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)

1. Intact rat epididymal fat-cells were incubated with 32Pi, and the intracellular proteins were separated by sodium dodecyl sulphate/polyacrylamide-gel electrophoresis. One of the separated bands of phosphorylated proteins had an apparent subunit mol.wt. of 42 000, which is the same as that of the alpha-subunit of the pyruvate dehydrogenase complex. By using a combination of subcellular fractionation, immunoprecipitation with antiserum raised against pyruvate dehydrogenase complex and two-dimensional electrophoresis it was apparent that the incorporation into alpha-subunits accounted for 35--45% of the total incorporation into this band of phosphoproteins. 2. The increase in the initial activity of pyruvate dehydrogenase that follows brief exposure of fat-cells to insulin was shown to be associated with a decrease in the steady-state incorporation of 32P into the alpha-subunits of pyruvate dehydrogenase. 3. Tryptic peptide analysis of pyruvate dehydrogenase [32P]phosphate, labelled in intact fat-cells, indicated that three serine residues on the alpha-subunit were phosphorylated, corresponding to the three sites phosphorylated when purified pig heart pyruvate dehydrogenase was incubated with [gamma-32P]ATP. The relative phosphorylation of all three serine residues appeared to be similar in 32P-labelled alpha-subunits in both control and insulin-treated fat-cells.
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PMID:Studies on the incorporation of [32P]phosphate into pyruvate dehydrogenase in intact rat fat-cells. Effects of insulin. 701 13

The seasonal variations in the ultrastructure and physiology of the epididymis of hedgehog were studied in relation to the reproductive functions. Five adult male hedgehogs were sacrificed every alternate month for one calendar year and the epididymis was fixed in Bouin's, Zenker and formol-calcium for light microscopy and in cold buffered glutaraldehyde, post-fixed in osmium tetraoxide for electron microscopy. The epididymal epithelium consists of four types of cells, the principal, the apical, the dark and the basal cells. The principal cells like other steroid synthesizing cells, contain the extensive Golgi apparatus, the smooth and the rough endoplasmic reticulum (SER and RER), the secretory vesicles and the lipid granules during the breeding season, but they are practically devoid of these cell organelles during regression, except for the retarded Golgi and moderate RER. The basal cell, on the other hand, show lipids and well developed organelles during regression but poorly developed structure in the sexually active hedgehog and possibly function as the cells storing lipids during regression and which are subsequently used at the beginning of the recrudescence. The epididymal epithelium recrudesces along with the seminiferous epithelium prior to the spermatozoa reaching the epididymal lumen, whereas the accessory sex glands which are also the extratesticular androgen dependent organs, still show regressed structure. Thus, the ultrastructural and the physiological observations suggest that the principal cells are probably the site of androgen synthesis and they become fully developed along with the cells in the testis on stimulation from the pituitary at the beginning of the recrudescence.
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PMID:Correlative study of the ultrastructure and the physiology of the seasonal regression of the epididymal epithelium in the hedgehog Paraechinus micropus. 725 98

Tyrphostins inhibit tyrosine kinases and have little effect on the activity of serine/threonine kinases. Pyruvate dehydrogenase kinase inactivates pyruvate dehydrogenase by phosphorylating serine residues within the multienzyme complex. This serine/theronine kinase represents a new family of protein kinases, and one (tyrphostin 47) of two tyrphostins tested appeared to activate the pyruvate dehydrogenase kinase as determined by [1-14C]-lactate oxidation to 14CO2. Experiments designed to determine if the tyrphostins altered pyruvate dehydrogenase activity in mitochondria prepared from rat epididymal adipocytes using [1-14C]-pyruvate as the substrate demonstrated a dose dependent increase in enzyme activity in the presence of tyrphostin 47, but not in tyrphostin 23. This apparent stimulation of pyruvate dehydrogenase activity was attributed to tyrphostin 47's ability to nonenzymatically decarboxylate [1-14C]-pyruvate, the substrate for the pyruvate dehydrogenase assay. Neither tyrphostin directly altered pyruvate dehydrogenase kinase activity. Therefore, assays utilizing [1-14C]-pyruvate and tyrphostin 47 are subject to analytical interference.
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PMID:Tyrphostin 47 nonenzymatically decarboxylates [1-14C]-pyruvate. 781 37

