respectively. Messenger RNA expression of canine BNP was detectable in the atria but not in the ventricles and the other tissues. Messenger RNA expression of canine BNP was, however, detectable in the infarcted portion of the ventricles. The amount of canine BNP mRNA in the infarcted ventricles was significantly increased, compared with that of noninfarcted ventricles. CONCLUSION: The cDNA sequence of canine BNP was determined. Expression of canine BNP mRNA was detected not only in the atria but also in infarcted ventricles. Synthesis of canine BNP increases in association with ischemic myocardial injury. Canine BNP may be used as an indicator of severity of ventricular myocardial injury.

Amino Acid Sequence↗

PubMed1994

Effects of vasoconstriction on dermal pharmacokinetics and local tissue distribution of compounds.

The effects of the local vasoconstrictor phenylephrine on the dermal absorption kinetics and local tissue distribution of compounds were investigated in rats. Phenylephrine (0.0025% -0.1%) and tracer quantities of salicylic acid, lidocaine, and water were applied in an aqueous solution to the exposed rat dermis. The disappearance of salicylic acid from the solution into the rat dermis and its appearance in blood, local underlying tissues, and similar tissues on the contralateral side was quantified. The clearance of salicylic acid into the dermis decreased and the concentrations of salicylic acid in underlying tissues increased with an increase in phenylephrine concentration (up to 0.01%). The concentrations of salicylic acid in plasma and contralateral issues decreased with increasing phenylephrine concentrations. At higher phenylephrine concentrations, no significant increase in local tissue concentrations of salicylic acid was observed. The effects of phenylephrine on local tissue levels of lidocaine and tritiated water paralleled those found for salicylic acid. The concentration-depth profiles for solutes in underlying tissues with variable blood flows were described by a compartment-in-series pharmacokinetic model in which each tissue's blood flows to and from a central compartment were incorporated. The values predicted under varying degrees of vasoconstriction were found to compare well with the experimentally determined concentrations of salicylic acid, lidocaine, and water in issues below a dermal application site, in the presence of phenylephrine. Phenylephrine can significantly increase quantities of solutes delivered to local tissues after dermal application, the observed effects being due to the vasoconstrictive properties of phenylephrine. Blood flow changes in skin can have profound effects on dermal pharmacokinetics and relative processes of local and systemic solute distribution.

Animals↗

PubMed2004

Tissue distribution of Thorotrast and role of internal irradiation in carcinogenesis.

Carcinogenesis in Thorotrastosis has been assumed due to direct bombardment by alpha-particle with high linear energy transfer during decay of 232Th. To revisit the mechanism of carcinogenesis by Thorotrast (THR), we examined the tissue distribution of THR granules and two-dimensional distribution of radioactivity in the organs of Thorotrastosis patients and studied their spatial relationship to histopathological changes. The high radioactivity in the patients' organ was predominantly derived from decay of Thorium series and showed unique distribution, while the far lower natural radioactivity was mainly from Uranium series decay and fairly evenly distributed. It was found that a large majority of THR granules were phagocytized by macrophages and were embedded in extensive fibrosis. Cancer was rarely in the center of THR deposition but rather at a distance from the deposits. These observations may indicate that the predominant feature of THR deposition is the tissue damage by direct hit of alpha-particles and subsequent fibrosis. The effect of THR resembles action of toxic chemical agents, as several authors have pointed out. We therefore assume that carcinogenesis in Thorotrastosis is a combination of events, such as regeneration of liver tissue after radiation damage, emission of secondary electrons, ionization of the surrounding tissue, and beta- or gamma-ray from daughter nuclei of Thorium (Th). In this context, the role of alpha-particle is important but more intriguing.

Aged↗

PubMed1999

Tissue distribution of mirtazapine (Remeron) in postmortem cases.

