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Query: UNIPROT:P56851 (epididymal)
11,273 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

1. Procedures were developed for the extraction and assay of glycolytic enzymes from the epididymis and epididymal spermatozoa of the rat. 2. The epididymis was separated into four segments for analysis. When rendered free of spermatozoa by efferent duct ligation, regional differences in enzyme activity were apparent. Phosphofructokinase, glycerol phosphate dehydrogenase and glucose 6-phosphate dehydrogenase were more active in the proximal regions of the epididymis, whereas hexokinase, lactate dehydrogenase and phosphorylase were more active in the distal segment. These enzymes were less active in the epididymis of castrated animals and less difference was apparent between the proximal and distal segments. However, the corpus epididymidis from castrated rats had lower activities of almost all enzymes compared with other epididymal segments. 3. Spermatozoa required sonication to obtain satisfactory enzyme release. Glycolytic enzymes were more active in spermatozoa than in epididymal tissue, being more than 10 times as active in the case of hexokinase, phosphoglycerate kinase and phosphoglycerate mutase. 4. The specific activities of a number of enzymes in the epididymis were dependent on the androgen status of the animal. These included hexokinase, phosphofructokinase, aldolase, glyceraldehyde phosphate dehydrogenase, phosphoglycerate kinase, pyruvate kinase, glycerol phosphate dehydrogenase, glucose 6-phosphate dehydrogenase, 6-phosphogluconate dehydrogenase and phosphorylase. 5. The caput and cauda epididymidis differed in the extent to which enzyme activities changed in response to an altered androgen status. The most notable examples were hexokinase, phosphofructokinase, aldolase, phosphoglycerate kinase, 6-phosphogluconate dehydrogenase and phosphorylase.
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PMID:Activity and androgenic control of glycolytic enzymes in the epididymis and epididymal spermatozoa of the rat. 18 56

Stromal vascular cells were isolated from adipose tissue obtained from three different anatomical locations: epididymal (EPI), retroperitoneal (RP), and dorsal subcutaneous (SC), and allowed to differentiate in primary tissue culture. Cell number, protein concentration, glycerophosphate dehydrogenase, and lipoprotein lipase activity were similar in cells obtained from the EPI, RP, and SC regions, as were total insulin binding and the affinity of insulin for its receptor. However, both maximal insulin receptor tyrosine kinase activity and insulin-stimulated phosphorylation of the insulin receptor were significantly lower (P less than 0.05) in cells cultured from the SC region. In addition, newly differentiated adipocytes from the SC region were less sensitive to the ability of insulin to stimulate glucose uptake, and maximal insulin-stimulated glucose uptake by these cells was also significantly lower (P less than 0.05) when compared to cells obtained from the two other regions. Since these studies were performed on adipocyte precursor cells, allowed to differentiate to a similar degree in primary culture, the observed differences in insulin receptor phosphorylating activity, as well as the ability of insulin to stimulate glucose uptake appear to be intrinsic to adipose tissue from the three sites.
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PMID:Differences in insulin action as a function of original anatomical site of newly differentiated adipocytes obtained in primary culture. 165 46

The stroma-vascular fraction (SVF) of inguinal and epididymal fat pads of 4 week-old rats was studied by electron microscopy. Among the various cell types, endothelial cells and preadipocytes were found in both SVF, while mesothelial cells were only detected in the epididymal SVF. The resulting heterogeneity of primary culture and the adipoconversion of the fat cell precursors were studied in a serum-supplemented medium enriched with insulin (14.5 nM) and exogenous triglycerides. Despite the heterogeneity of the inoculum, the primary cultures were rather homogeneous, fat cell precursors being the main cell type. Distinctive contaminant fibroblast-like cells were observed in both cultures, whereas epithelial-like cells, which correspond most probably to mesothelial cells, were only found in epididymal cultures. Differentiation of fat cell precursors was assessed by the appearance of lipoprotein lipase (LPL) and glycerol-3-phosphate dehydrogenase (GPDH). LPL activity was found in the same level in cells of both deposits while GPDH activity was elevated in inguinal vs epididymal derived stroma-vascular cells. The different adipose conversion pattern of both cultures was confirmed by morphological quantification: the maturation of epididymal fat cell precursors was faster but less extensive. These differences could be related mainly to regional localization rather than to different maturation of the two fat deposits.
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PMID:The stroma-vascular fraction of rat inguinal and epididymal adipose tissue and the adipoconversion of fat cell precursors in primary culture. 209 4