A protein kinase that causes phosphorylation of serine and threonine residues of casein has been partially purified from goat cauda-epididymal sperm plasma membrane and characterized. The kinase, solubilized from the membrane with 1.0% Triton X-100, was purified to 480-fold by using DEAE-cellulose and casein-Sepharose affinity chromatographic techniques. The kinase is a strongly basic protein with pI of 9.5. The enzyme has a molecular mass of 310 kilodaltons as estimated by Sephacryl S-300 gel exclusion. The kinase showed affinity for protein substrates in the order membrane proteins > casein > phosvitin > histone > protamine. The apparent Km values of the kinase for casein and membrane proteins were 1 and 0.15 mg/mL, respectively. The synthetic peptides Kemptide and poly(Glu80Tyr20) did not serve as substrates of the enzyme. ATP, rather than GTP or PP(i), is the donor of phosphate for the phosphorylation reaction. Cyclic AMP and GMP, NaCl (0.25 M), KCl (0.25 M), Ca2+, calmodulin, phosphatidylserine, and muscle protein kinase inhibitor had no appreciable effect on the kinase activity. Heparin (0.5 microgram/mL) showed high affinity for inhibiting only 40% of the kinase activity, whereas polyamines at a relatively high concentration (5 mM) inhibited 40-50% of the enzymic activity. The kinase appears to be distinct from other protein kinases including casein kinases. The activity of the kinase derived from the purified sperm plasma membrane was markedly (approximately 90%) lost when the intact spermatozoa were pretreated with diazonium salt of sulfanilic acid, a membrane nonpenetrating surface probe.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Purification and characterization of a protein kinase from goat sperm plasma membrane. 784 Sep 41

Prolactin treatment to castrated rats led to accumulation of triacylglycerol and esterified cholesterol. There was no appreciable drift in epididymal cholesterol: phospholipid ratio between the prolactin treated and control animals. However, further analysis of phospholipids showed a build up of phosphatidyl inositol, phosphatidyl choline and phosphatidyl ethanolamine but a drop in the levels of phosphatidyl serine and sphingomyelin in prolactin treated castrated rats as compared to those castrated animals injected with vehicle alone. Changes in phospholipids reported above were prominently seen in the group of castrated rats that received 100 micrograms oPRL/100 g body weight but not in those animals which received either lower or higher doses of the hormone. Interestingly, bromocryptine treatment in castrated rats produced a general depletion in the levels of all lipid classes studied in the epididymis. It is suggested that this may be due to impaired synthesis and/or increased breakdown of lipids in this organ.
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PMID:Impact of prolactin on epididymal lipid profile in castrated rats. 792 19

Some of the acute actions of insulin may be mediated by an enzyme-modulating inositol phosphate glycan, produced by the insulin-sensitive hydrolysis of a glycosyl phosphatidylinositol that is structurally similar to a membrane protein anchor. An inositol glycan fragment from the structurally characterized Trypanosoma brucei variant surface glycoprotein glycosyl phosphatidylinositol anchor inhibits isoproterenol-stimulated lipolysis in intact rat epididymal adipocytes in a manner mechanistically similar to that of insulin. To explore these effects in more detail, we evaluated the effects of this glycan on protein phosphorylation. Isoproterenol stimulates the phosphorylation of a 70-kilodalton (kDa) protein in these cells. Like insulin, the glycan fragment specifically attenuates the phosphorylation state of the phosphoprotein. In purified adipocyte cytosol, the glycan stimulates the dephosphorylation on serine residues of a 70-kDa protein in a time- and dose-dependent fashion. The glycan-dependent dephosphorylation of the 70-kDa phosphoprotein is unaffected by addition of trifluoroperazine, an inhibitor of serine/threonine phosphatase-2B, but is blocked by the addition of okadaic acid, an inhibitor of serine/threonine phosphatase-1 and -2A. The differential sensitivities of this dephosphorylation reaction to polycations, which activate phosphatase-2A, and phosphorylated inhibitor 1, which blocks phosphatase-1, suggest that dephosphorylation of the 70-kDa protein results from the specific activation of a type 1 serine/threonine phosphatase in adipocytes, providing a mechanistic basis for the insulin-mimetic effects of the inositol glycan.
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PMID:An inositol phosphate glycan derived from a Trypanosoma brucei glycosyl phosphatidylinositol promotes protein dephosphorylation in rat epididymal adipocytes. 795 8