Mirtazapine (Remeron) is a member of the relatively new class of tetracyclic antidepressants. There are published cases of mirtazapine's detection as an incidental finding in postmortem cases; however, case reports with associated tissue concentrations and interpretations are not available. This report documents the tissue distribution of mirtazapine in eight postmortem cases in which it was identified but did not contribute to the cause or manner of death. The following mean mirtazapine concentrations (milligrams per liter or milligrams per kilogram) were found: heart blood 0.12 (range, < 0.01-0.33, n = 7); peripheral blood 0.09 (< 0.01-0.14, n = 4); urine 0.61 (0.01-3.2, n = 7); liver 0.88 (0.04-3.6, n = 6), kidney 0.21 (0.02-0.48, n = 5); and bile 0.62 (0.11-1.6, n = 6). In each case, the mirtazapine concentration in heart blood was approximately equal to that of peripheral blood, indicating that postmortem redistribution was not a factor in evaluating postmortem blood concentrations in these cases. However, because the liver mirtazapine concentrations were 5-30 times the blood concentrations, the potential for postmortem redistribution cannot be excluded. Additionally, because urine concentrations of the parent compound were consistently greater than the blood concentrations, urine is an adequate screening specimen for mirtazapine.

Antidepressive Agents, Tricyclic↗

PubMed1988

Tissue distribution and selective inhibition of subtypes of high affinity cAMP phosphodiesterase.

High affinity cAMP phosphodiesterase (PDE), also referred to as PDE III, or low Km PDE occurs as two subtypes. One subtype is sensitive to inhibition by cGMP while the other is relatively insensitive. To be consistent with previously recommended nomenclature, these subtypes were designated Types IV and V PDEs respectively. Tissue distribution of these subtypes of high affinity cAMP PDE was investigated using comparative potencies of specific inhibitors. Of the tissues examined, dog heart contained the highest proportion of the cGMP inhibitable form (Type IV PDE), whereas dog kidney cortex and brain were composed almost entirely of the cGMP non-inhibitable form (Type V PDE). Enoximone and other new cardiotonic drugs that inhibit high affinity cAMP PDE were shown to be specific for the cGMP inhibitable form, whereas rolipram was specific for the cGMP non-inhibitable form. The apparently partially competitive kinetics shown by one of these drugs, enoximone, was due to the presence of both subtypes of the enzyme. When the activity of the cGMP non-inhibitable form was suppressed by rolipram, competitive inhibition of the cGMP inhibitable subtype by enoximone was observed. Rat heart high affinity cAMP PDE activity contained a higher proportion of the cGMP non-inhibitable subtype than did the enzyme from dog heart. It is suggested that this may account for the relative insensitivity of rats to the cardiotonic PDE inhibitors.

3',5'-Cyclic-AMP Phosphodiesterases↗

PubMed1993

Tissue distribution and excretion of 14C-labelled cinnamic aldehyde following single and multiple oral administration in male Fischer 344 rats.

14C-labelled cinnamic aldehyde (CNMA) was given as a single oral dose, or 24 hr after multiple oral administration of non-radioactive CNMA for 7 days at 24-hr intervals, to male Fischer 344 rats at dose levels of 5, 50 or 500 mg/kg body weight. Residues of radioactive CNMA were measured. After the single dose radioactivity was distributed primarily in the gastro-intestinal tract, the kidneys and the liver of the rats. The radiolabel was excreted mainly in the urine, and at 24 hr 85.1, 84.2 and 81.2% of the administered radiolabel was recovered in the urine at the 5, 50 and 500 mg/kg dose levels, respectively. Faecal excretion of radiolabel at 24 hr for the 5, 50 and 500 mg/kg doses was 5.1, 4.0 and 3.2% of the administered dose, respectively. At all dose levels, a small amount of the dose was distributed to the fat and was easily measured in animals killed 3 days after dosing at the 50 or 500 mg/kg dose levels. Following multiple oral administration, similar tissue distribution and excretion patterns of radiolabel were found at the three dose levels. After 24 hr the administered radiolabel was distributed mainly to the fat, liver and gastro-intestinal tract. At 24 hr, recoveries of the radiolabel in the urine were 80.4, 80.6 and 81.9% of the dose for the 5, 50 and 500 mg/kg dose levels, respectively. Faecal excretion of radiolabel after multiple dosing at 24 hr accounted for 6.3, 6.9 and 4.5% of the administered radioactivity at the 5, 50 and 500 mg/kg dose levels, respectively. The major metabolic pathway of CNMA for all single and the 5 and 50 mg/kg multiple dose levels in this species of rat was found to be degradation to benzoic acid through beta-oxidation and excretion in the urine mainly as hippuric acid, with much smaller amounts of benzoic and cinnamic acids. At the multiple dose level of 500 mg/kg, benzoic acid was the major urinary metabolite, indicating that in the Fischer 344 male rat at this relatively high oral dose level the detoxification of CNMA proceeds differently and an alternative metabolic pathway is proposed.