Transient exposure of cultured 3T3-L1 preadipocytes to hypolipidemic fibrate drugs results in extensive adipocyte conversion. Adipocyte conversion in culture was characterized by an increase in neutral lipids content and in adipocyte marker enzymes like hormone-sensitive lipase and glycerol-3-phosphate dehydrogenase. Adipocyte conversion in culture was also accompanied by induction of cyanide-insensitive peroxisomal palmitoyl-CoA oxidation. The conversion pattern exerted by fibrate drugs in 3T3-L1 cells was similar to that reported previously for primary cultured epididymal preadipocytes (R. Brandes, R. Arad and J. Bar-Tana, Biochim. Biophys. Acta, 877, 314-321 (1986)), and seems to refute clonal selection in the conversion sequel initiated by fibrate drugs in primary cultured preadipocytes.
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PMID:Adipocyte conversion of cultured 3T3-L1 preadipocytes by bezafibrate. 243 18

A reproducible cell culture system is described that allows the study of adipose conversion in fibroblast-like cells isolated by collagenase digestion of epididymal and perirenal adipose tissue from male rats weighing 70-200 g. Adipose conversion as measured by lipid accumulation and increase in glycerophosphate dehydrogenase (GPDH) activity during differentiation strongly depends on the density at which cells are inoculated and starts only when cells are confluent and when physiological amounts of corticosterone and insulin are added. beta-Estradiol, testosterone, thyroxine, triiodothyronine, and growth hormone do not affect the differentiation process. Methylisobutylxanthine added during the first 2 days after confluence, added with insulin and corticosterone, potentiates the effect of insulin on GPDH activity and accelerates triglyceride accumulation. The effect of methyl-isobutylxanthine seems to be mediated by increased cyclic AMP concentrations, inasmuch as it may be replaced by forskolin.
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PMID:Hormonal regulation of the differentiation of rat adipocyte precursor cells in primary culture. 244 Sep 70

In primary cultures of rat preadipocytes (PA) isolated from epididymal or perirenal depots, rat serum is more effective than other animal sera (fetal calf, newborn calf, human, horse, rabbit, cat, sheep, goat, dog, pig) in promoting adipogenic conversion, biochemical differentiation, and mitogenesis. Only mouse serum is comparable to rat serum. This activity is attributable to a specific growth factor (preadipocyte stimulating factor, PSF). An assay for PSF in rat serum was devised using PA from perirenal fat of 3-month-old Fischer 344 rats grown first to confluence in FCS for 8 days and then for the next 3 days in test serum, followed by measurement of triglyceride (TG) and glycerol-3-phosphate dehydrogenase (GPDH). Rat serum induces dose-dependent rapid cell division, which coincides with accumulation of TG and increase of GPDH; for routine quantitation, TG is assayed. The biochemical characteristics of PSF in serum are as follows: stable at 4 degrees C for up to 1 year; inactivated at 100 degrees C (80% loss, 30 min) but stable at 56 degrees C for 1 hr; stable at pH 2-12; non-dialyzable; completely resistant to pepsin, trypsin, and chymotrypsin but destroyed by pronase and subtilisn; stable to DTT and periodate; and m.w. between 68 kDa (Sephacryl-300) and 58 kDa (Sephacryl-300 in 5 M urea). PSF activity is greater in serum from Wistar than from Fischer 344 rats, while activity of serum from Zucker obese (fa/fa) rats is at least as great as that from Wistar rats and, like serum of rats made obese by feeding a high-fat, high-carbohydrate diet, is not suppressed. PSF activity is not due to insulin, insulin-like growth factor-1 (IGF-1), growth hormone, glucocorticoids, or combinations of these hormones. PSF activity was not seen with a number of growth factors including colony-stimulating factor (CSF-1), GM-CSF, interleukins 1, 2, and 3, neuroleukin, tumor necrosis factor, and others. PSF is distinct from the low molecular weight (4-8 kDa) differentiation factor present in rat serum, FCS, and human serum that promotes the adipogenic conversion and cellular differentiation of 3T3-L1, 3T3-F442A, and Ob17 cells. PSF appears to be a new differentiation factor for rat preadipocytes, has properties suggestive of a highly glycosylated protein, and may be highly species specific.
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PMID:Preadipocyte stimulating factor in rat serum: evidence for a discrete 63 kDa protein that promotes cell differentiation of rat preadipocytes in primary cultures. 268 98