Seven independent cross-hybridizing clones have been isolated from a Macaca fascicularis epididymal cDNA library and their inserts shown to correspond to a secreted inhibitor of the sperm serine proteinase, acrosin. Hybridizing transcripts of approx. 0.6 kb have been shown by Northern blot analysis to be considerably more abundant in the epididymis than the testis. This finding is in surprising contrast to a previous report that human acrosin-trypsin inhibitor mRNA predominates in the testis.
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PMID:Sequence analysis of monkey acrosin-trypsin inhibitor transcripts and their abundant expression in the epididymis. 843 54

The proto-oncogene c-raf-1 and the related genes A-raf and B-raf encode serine/threonine protein kinases thought to be involved in regulating gene expression by acting as part of second-messenger signaling pathways within the cell. Among the tissues in which A-raf and c-raf-1 have been shown to be expressed was mouse epididymis. The present studies were undertaken to determine if the raf family genes exhibited specificity in their pattern of expression that might be indicative of specific function in the epididymis. Northern and in situ hybridization analyses demonstrated that c-raf-1 mRNA was expressed as a 3.1 kb transcript at uniform levels throughout the length of the epididymis in all types of epididymal epithelial cells. Neither the germ cell-specific testicular transcripts nor the somatic transcripts of B-raf were detected by either Northern or in situ hybridization analysis in any region of the epididymis. A-raf, expressed as two transcripts of 2.6 and 4.3 kb, was the only gene examined which exhibited a segment-specific pattern of expression, being highest in the principal epithelial cells of the proximal caput epididymis and decreasing progressively in more distal regions of the tubule. These studies indicate that each raf gene exhibits a characteristic pattern of expression in the epididymis; A-raf in particular may play a unique regulatory role in the regionalized functions of the epididymis.
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PMID:Members of the raf gene family exhibit segment-specific patterns of expression in mouse epididymis. 850 75

Binding of mammalian spermatozoa to the zona pellucida of homologous eggs is mediated by specific molecules on their surface membranes. In the present investigation we describe the biogenesis, epididymal processing and cellular distribution of a plasma membrane antigen (2B1) on rat spermatozoa that has a potential role in mediating zona binding. 2B1 is expressed postmeiotically in the testis as a precursor glycoprotein (approximately 60 kDa) that first appears on the plasma membrane of stage 6 to 8 round spermatids. Northern and western blot analyses show that there is a close correlation between the timing of transcription and expression of the glycoprotein on the cell surface. During spermatid elongation 2B1 is excluded from the head domain and is sequestered onto the sperm tail. As spermatozoa pass through the caput epididymidis 2B1 is endoproteolytically cleaved at a specific arginine residue (Arg 312) to produce a heterodimeric glycoprotein (approximately 40 kDa and approximately 19 kDa) containing intramolecular disulphide bridges. Endoproteolysis at Arg 312 also takes place during culture of washed testicular or caput spermatozoa in vitro and can be prevented by serine proteinase inhibitors or enhanced by trypsinisation. However, neither processing in vivo or in vitro has any effect on the domain organisation of 2B1 antigen i.e. it remains localised to the tail. These results support the hypothesis that sperm antigens that are important for fertilization are synthesized as precursor molecules in the testis and are then "activated' during epididymal maturation and capacitation, thereby ensuring that they only become fully functional at the site of fertilization.
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PMID:Testicular biosynthesis and epididymal endoproteolytic processing of rat sperm surface antigen 2B1. 892 17

Guanidinobenzoatase (GB), a proteolytic enzyme found in the epididymal fluids of mice, was purified to apparent homogeneity by molecular sieving and affinity chromatography. It has a molecular mass of 71 kDa and its enzymatic activity is heat labile and sensitive to EGTA. Its kinetic parameters (K(m) of 6.66 microM and a Vmax of 4.38 nmol/min/mg) were determined using 4-methylumbelliferyl-p-guanidinobenzoate (MUGB) as the substrate. GB activity is concentrated in the cauda epididymal region of the genital tract. Heat-solubilized whole zonae, biologically active ZP3, and several serine proteinase inhibitors, including a proteinase inhibitor endogenous to the male genital tract, effectively block the ability of GB to hydrolyze MUGB. Pretreating cumulus-free, zonae intact oocytes with purified GB reduces, in a concentration-dependent manner, the number of sperm able to bind to the zonae. The function of the soluble enzyme is not known. Its ability to bind both trypsin inhibitors and ZP3 suggests a possible role in gamete recognition.
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PMID:Characterization of the guanidinobenzoatase in the epididymal fluids of the mouse. 913 23


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