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

Under defined conditions, in the presence of 10 mg/ml of bovine serum albumin, cauda epididymal rat spermatozoa displayed vigorous motility, and a high proportion (81%) of eggs were fertilized. In contrast, no fertilization was observed after omission of albumin, or replacement of the protein by 10 mg/ml of cytochrome c, beta-globulin, gamma-globulin, hemoglobin, lysozyme, and polyvinylpyrrolidone, and 5 mg/ml of ribonuclease. However, high motility occurred in suspensions containing 3 x 10(6) spermatozoa/0.1 ml of medium with cytochrome c, beta-globulin, or gamma-globulin. In medium with 1 mg/ml of ovalbumin, 7% (2/29) eggs were fertilized. Use of defatted albumin resulted in a higher rate of fertilization than unmodified albumin (87 vs 70%), and this difference approached statistical significance. No fertilization was obtained in the presence of albumin presaturated with cholesterol. These results suggest that: (a) rat sperm cells failed to capacitate in the absence of albumin; (b) the protein exerted more than a nonspecific macromolecular effect; and (c) lipids associated with albumin may modify its ability to promote sperm capacitation.
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PMID:Influence of serum albumin on the fertilizing ability in vitro of rat spermatozoa. 125 Aug 65

Cinnamon and Brewer's yeast extracts have been shown to potentiate the action of insulin in isolated adipocytes. In this study, isolated rat epididymal adipocytes were used to evaluate the influence of bovine serum albumin on insulin activity as affected by cinnamon and Brewer's yeast extracts. Albumin at 0.01-0.1% decreased the insulin stimulatory effects of cinnamon from 11.8- to 5.3-fold and 2% albumin decreased this effect to near control levels. Conversely, the insulin-enhancing properties of Brewer's yeast remained low in the presence of less than 0.25% albumin but subsequently increased 2.8-, 4.8- and 5.6-fold in the presence of 0.25, 0.50 and 1.0% albumin, respectively. In the absence of added insulin, increased activity of the insulin-stimulated utilization of glucose by both extracts was observed but only Brewer's yeast extract displayed additive effects when tested at higher insulin levels. Due to the inhibitory and enhancing effects of albumin on the insulin activity of cinnamon and Brewer's yeast, respectively, it is suggested that the effects of albumin be assessed when evaluating the insulin-enhancing effects of other substances using isolated adipocytes.
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PMID:Insulin activity: stimulatory effects of cinnamon and brewer's yeast as influenced by albumin. 129 75

The binding of [3H] delta 6-testosterone photoaffinity-labelled rat androgen-binding protein (rABP) has been studied in an enriched fraction of plasma membranes of epithelial epididymal cells in immature (15 days) and adult rats (40 days). The binding was maximal in less than 30 min and more rapid at 4 degrees C than at 34 degrees C. It was calcium and pH dependent. Scatchard plots of the binding data gave curvilinear plots with two types of binding sites corresponding to a K(ass1) of 18.2 nM-1 and K(ass2) of 1.6 nM-1 (2.2 x 10(11) sites/mg protein and 5.4 x 10(11) sites/mg protein, respectively). In adult rats, only one type of binding site was found, with a K(ass) of 3.7 nM-1 (4.5 x 10(11) sites/mg protein). The number of receptors was 5-fold lower in the cauda than in the caput of the epididymis. The pretreatment of the isolated intact cells with streptozotocin induced a 45% reduction of the binding. Only unlabelled rABP and hSBP (human sex steroid-binding protein) but not other proteins (lactotransferrin, serotransferrin, asialofetuine, fetuine and bovine serum albumin) competed with the labelled ligand to bind plasma membranes. The membrane fraction was solubilized by triton X-100. Its incubation with labelled rABP and hSBP provoked the elution of the tracer as an aggregate into the void volume fraction of superose 6B mini-gel filtration columns. Structural homology between hSBP and rABP could be responsible for the common behaviour of the steroid-carrier molecules for the ABP receptor of rat epididymal epithelial cells.
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PMID:The plasma membrane of epididymal epithelial cells has a specific receptor which binds to androgen-binding protein and sex steroid-binding protein. 131 34