Acrolein↗

PubMed1991

Pathologic changes, tissue distribution, and extent of conversion to ethylenethiourea after subacute administration of zinc ethylene-bis-dithiocarbamate (zineb) to calves with immature rumen function.

The toxicity of zinc ethylene-bis-dithiocarbamate (zineb), a widely used fungicide, was studied in four 4-week-old Friesian calves with immature rumen function. Calves were first subjected to liver biopsy, and thereafter, 3 of them were orally administered 200 mg of zineb/kg of body weight daily for 80 days, whereas the fourth calf served as control and remained untreated. Clinical, hematologic, and pathologic (including ultrastructural) findings were recorded. The distribution in body fluids and tissues of the parent compound and one of its main metabolites, ethylenethiourea (ETU), also was examined. Treated calves had unthrifty appearance and reduction in weight gain. They also had remarkable impairment of thyroid function, as reflected by reduction in serum concentrations of triiodothyronine and thyroxine and increase in weight of the thyroid gland associated with epithelial vacuolization and foci of hyperplasia. Moderate increase in liver glycogen content and impairment in maturation of germ cells were recorded consistently. Whereas zineb was widely distributed in body tissues, ETU accumulated mainly in the liver and the thyroid gland, although noticeable concentrations also were attained in muscle. Data were consistent with involvement of ETU mainly in the pathogenesis of thyroid gland lesions, and indicate that unweaned calves given zineb develop a clinicopathologic syndrome that does not differ qualitatively from that already described in adult cattle exposed to zineb.

Age Factors↗

PubMed1979

Tissue Distributions of Dhurrin and of Enzymes Involved in Its Metabolism in Leaves of Sorghum bicolor.

The tissue distributions of dhurrin [p-hydroxy-(S)-mandelonitrile-beta-d-glucoside] and of enzymes involved in its metabolism have been investigated in leaf blades of light-grown Sorghum bicolor seedlings. Enzymic digestion of these leaves using cellulase has enabled preparations of epidermal and mesophyll protoplasts and bundle sheath strands to be isolated with only minor cross-contamination. Dhurrin was located entirely in the epidermal layers of the leaf blade, whereas the two enzymes responsible for its catabolism, namely dhurrin beta-glucosidase and hydroxynitrile lyase, resided almost exclusively in the mesophyll tissue. The final enzyme of dhurrin biosynthesis, uridine diphosphate glucose:p-hydroxymandelonitrile glucosyltransferase, was found in both mesophyll (32% of the total activity of the leaf blade) and epidermal (68%) tissues. The bundle sheath strands did not contain significant amounts of dhurrin or of these enzymes. It was concluded that the separation of dhurrin and its catabolic enzymes in different tissues prevents its large scale hydrolysis under normal physiological conditions. The well documented production of HCN (cyanogenesis), which occurs rapidly on crushing Sorghum leaves, would be expected to proceed when the contents of the ruptured epidermal and mesophyll cells are allowed to mix.

