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)

Male mouse urogenital ridges (URs) at 15.5 days of gestation (vaginal plug = day 0) containing Wolffian (WDs) and Mullerian ducts were cultured for 4 days with or without gonads in serum-free medium (1:1 mixture of Dulbecco's modified Eagle's medium and Ham's F-12 supplemented with insulin, transferrin, cholera toxin, epidermal growth factor, and BSA). URs without gonads were grown in serum-free medium with testosterone (T, 10(-7) M), 5 alpha-dihydrotestosterone (DHT, 10(-8) M), T (10(-7) M) plus cyproterone acetate (antiandrogen, 10(-5) M), or T (10(-8) M) plus 390 MSD (17 beta-N, N-diisopropylcarbamoyl-4-aza-5 alpha- androstan-3-one, an inhibitor of 5 alpha-reductase, 10(-5) M). After 4 days of culture the number of epididymal curvatures that appeared in the upper portion of WDs were quantified. DNA content of URs grown in serum-free medium was also measured. Both T and DHT increased DNA contents in a dose- (T = 10(-8) to 10(-10) M, DHT = 10(-9) to 10(-11) M) and time-dependent manner. DHT was approximately 10-fold more effective than T in eliciting epididymal coiling and increasing DNA content of URs. The effects of T or DHT were mimicked by coculture with fetal testes. Epididymal coiling and an increase in DNA content occurred in URs grown in the presence of T plus 390 MSD. By contrast, URs cultured without androgens or with T plus cyproterone acetate failed to undergo epididymal coiling and to increase DNA content. The conversion rate per mg protein of [1 beta, 2 beta-3H]T into [3H]DHT was 0.30-fold lower in 15.5 day URs cultured over a 4-day period in comparison to urogenital sinuses whose development is known to be dependent upon DHT. These data suggest that T is an important hormone in the development of the upper portion of WDs, although it is not possible to exclude a role for DHT in the development of the epididymis.
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PMID:In vitro androgen-induced growth and morphogenesis of the Wolffian duct within urogenital ridge. 182 79

The objective of this study was to determine the relationship between seminal transferrin and sperm output in ejaculates from mature dairy bulls. Caudal sperm reserves in mature Holstein bulls (n = 15) were depleted by 8 successive ejaculations during a 50-70-min period (depletion phase). Bulls were then ejaculated 6 times per week for a period of 4 weeks (6X phase). Weekly sperm output (WSO) and weekly transferrin output (WTfO) were the sums of sperm and transferrin levels in 6 ejaculates taken in 1 week of the study. Mean WSO ranged from 20.7 billion to 39.6 billion and mean WTfO ranged from 334 micrograms to 1872 micrograms among the bulls. Regression analysis of sperm and transferrin levels in ejaculates collected during the depletion phase indicated that approximately 40% of seminal transferrin was not related to sperm output and probably was from accessory fluids. A relationship between total seminal transferrin and total sperm in ejaculate was observed (p less than 0.01, r = 0.54). This relationship was stronger when the transferrin was corrected for accessory fluid contribution (p less than 0.01, r = 0.65). The relationship between WSO and WTfO corrected for accessory fluid transferrin contribution (cWTfO) was significant (p less than 0.01, r = 0.64). The relationship between WSO and cWTfO can be interpreted to reflect the relationship between actual testicular sperm production and transferrin from testicular or epididymal origin.
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PMID:Seminal transferrin and spermatogenic capability in the bull. 239 88

Seminiferous peritubular cells have previously been shown to secrete a protein termed P-Mod-S which modulates the functions of Sertoli cells. The present study provides an initial characterization of P-Mod-S and examines the actions of P-Mod-S on Sertoli cells. Gel filtration chromatography demonstrates that P-Mod-S has an apparent molecular weight of 70 000 that could not be dissociated to a lower molecular weight form. A 40- to 90-fold purification of P-Mod-S was obtained with a predicted half maximal effective concentration for Sertoli cells of less than 10(-9) M. Through an analysis of the actions of P-Mod-S on Sertoli cells it is demonstrated that P-Mod-S stimulates the Sertoli cell to a greater extent than any single hormone or vitamin known to influence the cell. P-Mod-S maximally stimulates testicular transferrin and androgen-binding protein production by Sertoli cells, but does not stimulate levels of plasminogen activator activity. P-Mod-S also appears to induce the synthesis of several proteins that are not detected in control non-treated Sertoli cell cultures. One such protein whose synthesis was stimulated by P-Mod-S treatment of Sertoli cells was a component having a molecular mass of 20 kDa. This 20 kDa Sertoli cell-secreted protein was specifically immunoprecipitated with an antibody against an epididymal lactalbumin-like protein. This implies that P-Mod-S can induce Sertoli cells to synthesize and secrete a lactalbumin-like protein. P-Mod-S was found not to contain mitogenic activity. Data presented indicate that testicular peritubular cells synthesize and secrete a 70 kDa non mitogenic paracrine factor termed P-Mod-S which has a dramatic influence on Sertoli cell functions. Results are discussed with respect to modulation of epithelial (Sertoli) cell functions by components produced by mesenchymal (peritubular) cells.
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PMID:Identification of a non-mitogenic paracrine factor involved in mesenchymal-epithelial cell interactions between testicular peritubular cells and Sertoli cells. 308 88

