Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P56851 (epididymal)
 11,273 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Effects of protein malnutrition on adipose tissue development were studied in weanling male Sprague-Dawley rats fed isocaloric diets ad libitum containing either 22% (controls) or 8% (protein-malnourished rats) casein, and in rats pair-fed to the protein-malnourished rats with the 22% casein diet. After 32 days on the diet, protein-malnourished rats were 37% and pair-fed 67% the weight of the controls, while torso length was 37% and 73% of controls, respectively. Food consumption relative to body weight was greatest in protein-malnourished rats. Compared to control rats, the distal epididymal adipocyte number in the protein-malnourished rats was decreased in proportion to the decrease in body size and was more closely related to the protein intake than to the total calories consumed. After 32 days on diet, mean adipocyte number per 2 distal pads was 11.7 x 10(6) in controls and 4.3 x 10(6) in protein-malnourished rats. In pair-fed rats, cell number lagged behind controls at 4 and 11 days, but was normal at 32 days (11.4 x 10(6) cells). The distal epididymal pad adipocyte size and percent lipid were similar in all groups during the first 25 days of dietary treatment. Adipocyte size was increased significantly in controls at day 32 compared to the other two groups. At each time studied through day 25 on diet, epididymal pad weight was related to the adipose cell number rather than the cell size. It is concluded that severe restriction of dietary protein during the postweaning period of growth in rats results in decreased epididymal adipocyte proliferation and/or differentiation concomitant with generalized growth retardation, whereas isocaloric feeding of a diet of normal protein content is associated with only a transient delay in adipose tissue development.
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PMID:Adipose tissue development, growth, and food consumption in protein-malnourished rats. 10 48

The effects of voluntary exercise on growth and food intake, body composition, organ weight, and fatty acid composition of adipose tissue of mice fed on a 20% casein diet or a 10% casein diet were examined. The weight gain was greater for the 20% casein nonexercise group (20% NE) than that for the 20% casein exercise group (20% E), 10% casein exercise group (10% E) and 10% casein nonexercise group (10% NE). There were no significant differences between the groups except the 20% NE. In 20% E and 10% E, body fats decreased markedly. On the other hand, a very high ratio of protein was present in the body composition of both groups. In the 20% and 10% casein diet groups, food intake was increased by voluntary exercise, but there was no significant difference between 10%E and 10% NE except occasional periods during these experiments. After 6 weeks of age, 10% E had a tendency to undertake more voluntary exercise than 20% E, though the difference was not statistically significant. Development of the heart and gastrocnemius muscles was accelerated by voluntary exercise and epididymal fat tissue was markedly decreased.
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PMID:Effect of voluntary exercise on physiological function and feeding behavior of mice on a 20% casein diet or a 10% casein diet. 44 75

1. When fat-cells are isolated from the epididymal adipose tissue of 24h-starved rats and incubated at 25 degrees C in the presence of dialysed serum, glucose, insulin, amino acids and heparin, the total clearing-factor lipase acitivity of the incubation system increases progressively over a period of several hours. 2. All of the increase in activity is accounted for by the appearance of enzyme in the appearance of enzyme in the incubation medium and the fat-cell activity does not change significantly. Cycloheximids, at a concentration that prevents protein synthesis, does not affect the appearance of enzyme in the incubation medium, but the fat-cell enzyme activity is decreased in its presence. 3. The magnitude of the increase in total clearing factor lipase activity is unaffected by the omission of heparin from the medium. However, less enzyme is extracted in tis absence and the fat-cell activity increases. Cycloheximide again only affects the rise in cell activity and does not alter the activity in the incubation medium. 4. When serum in the incubation medium is replaced by casein, the distribution of enzyme between the cells and the medium is changed, but the magnitudes of the increases in total enzyme activity are similar. 5. These characteristics of the clearing-factor lipase response of isolated fat-cells differ in several respects from those observed earlier with intact adipose tissue from 24h-starved rats (Robinson & Wing, 1971; Cryer et al., 1973). The differences could be due, in part, to changes in the relative amounts of two different molecular forms of the enzyme that occur during the isolation of the fat-cells.
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PMID:The clearing-factor lipase activity of isolated fat-cells. 80 20