Journal Article↗

PubMed1994

Tissue distribution of IL-10 mRNA in normal mice. Evidence that a component of IL-10 expression is T and B cell-independent and increased by irradiation.

Murine IL-10, initially identified as a product of Th2 CD4+ T cell clones, is known to be produced by a variety of hematopoietic cells. The cellular and tissue expression of IL-10 in vivo is not known and could be relevant to understanding its functions. We examined in vivo, expression of IL-10 mRNA using RT-PCR in various normal and mutant mice and after irradiation. In addition, expression was studied during rejection of an i.p. injection of P815 tumor cells. Total RNA was extracted from whole organs; standard RT-PCR, semiquantitative PCR, and RNase protection assays were performed. In normal mice IL-10 mRNA was detectable in all tissues surveyed. Semiquantitative PCR allowed an estimation of the relative levels of IL-10 mRNA in tissues. IL-10 mRNA in spleen and kidney of nude mice and SCID mice was detectable in normal amounts. Expression of IL-10 mRNA was increased in spleen and kidney in a dose-dependent fashion after irradiation. During allogeneic stimulation IL-10 mRNA was increased in spleen and kidney as demonstrated by the PCR and RNase protection assays. In conclusion, IL-10 mRNA is detectable by PCR in many organs of normal mice and is largely T and B cell-independent. The increase of IL-10 mRNA in spleen and kidney during an intraperitoneal T cell response, at a time when IFN-gamma mRNA is known to be increased in the same organs, suggests a complex systemic interaction between IL-10 and other cytokines during rejection. Moreover, the ubiquitous tissue distribution and the increased levels of steady state IL-10 mRNA after irradiation suggest that this molecule plays a general role in the biology of all tissues and may explain some of the immunosuppressive effects of ionizing radiation.

Animals↗

PubMed1986

Tissue distribution and characterization of peptide C-terminal alpha-amidating activity in rat.

The C-terminal alpha-amide formation of peptides is one of the most important events in prohormone processing. Recently, we developed a simple and sensitive assay for detecting alpha-amidating activity in tissues by using (125I)-Ac-Tyr-Phe-Gly as a substrate. Using this assay method, we have determined the tissue distribution of alpha-amidating enzyme activity in adult male rat. High concentrations of alpha-amidating activity were found in pituitary, brain, thyroid, gastrointestinal tract, pancreas, heart, submaxillary glands and parotid glands. Alpha-amidating enzyme activities in all tissues examined exhibit very similar copper and ascorbate requirements, pH dependence, and behavior on gel-filtration.

Amides↗

PubMed1995

Genomic structure and tissue distribution of the mouse dopamine D4 receptor.

The mouse dopamine D4 receptor gene was isolated from a genomic DNA library by plaque hybridization. The D4 receptor gene encoded an open reading frame consisting of 387 amino acids, interrupted by three introns. Distribution of the D4 receptor mRNA in brain regions and peripheral tissues of mice was examined by reverse transcription-polymerase chain reaction (RT-PCR). There was a remarkable expression of the receptor mRNA in various brain regions, showing the highest expression level in the cerebellum. Also, in the peripheral tissues a high level expression of the D4 mRNA was detected in the eye, adrenal gland and testes. We observed several differences in tissue distribution of the D4 mRNA in mice from that reported in other mammalian species.

Amino Acid Sequence↗

PubMed1994

Tissue distribution of ecto-Mg-ATPase in adult and embryonic chicken.

We have determined the distribution of chicken ecto-Mg-ATPase in a variety of tissues from adult and embryonic chicken. The presence of ecto-Mg-ATPase was identified by an antibody raised against a 12 amino acid residue peptide, NH2-KILSGEEEGVFG, derived from proteolysis and sequencing of the chicken gizzard ecto-Mg-ATPase. Adult chicken tissues were also assayed for ATPase activity in the presence/absence of stimulators/inhibitors of the ecto-ATPase in order to confirm the immunologic tissue distribution results. There is controversy in the literature as to the size(s) of ecto-Mg-ATPases. We demonstrate here that the apparent size of the enzyme(s) recognized by anti-peptide antibodies by Western blot analysis depends on the denaturation conditions used prior to electrophoresis. Lastly, we deduce that the chicken ecto-ATPase is not identical to T-cadherin, as has been recently proposed.