Continuous low-dose gamma-irradiation of mature rats induced a progressive degeneration of the germ cells. Blood FSH increased by 127, 176 and 214%, respectively, after 55, 70 and 85 days of treatment when compared to FSH levels in control rats (8.50 +/- 0.60 ng/ml); conversely, serum LH and testosterone levels were unchanged. The Sertoli cell function was affected by the treatment from 70 days on, as attested by androgen binding protein (ABP) and transferrin secretions which diminished 35-40%. Serum ABP levels were not altered, whatever the duration of irradiation, even though epididymal ABP contents (as well as concentrations) diminished 34-60% when compared to those of the controls. Moreover, in purified Leydig cells, LH-stimulated intracellular cAMP levels, which were decreased by seminiferous tubule medium (STM) from control rats, were enhanced in presence of STM from treated animals. Testosterone output was stimulated 9-fold in presence of oLH and further increased (46-76%) from stages XIV-V by STM prepared from control and irradiated rats, respectively. After 85 days the STM effects on both cAMP and testosterone syntheses were zero. These results demonstrate a probable alteration of Sertoli cell function after irradiation, but also a role of the germ cells in the regulation of the synthesis of ABP, transferrin and Sertoli cell paracrine factors.
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PMID:Effect of continuous low-dose gamma-irradiation on rat Sertoli cell function. 314 90

Sperm maturation and storage occur in a unique milieu created in large part by the epididymal epithelium. To learn more about the interaction of the epididymal epithelial cell with both luminal and systemic environments, we now report on the preparation and characterization of epididymal epithelial cell plasma membranes. A preparation enriched for epididymal epithelial cell plasma membranes was isolated from collagenase-digested epididymal tubule fragments by hand-Dounce homogenization, differential centrifugation, and sucrose gradient centrifugation. The final membrane fraction was enriched 11-fold for the plasma membrane marker 5'-nucleotidase; 2.6-fold for the lysosomal marker acid phosphatase, and 3-fold for the Golgi marker thiamine pyrophosphatase. No enrichment was observed for mitochondrial or endoplasmic reticulum enzyme markers. Specific and saturable transferrin-binding activity was also detected in the final preparation. Electron microscopy revealed the presence of vesicles and sheets of membranes as well as an occasional Golgi apparatus. The plasma membrane fraction was used to generate monoclonal antibodies. Of 102 wells exhibiting growth, 12 were positive by immunofluorescent staining of frozen sections. Ten of these recognized determinants in epithelial cells, and 2 stained peritubular smooth muscle cells. Most of the epithelial cell-specific antibodies stained brush border alone or in combination with the basolateral plasma membrane. Three antibodies stained the Golgi apparatus. Most antibodies were specific for particular epididymal regions, 3 also recognized determinants in the kidney, and 1 stained residual bodies in the testis.
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PMID:Isolation and characterization of epididymal epithelial cell plasma membranes. 336 69