Differences in weight of the body, six different skeletal muscles, epididymal fat pads, three different bones, spleen, heart, kidneys, testes and liver were observed in 21-day-old male Sprague-Dawley rats from two different suppliers. All rats were pair-fed a 10% casein diet ad libitum, 10%, 20%, 30% restricted for 4 or 8 weeks. Original body and tissue weight differences between the two strains of rats were maintained in all diets during the 4 and 8 week feeding periods. Trends in body and tissue weight changes due to dietary restriction were similar in both strains of rats. Diet restrictions for 4 or 8 weeks caused similar patterns of weight decrease in most tissues. Feed efficiency ratio (FER) was reduced significantly at the 20% and 30% restriction for 4 weeks only in the lighter strain of rats. FER was higher in the heavier strain than in the lighter strain of rats at all levels of diet restriction. Food conversion efficiency with reduced food intake was constant or decreased depending on the skeletal muscle studied; decreased significantly for epididymal fat pad, bone weight (one strain only), kidneys and liver (one strain only) with the 30% reduced diet for 4 weeks; and increased for bone length and testes weight. Therefore, significant deviations from ad libitum controls were found only at 30% diet restriction, and the wide differences in body and tissue weight of two strains of Sprague-Dawley rats did not affect the interpretation of results when fed the same restricted diets.
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PMID:Effect of dietary restrictions and source of rats on growth rate and efficiency of conversion of food into muscles, bones and organs. 91 58

1. Rates of in vivo fatty acid (FA) synthesis were assessed with 3H2O in carcass, liver, intestine, muscle and four adipose depots from rats fed a high-protein, carbohydrate-free diet (70% casein, 8% fat, w/w) or a balanced diet (66% carbohydrate, 17% casein, 8% fat) for 25-30 days. 2. Rats adapted to the high protein (HP) diet showed a marked reduction of total FA synthesis from all carbon sources, which was due to a decreased synthesis of triacylglycerols. Rates of phospholipid-fatty acid synthesis in both carcass and liver were not affected by the diet. Rates of triacylglycerol-fatty acid (TAG-FA) synthesis were markedly reduced in adipose tissue from four different sites: epididymal (79%), retroperitoneal (78%), subcutaneous (65%) and intermuscular (82%). 3. In rats fed the balanced control diet, TAG-FA synthesis in adipose tissue accounted for about 75% of synthesis in whole carcass, whereas it was reduced to 36% in rats under the HP regimen. 4. Although hepatic lipogenesis was also reduced in HP-fed rats, the contribution of the liver to total TAG-FA synthesis was approximately the same in HP (24%) and control (20%) rats, whereas the contribution of adipose tissue was only 26% in HP-fed animals compared to 57% in controls. 5. Force-feeding fed rats with components of their own diets resulted in a significant (100%) increase of liver TAG-FA synthesis in animals fed the control diet, but did not significantly affect liver lipogenesis in HP rats.
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PMID:Reduced lipogenesis in rats fed a high-protein, carbohydrate-free diet: participation of liver and four adipose depots. 134 18

Casein kinase II from bovine epididymal spermatozoa was purified to apparent homogeneity by repeated chromatography with phosphocellulose and gel filtration with sephacryl S-200. The purified enzyme exhibited a molecular mass of 130 kDa by gel filtration and displayed three polypeptide bands with molecular masses of 26, 33, and 36 kDa by SDS-polyacrylamide gel electrophoresis. Antibodies raised against calf thymus casein kinase II cross reacted with the three sperm polypeptides. Incubation of the holoenzyme with either [gamma-32P]ATP or [gamma-32P]GTP resulted in the phosphorylation of the 26-kDa subunit. The enzymatic activity with casein as substrate was strongly inhibited by nanomolar heparin and greatly stimulated by micromolar spermine. With casein as substrate, the specific activity of the pure enzyme (0.5 mumol/min/mg protein) was comparable to that of casein kinase II from other sources. Endogenous substrates of the kinase were demonstrated by incubating sperm cytosolic extracts with [gamma-32P]GTP, under conditions that limit the expression of other protein kinases, and analyzing the products by SDS-PAGE and autoradiography. Similar results were obtained when sperm extracts, suitably diluted to minimize endogenous casein kinase II, were incubated with [gamma-32P]GTP and aliquots of pure sperm casein kinase II. Low concentrations (50 microM) spermine strongly enhanced the phosphorylation of 92- and 106-kDa cytosolic proteins. Our results clearly show that casein kinase II is present in spermatozoa and that it shares many of the properties of the enzyme from other sources. Further, they indicate that the enzyme plays a role in mediating the phosphorylation state of sperm proteins.
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PMID:Purification and characterization of polyamine-stimulated protein kinase (casein kinase II) from bovine spermatozoa. 189 32