Adenosine Triphosphatases↗

PubMed1993

Tissue distribution of a dynorphin-processing endopeptidase.

A number of peptide hormones and neurotransmitters require post-translational processing at monobasic cleavage sites. An enzymatic activity capable of processing prodynorphin at a monobasic processing site has been previously reported in rat brain and bovine pituitary. This dynorphin (Dyn)-converting enzyme (DCE) activity is capable of converting Dyn-B-29 (leumorphin) to Dyn-B-13 (rimorphin). The tissue distribution of the DCE activity in the adult rat shows that the activity is present at high levels in the brain, ileum, neurointermediate pituitary, and adrenal. Lower levels of activity are found in the anterior pituitary, liver, heart, ovary, kidney, lung, and serum. In the rat pituitary, the anterior lobe has 10-fold lower specific activity than the neurointermediate lobe. The protease inhibitor profile shows that the activity in various tissues is considerably inhibited by the thiol protease inhibitor p-chloromercuriphenyl sulfonic acid (PCMPS), suggesting that the Dyn-converting activity is due to a putative thiol protease. The Dyn-converting activity in the rat ileum and brain was subjected to ion exchange chromatography on diethylaminoethyl-cellulose; the majority of activity eluted around 0.3 M NaCl, as did bovine pituitary DCE. This chromatography behavior, peptide inhibitor profile, and pH optima are consistent with those of the previously reported enzyme activity from bovine pituitary and pituitary-derived cell lines. In the bovine brain, the distribution of activity generally matches that of Dyn-B-13. In the bovine adrenal medulla, the activity is localized to secretory vesicles that also contain carboxypeptidase-E activity, an enzyme thought to be involved with peptide processing. Taken together, the tissue distribution and enzyme properties support the possibility that the DCE is involved in the maturation of Dyn as well as many peptide hormones and neuropeptides.

Adrenal Glands↗

PubMed1988

Tissue distribution of ethosuximide and clobazam in a seizure related fatality.

The case of a six-year-old male who died in a hospital while receiving several anticonvulsant drugs is described. Phenytoin, desmethyldiazepam, clobazam (an experimental 1,5 benzodiazepine), and desmethylclobazam were quantitated in serum, liver, and brain tissue by high performance liquid chromatography. Ethosuximide was quantitated by gas chromatography. To our knowledge, this is one of few reports describing tissue concentrations of ethosuximide collected at autopsy and the first report of clobazam/desmethylclobazam tissue distribution in man.

Anti-Anxiety Agents↗

PubMed1995

Tissue distribution and influence of selenium status on levels of selenoprotein W.

Rabbits were immunized with two synthetic peptides based on hydrophilic regions of selenoprotein W from rat muscle. The resulting polyclonal antibodies were used in Western blots to determine the compartmentation and tissue distribution of selenoprotein W, and to determine the influence of selenium on the levels of this selenoprotein in rat muscle. Selenoprotein W exists mainly in cytosol, but very small amounts were associated with membranes. Western blots revealed selenoprotein W in muscle, spleen, testis, and brain of rats. Rats were fed diets of either no addition of selenium (0 ppm Se) or additions of 0.1 and 4.0 mg selenium/g (0.1 ppm Se and 4.0 ppm Se) diet for 6 wk. Selenoprotein W was undetectable in skeletal muscle of rats fed the basal diet, detectable in those fed 0.1 ppm selenium in the diet, and much higher in muscle from rats fed 4 ppm selenium diet. In a species comparison, Western blots indicated the presence of selenoprotein W in muscle of rabbits, sheep, and cattle.

Amino Acid Sequence↗