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

To determine the clinical value of seminal transferrin measurements, transferrin concentrations in seminal plasma were determined by single radial immunodiffusion. Men with various disorders of spermatogenesis had significantly lower mean values than those with normal semen (170 micrograms/ejaculate, s.e.m. = 18.4), oligospermia (40.5 micrograms, s.e.m. = 7.2) or azoospermia due to primary seminiferous tubule failure (65.9 micrograms, s.e.m. = 29.1). In these subjects with patent genital tracts, seminal transferrin was directly correlated with sperm concentration and indirectly correlated with serum FSH levels. Seminal transferrin increased following gonadotrophin treatment of men with gonadotrophin deficiency from 19.6 micrograms (s.e.m. = 5.5) to 108.6 micrograms (s.e.m. = 31.7). Patients with genital tract obstructions also had low levels; vasal agenesis (21.8 micrograms, s.e.m. = 5.6), vasectomy (48.5 micrograms, s.e.m. = 21.0), epididymal obstruction (46.6 micrograms, s.e.m. = 7.1). These results confirm that most seminal transferrin comes from the testes and reflects Sertoli cell function. However, there is a very wide range of transferrin levels in normal semen and a number of normospermic samples have low values similar to those seen with abnormal Sertoli cell function or obstruction. Thus, measurement of seminal transferrin is of limited diagnostic value.
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PMID:Seminal transferrin, an index of Sertoli cell function: is it of clinical value? 374 35

Ob17 is a clonal cell line isolated from the epididymal fat pad of C57 BL/6J ob/ob mouse that differentiates into adiposelike cells in serum-supplemented medium. In serum-free medium, this cell line shows increased growth under the addition of insulin, transferrin, fibroblast growth factor (FGF), and a factor present in extract of rat submaxillary gland (SMGE). This medium is referred to as 4F. Epidermal growth factor or nerve growth factor cannot replace SMGE, whereas partially purified platelet extract can substitute for FGF but only partially for SMGE. 4F Medium is able to support the proliferation of cells from other established preadipocyte clonal lines, HGFu and 3T3-F442A, and also of preadipocyte cells isolated from the stromal-vascular fraction of rat and mouse adipose tissues. In each case 4F medium is insufficient to support the differentiation of these cells into adipocytes. Ob17 cells grown and maintained in serum-free hormone-supplemented medium retain the ability to convert to adiposelike cells after serum addition. This serum requirement for differentiation cannot be substituted by the addition of growth hormone or of other putative adipogenic factors, or both. The results are discussed with respect to the requirements for growth and differentiation of the 3T3-L1 and 1246 preadipocyte cell lines previously described.
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PMID:Growth of preadipocyte cell lines and cell strains from rodents in serum-free hormone-supplemented medium. 636 69

Two-dimensional electrophoresis of six fractions of split ejaculates from normal men (median age 23 years, n = 6) revealed large differences in the pattern of proteins found between the prostate-enriched fractions and secretions associated with the seminal vesicles. The glandular contributions were assessed using the concentrations of spermine, zinc and prostatic acid phosphatase (PAP) for prostatic secretion, and fructose and prostaglandin E for seminal vesicle secretion in the various fractions. Aside from PAP, four additional proteins were apparently associated with the prostatic fraction, one of which shared the biochemical characteristics of the specific ventral lobe protein of the rat prostate, prostatein (molecular mass 16 000, pI 4.8). The presumptive vesicular fractions contained a large number of low molecular mass proteins (10-20 000), with widely varying pI-values. The concentration of albumin and transferrin appeared to be highest in the sperm cell enriched fractions, indicating a major contribution to the ejaculate of testicular/epididymal origin.
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PMID:Two-dimensional electrophoresis of proteins in various fractions of the human split ejaculate. 652 15

Vesicular transport of solutes across capillary walls may be regulated by specific solute-endothelial interactions. Little data is available on the vesicular transport of serum proteins which may transit the capillary wall in situ. Capillaries were isolated from epididymal fat and incubated in fluorescent-labeled transferrin and radiolabeled sucrose. Endocytosis and exocytosis of these tracers were quantitated on a picomolar basis over timed intervals and standardized against the amount of endothelial DNA present in the isolate. The rate of vesicular endocytosis of transferrin was 6-7 times greater than that of sucrose indicating a mechanism of selection for transferrin. Endocytosis as a function of external concentration exhibited complex kinetics for transferrin that was consistent with an adsorptive component and a fluid component. Sucrose uptake appeared to be simple fluid endocytosis but with a rate-limiting concentration at 500-600 microM. Vesicular exocytosis of both solutes from preloaded capillaries appeared to occur more rapidly than their endocytosis. This was probably not due to different rates of filling and emptying of attached vesicles nor to an intrinsic difference in rates of vesicle interiorization and refusing with the plasma membrane. Different rates of endocytosis and exocytosis may only be apparent since exocytosis of marker before the capillaries reach ingestion equilibrium would reduce the measured uptake rate.
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PMID:Endocytosis and exocytosis of transferrin by isolated capillary endothelium. 685 37


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