The influence of perfusion medium on in vitro recovery of 14C-oleate to microdialysis probes was investigated. Four perfusion media were investigated: water, 4% bovine serum albumin (BSA) in Ringer solution, 2.25% glycerol in water and a 20% soybean oil/egg phospholipid emulsion (Intralipid). The following order of recovery was found (highest recovery first): BSA = Intralipid greater than glycerol greater than water. The recoveries at 0.5 microliter/min. perfusion rate of the dialysis probe were 4.8%, 4.4%, 2.6% and 1.2% respectively. It was attempted to measure 14C-oleate after intravenous infusion. The samples were extracted with hexane/isopropyl alcohol in order to separate the free fatty acid from products of oxidation which are hydrophilic. Dialysis probes were implanted in interscapular adipose tissue, epididymal fat, muscle, liver and jugular vein of rats. We were not able to detect unbound fatty acids, neither basally nor after stimulation with 1 mg/kg norepinephrine intraperitoneally. However, products of oxidation from the infused oleate were released in response to norepinephrine stimulation. It is concluded that the recovery of lipophilic compounds in microdialysis devices can be improved by means of a lipophilic perfusion medium or by means of e.g. BSA to which the compound binds. The free fatty acid levels were too small to be measureable in vivo in the present study.
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PMID:Microdialysis of lipophilic compounds: a methodological study. 180 49

An autosomal recessive mutation (ipv) causing infertility in homozygous females (ipv/ipv) because of imperforate vaginae was discovered in a line of mice selected for low lean tissue mass as a proportion of body weight. The aim of this study was to determine if the mutation could be propagated in offspring following embryo transfer of oocytes collected from mutant females and fertilized in vitro with sperm from males known to carry the gene (ipv/?). Caudal epididymal sperm were incubated with cumulus-enclosed oocytes for 8-10 hr in tissue culture medium 199 + 5% fetal calf serum + 0.4% bovine serum albumin. Oocytes possessing at least two pronuclei were transferred to recipient CD-1 females which had been mated 24 hr earlier to vasectomized males. A total of 683 oocytes was collected from 27 superovulated mutant females. A large proportion of the oocytes was abnormal as evidenced by cytoplasmic fragmentation (259/683, 38%). Seventy-eight percent (331/424) of the normal oocytes were fertilized and 181 of these were transferred to 10 recipients. Six of 10 recipients delivered 38 offspring (24 females, 14 males). Fifty-eight percent (14/24) of the female offspring displayed an imperforate vagina. The results demonstrate that in vitro fertilization and embryo transfer can be used for propagating a mutant gene that causes infertility in females.
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PMID:Use of in vitro fertilization and embryo transfer to circumvent infertility caused by an inherited imperforate vagina in mice. 191 65

The purpose of this study was to determine whether sulfogalactosylglycerolipid (SGG) was desulfated during mouse sperm capacitation. Levels of [35S]SGG were determined in freshly retrieved caudal epididymal sperm, motile capacitated sperm, and immotile sperm, after feeding mature male mice with [35S]sulfate-laced chow for 32 days. Caudal epididymal sperm and coisolated epididymal cells were separated into pellet and interphase fractions by centrifugation through a two-step Percoll gradient (45 and 90%). Upon resuspension in Krebs-Ringer bicarbonate medium supplemented with 0.4% bovine serum albumin, the Percoll-gradient pellet fraction consisted mainly of motile capacitated sperm, whereas the interphase fraction comprised largely immotile sperm and fragmented epididymal epithelial cells. The level of [35S]SGG in the Percoll-gradient-pelleted sperm appeared to be much higher than that in the Percoll-gradient interphase sperm. Percoll-gradient-pelleted sperm were further incubated in the culture medium for 2 h. The level of [35S]SGG showed little or no change after 1 h, but was reduced appreciably after 2 h. At this time point, sperm motility was also decreased. Reduction of sperm SGG is correlated with sperm immotility and (or) senescence and may have no direct relation to the capacitation process.
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PMID:Levels of sulfogalactosylglycerolipid in capacitated motile and immotile mouse spermatozoa. 234 1