Casein kinase 2 activity as measured by phosphorylation of the peptide substrate Arg-Arg-Arg-Glu-Glu-Glu-Thr-Glu-Glu-Glu is increased by about 50% in extracts from insulin-treated epididymal fat-pads or isolated fat-cells after purification by Mono Q chromatography. Insulin acts to increase the Vmax. of the kinase. An acid-soluble protein with an apparent subunit molecular mass of about 22 kDa appears to be a substrate for casein kinase 2. The protein possesses a number of properties in common with the acid-soluble heat-stable 22 kDa protein which exhibits increased phosphorylation in rat adipose tissue exposed to insulin.
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PMID:Evidence that insulin activates casein kinase 2 in rat epididymal fat-cells and that this may result in the increased phosphorylation of an acid-soluble 22 kDa protein. 195 48

Blood sera of humans, rats, goats, and buffalo have been shown to possess a forward motility-stimulating factor (FMSF) that markedly stimulated goat cauda epididymal sperm forward motility, as assayed by a microscopic method in the presence of epididymal plasma (1.2 mg protein/ml) that had sufficient anti-sticking activity to eliminate the possibility of cell-sticking artifacts in motility assays. The specific activity of FMSF was greatest in buffalo blood serum compared to the sera of the other species. Buffalo serum at a concentration as low as 8.5 mg protein/ml induced forward motility in nearly 45% of the cells. The buffalo serum FMSF was heat-stable, nondialyzable, and sensitive to the action of trypsin. Purified proteins--casein, serum albumin, ovalbumin, myoglobin, and beta-lactoglobulin--showed little or relatively low FMSF activity. FMSF is a glycoprotein, as it binds with high affinity to concanavalin A-agarose. A major portion of the serum protein (approx. 70%) did not bind to the affinity matrix, and this unretained serum protein fraction showed little FMSF activity. The FMSF activity of buffalo serum was confirmed by estimating sperm forward motility spectrophotometrically: an objective method of assessing sperm motility.
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PMID:Stimulation of forward motility of goat cauda epididymal spermatozoa by a serum glycoprotein factor. 262 73

Phosphatidyl inositol has been found to inhibit strongly the activity of a cyclic AMP-independent protein kinase located on the external surface of goat epididymal intact spermatozoa. Phosphatidyl inositol at a concentration as low as 10 micrograms/ml inhibited nearly 50% of the ecto-kinase activity for the phosphorylation of the exogenous protein substrate: casein. Phosphatidyl ethanolamine at a relatively high concentration (125 micrograms/ml) inhibited slightly (approx 25%) the activity of the enzyme whereas other phospholipids: phosphatidyl serine and choline, diacyl glycerol, phosphatidic acid and myo-inositol-2-phosphate had no appreciable effect on the kinase activity. Phosphatidyl inositol has also served as a potent inhibitor of the phosphorylation of sperm ecto-phosphoproteins by the endogenous kinase activity of intact spermatozoa. By thin layer chromatography it has been shown that the observed inhibitory effect of the phospholipid was not due to any impurities or degraded products of phosphatidyl inositol. Phosphatidyl inositol inhibited the kinase activity noncompetitively with respect to casein and Mg2+ but uncompetitively with respect to ATP. The results raised the possibility that phosphatidyl inositol-mediated high affinity inhibition of protein kinase(s), may constitute a novel mechanism for the regulatory actins of the phospholipid in mammalian cells.
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PMID:Phosphatidyl inositol inhibition of a sperm cyclic AMP-independent protein kinase. 303 78

1. To study the efficiency of rehabilitation after different periods of protein-energy malnutrition, we used as a model preweaning malnourished rats. After weaning, male Wistar rats were fed on a protein-deficient diet (50 g casein/kg) ad lib. for the whole study (DR group) or rehabilitated with normal diet (180 g casein/kg; RR group) from weaning, week 0, or weeks 1, 3, 5, 8 and 16 thereafter. 2. Twelve animals from the DR group were killed at the beginning of each rehabilitation period. The twelve rehabilitated rats were killed after 2 weeks. Body-weight and epididymal adipose tissue weight, blood glucose, plasma immunoreactive insulin (IRI) and immunoreactive glucagon (IRG), and pancreatic contents of IRI and IRG were determined. 3. Food intake of RR rats rose significantly except during the last period where body-weight increased less than that during the previous period. Fat-pad weights increased in the same manner in DR and RR groups. 4. Blood glucose fell and plasma IRG rose significantly without any change in plasma IRI after each rehabilitation period, except during the last period where blood glucose concentrations became stable. Pancreatic IRG and IRI showed the same type of response to those of the plasma. 5. All short-term rehabilitation periods were similarly efficient at producing catch-up growth. High insulin sensitivity of target cells was responsible for good recovery except after long-term malnutrition.
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PMID:Effect of the duration of malnutrition and of nutritional rehabilitation on blood glucose homeostasis and pancreatic hormones in rats. 313 98


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