The present study was conducted to provide biochemical and morphological evidence for ethanol-induced impairment of testicular development. The specific activities of testicular postmeiotic enzyme markers--sorbitol dehydrogenase (SDH), lactate dehydrogenase (LDH), and alpha-glycerophosphate dehydrogenase (GDH)--increased with age in CFW mice from ages 23 to 60 days, providing a biochemical measure of testicular development during puberty. Chronic ethanol treatment via liquid diets from ages 20 to 55 days resulted in decreased activities of SDH and LDH at ages 40 and 44 days, and of GDH at ages 34, 40, and 44 days. These decreases were consistent with an arrest in the developmental increase in SDH, LDH, and GDH at ages 31 +/- 0.6, 31 +/- 2.6, and 24 +/- 0.5 days, respectively. After 29 days of ethanol treatment (age 50 days), testicular weights, epididymal sperm content, and sperm motility were reduced, relative to controls, by 37, 83, and 60%, respectively (p less than 0.05). Epididymal weights were unaffected. Light microscopic evaluation of testes revealed disorganization of spermatogenesis, germ cell degeneration, decreased tubular luminal diameter, and vacuolation of Sertoli cells in ethanol-treated mice at age 50 days. Electron microscopic analysis showed that germ cell degeneration was not restricted to a specific cell type. Stage IX-XI tubules were observed in which spermatids had been retained and underwent phagocytosis within the Sertoli cell. Sertoli cells showed evidence of atypical nuclear invaginations. Sertoli cells underwent degenerative changes and were sloughed into the rete testis. However, relative Leydig cell size, as well as fractional volume occupied by the nucleus, mitochondria, and endoplasmic reticulum were unaffected by ethanol. The data (1) confirm previous findings suggesting ethanol-induced delayed testicular development; (2) suggest that certain aspects of testicular development are arrested relatively early in ethanol treatment (4-11 days); and (3) indicate that the Sertoli cell, rather than the Leydig cell, is the primary target with regard to the deleterious effect of chronic ethanol treatment on testicular maturation.
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PMID:Biochemical and structural evidence for ethanol-induced impairment of testicular development: apparent lack of Leydig cell involvement. 276 3

Cultured rat epididymal preadipocytes exposed for 24-72 h to either bezafibrate or clofibrate added to the culture medium were extensively converted to fat-loaded adipocytes. Adipocyte conversion increased during the first 5-7 days following plating, reaching a level of 100% and 60% conversion with bezafibrate and clofibrate, respectively, as compared to 10% conversion in their absence. Adipocyte conversion in culture was a saturable function of the hypolipidemic effectors and was associated with an increase in the incorporation rate of exogenous palmitate into triacylglycerols, in glycerol-3-phosphate dehydrogenase and hormone-sensitive lipase activities but not in lipoprotein lipase activity. Adipocyte conversion by hypolipidemic drugs was much more prominent than that exerted by dibutyryl cAMP, and the relative conversion efficiency of the two fibrate drugs did not correlate with their respective cAMP content of the culture. Hence, hypolipidemic drugs and dibutyryl cAMP appear to act independently in initiating adipose conversion in primary epididymal preadipocytes.
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PMID:Adipose conversion of cultured rat primary preadipocytes by hypolipidemic drugs. 301 19

Stromal-vascular cells from the epididymal fat pad of 4-week-old rats, when cultured in a medium containing insulin or insulin-like growth factor, IGF-I, triiodothyronine and transferrin, were able to undergo adipose conversion. Over ninety percent of the cells accumulated lipid droplets and this proportion was reduced in serum-supplemented medium. The adipose conversion was assessed by the development of lipoprotein lipase (LPL) and glycerol-3-phosphate dehydrogenase (GPDH) activities, [14C]glucose incorporation into polar and neutral lipids, triacylglycerol accumulation and lipolysis in response to isoproterenol. Similar results were obtained with stromal-vascular cells from rat subcutaneous and retroperitoneal adipose tissues. Stromal-vascular cells required no adipogenic factors in addition to the components of the serum-free medium. Insulin was required within a physiological range of concentrations for the emergence of LPL and at higher concentrations for that of GPDH. When present at concentrations ranging from 2 to 50 nM, IGF-I was able to replace insulin for the expression of both LPL and GPDH. The development of a serum-free, chemically defined medium for the differentiation of diploid adipose precursor cells opens up the possibility of characterizing inhibitors or activators of the adipose conversion process.
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PMID:Development of a chemically defined serum-free medium for differentiation of rat adipose precursor cells. 353 40

The ob17 preadipocyte clonal line has been established from the adipocyte fraction of the epididymal fat pads of adult C57 BL/6J ob/ob mice. In vivo, injection of ouabain-resistant mutant cells (ob 17OR11 cell line) into athymic mice is followed by the formation of fat pads containing ouabain-resistant mature fat cells. In vitro, ob17 cells develop after confluence biochemical and morphological characteristics of adipocytes. The adipose conversion process is best represented by a stochastic model in which a pool of stem cells (adipoblasts) give rise to clusters of adipose cells and to additional stem cells that remain in the population. The role of the different factors involved in such conversion is discussed; (1) factors that enhance the number of susceptible cells (ACF or ACF-like compounds), (2) factors without which no adipose conversion takes place (triiodothyronine, growth hormone and other factors still to be characterized), (3) factors that enhance the expression of the differentiation program (insulin). The early emergence of lipoprotein lipase occurs normally in insulin-depleted medium. The separation of ob17 cells by isopycnic centrifugation shows that lipoprotein lipase is present at high levels in early differentiating cells which are still devoid of late markers, ie glycerol-3-phosphate dehydrogenase and triglycerides. These results are discussed with respect to the determination of cellularity during development of adipose tissue in vivo.
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PMID:Adipose conversion of ob17 cells and hormone-related events. 390 48


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