During a search for hormonally responsive products in media from Sertoli cell enriched cultures, a major follicle stimulating hormone responsive and testosterone-responsive protein was identified and designated CMB-1. The results of the present study indicate that this protein is related immunologically to rat albumin and rat alpha-fetoprotein (AFP) and is concentrated in the testis of the adult rat. CMB-1 was therefore termed testibumin. Testibumin was purified from Sertoli cell enriched cultures to apparent homogeneity by sequential high-performance liquid chromatography on anion-exchange, chromatofocusing, gel permeation, and hydroxylapatite columns. The purified protein consists of two concanavalin A (Con A) reactive forms: one which does not interact with Con A and the other which binds to this lectin and is eluted with methyl alpha-mannoside. Testibumin is a monomer with an apparent molecular weight of 69,000 and a pI ranging between 4.5 and 4.85. The heterogeneity of this protein was further demonstrated by crossed-immunoelectrophoresis and two-dimensional gel electrophoresis. A monospecific antiserum and highly purified testibumin were used to develop a specific radioimmunoassay which permitted studies of the hormonal responsiveness of Sertoli cell enriched culture and of the content of testibumin in the reproductive tract fluids in vivo. Even though testibumin was found in serum of both sexes, it was highly concentrated in the testicular and epididymal compartments in adult rats. This protein was compared to rat serum albumin and rat AFP immunologically. With the use of immunoblots, antiserum developed against testibumin showed partial cross-reactivity with albumin and AFP when these latter proteins were denatured and were present in amounts several orders of magnitude greater than testibumin. The extent of this cross-reactivity was then examined by comparing the ability of native and S-carboxymethylated albumin to compete with 125I-testibumin for binding to a monospecific testibumin antiserum. It was shown that the unfolded derivative of albumin showed partial cross-reactivity with testibumin. We conclude that testibumin is immunologically related to albumin and AFP as these latter proteins are related to one another and that testibumin is possibly the homologue of albumin in the seminiferous tubular compartment.
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PMID:Rat testicular testibumin is a protein responsive to follicle stimulating hormone and testosterone that shares immunodeterminants with albumin. 242 98

The murine monoclonal antibody H316 reacts with a cell-surface antigen of human trophoblast, leukocytes, certain epithelia, and several malignant cell types. We have found that the H316 antibody also recognizes an antigen synthesized by pre- and post-meiotic human testicular germ cells and is expressed in the acrosomal region of methanol-fixed testicular, epididymal, and ejaculated sperm. The antigen is poorly expressed on the surface of fresh ejaculated motile sperm, but is detectable on most viable sperm after a 6-h incubation in medium containing human serum albumin (HSA), or 60-min incubation with the calcium ionophore A23187 (both treatments induce sperm acrosomal changes termed capacitation and acrosome reaction). We found that antigen recognized by H316 is immunoprecipitated as a single, broad 50 kDa band from radiolabeled ionophore-treated sperm extracts and that preincubation of HSA-capacitated sperm with this antibody causes a moderate, but significant, inhibition of hamster egg penetration. These data indicate that the antigen recognized by the H316 monoclonal antibody is synthesized by testicular germ cells and is surface-expressed on capacitated/acrosome-reacted sperm populations. Its potential as a human sperm acrosome reaction marker, and possible biological role in sperm-egg or sperm-lymphocyte interactions, warrants further investigation.
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PMID:Trophoblast/leukocyte-common antigen is expressed by human testicular germ cells and appears on the surface of acrosome-reacted sperm. 252 14

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

By using a chemically defined (protein-free) culture medium that supports sperm viability but not capacitation or the acrosome reaction, we have determined that hamster spermatozoa can be chemically capacitated in vitro by the divalent cation chelators D-penicillamine, L-histidine, and L-cysteine in the absence of bovine serum albumin (BSA). Washed cauda epididymal spermatozoa were preincubated (1-2 x 10(6) sperm/ml) for 3, 4, or 6 hr at 37 degrees C in 5% CO2 in air. The basic culture medium used for sperm preincubation and for sperm:egg coincubation was a modified Tyrode's solution (protein-free) containing 10 mM sodium lactate, 100 microM sodium pyruvate, and 1.0 mg/ml polyvinylalcohol (TLP-PVA). Sperm viability was maintained in all preincubation and coincubation media with PHE (20 microM D-penicillamine, 100 microM hypotaurine, and 1.0 microM epinephrine). The low control sperm preincubation medium consisted of TLP-PVA. In some cases the high control preincubation medium also contained 3 mg/ml BSA (TALP-PVA). The experimental preincubation medium was TLP-PVA with additional D-penicillamine (125 or 500 microM), or L-histidine (10, 100, or 1,000 microM) or L-cysteine (25, 75, or 125 microM). After preincubation, sperm were coincubated (2 x 10(4) sperm/ml) with cumulus-free hamster eggs in TALP-PVA +/- additional D-penicillamine, L-histidine, or L-cysteine for 1.5 hr, fixed, and evaluated for percent egg penetration as an index of sperm capacitation. The results demonstrate that hamster spermatozoa can be chemically capacitated in vitro with D-penicillamine (500 microM: range of mean penetration values, 53.6%-84.3%), L-histidine (100 microM: range of mean values, 24.8%-56.3%) or L-cysteine (75 microM: 51.3%) in the absence of exogenous protein.
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PMID:Capacitation of hamster spermatozoa with the divalent cation chelators D-penicillamine, L-histidine, and L-cysteine in a protein-free culture medium. 273 1


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