Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P06889 (Mol)
 630,302 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

1. The capacity of various tissues of the porcine kidney to convert [1-14C]arachidonic acid into radiolabelled prostaglandins was studied. 2. Only after removal from the cortical matrix, were renal blood vessels able to convert arachidonic acid into prostaglandins (primarily prostacyclin). In contrast, convoluted tubules showed a low capacity to metabolize arachidonic acid. 3. The failure to demonstrate prostaglandin synthesis by renal cortical slices is related to the presence of an inhibitor of cyclo-oxygenase. Thus the addition of renal cortical incubate to isolated vascular tissues and ram seminal vesicles inhibited their ability to synthesize prostaglandins. 4. Slices of renal medulla metabolized arachidonic acid primarily to prostaglandin F2alpha; lesser amounts of prostaglandin E2 and prostacyclin were generated. 5. The large capacity of the renal vasculature to generate prostacyclin is consistent with an important role for this prostaglandin in regulation of renin release and renal haemodynamics.
Clin Sci Mol Med Suppl 1978 Dec
PMID:Endogenous prostaglandin synthesis inhibitor in the renal cortex. Effects on production of prostacyclin by renal blood vessels. 10 75

After i.m. injection of [3H]butyrobetaine into rats, the accumulation of carnitine into the epididymis, prostate gland, seminal vesicles, testis and heart was studied. The concentration of radiolabeled carnitine into the cauda epididymis increased linearly with time up to 72 h after the injection of the precursor, while its level in the prostate and seminal vesicles decreased rapidly. Very low levels of carnitine were found in the testis. Castration reduced the carnitine accumulation by cauda epididymis to 6% of the control levels while treatment of castrated animals with testosterone propionate (500 mug/day) partly restored the carnitine uptake. Similar treatment with 17beta-oestradiol valerate or 17alpha-hydroxyprogesterone had no effect. Surprisingly, cyproterone acetate (5 mg/day) also significantly stimulated carnitine accumulation by the epididymis to a level above that of the castrated controls. Simultaneous injection of both cyproterone acetate and testosterone propionate to castrated animals caused an additive effect of these steroids. This indicated that cyproterone acetate in this system is working as a weak androgen. Treatment of rats with 17beta-oestradiol valerate also reduced carnitine accumulation by the cauda epididymis. This is due to suppression of pituiatry gonadotrophin secretion, since concommitant treatment with testosterone propionate (500 mug/day) caused a normalization of the carnitine uptake. Treatment of intact rats with cyproterone acetate significantly reduced the epididymal weight, but not the carnitine accumulation. 17alpha-Hydroxyprogesterone treatment had no effect either on the epididymal weight or the accumulation of the carnitine. Unilateral orchiectomy reduced the carnitine accumulation by the cauda epididymis to about 40% of that occurring in the non-operated control side. This indicates that the luminal contact between the testis and epididymis or the luminal content of the epididymis itself is of importance for the androgen-dependent metabolic process occurring in the cauda epididymis. Castration or hormone treatment did not change the conversion of butyrobetaine to carnitine, or the carnitine uptake by heart. Carnitine uptake by the testis after [3H]butyrobetaine injection was rather low and this would exclude the possibility of synthesis of carnitine in the testis as a source of epididymal carnitine. Carnitine only accumulated in the cauda epididymis in vivo 4 to 96 h after injection of [3H]butyrobetaine. The presence of radioactively labeled butyrobetaine or methylcholine was not detected.
Mol Cell Endocrinol 1975 Aug
PMID:Androgen-dependent accumulation of carnitine by rat epididymis after injection of [3H]butyrobetaine in vivo. 17 Jan 50

The sensitivity of resting and proliferating cells of the seminal vesicle to X-irradiation and adriamycin has been investigated. Stimulation with testosterone propionate (250 micrograms/day) was started 11 days after castration in BALB/c mice. X-rays (2.5-7.5 Gy total body irradiation) and intraperitoneal injections of adriamycin (4-16 mg/kg body weight) were administered at various times before or after induction of proliferation by testosterone injection. The DNA contents and the weights of the seminal vesicles were determined at 4 days after the start of stimulation. A Do for X-rays of about 10 Gy was found for the seminal vesicle epithelium. For both X-irradiation and adriamycin no significant differences in sensitivity were observed between quiescent (Go) and proliferating (G1; S) seminal vesicle cells.
Virchows Arch B Cell Pathol Incl Mol Pathol 1992
PMID:Effects of X-irradiation and adriamycin on quiescent and proliferating cells of the seminal vesicle in the castrated mouse. 134 94

Six lines of transgenic mice harboring the cDNA for polyomavirus large-T antigen (PVLT) linked to the mouse metallothionein-1 promoter were isolated. The transgene was expressed in testes in all lines isolated and in testes and seminal vesicles in two lines. Three lines developed enlarged testes and seminal vesicles. Development of the phenotype was divided into three stages separable by age and pathology. In stage 1, birth to 6 mo, PVLT was expressed in testes but no pathology was noted; in stage 2, 6-10 mo, PVLT was expressed solely in testes and not in seminal vesicles, yet the seminal vesicles were enlarged; and in stage 3, 10 mo and older, both testes and seminal vesicles expressed PVLT and both were enlarged. Testes were up to sevenfold heavier and increased up to fourfold to fivefold in each dimension. Seminal vesicles were enlarged up to 20-fold as the result of an accumulation of seminal vesicle fluid. In addition to the four major proteins of seminal vesicle fluid, extra proteins, initially found in stage 2, were increased in stage 3 seminal vesicle fluid. The Leydig cell was the dominant cell type in affected testes; there were few or no normal Sertoli cells or seminiferous tubules remaining by stage 3. The Leydig cells were physiologically active, as indicated by a 8.5-fold higher testosterone level in sera from stage 3 affected mice compared with sera from age-matched normal males. PVLT was present in the nuclei of the Leydig cells and was able to confer an immortal phenotype in vitro. Formation of the Leydig cell adenoma was dependent on PVLT expression, but since PVLT expression occurred much earlier than did pathology, additional secondary factors must determine the delay in phenotype development.
Mol Carcinog 1992
PMID:Testicular adenoma and seminal vesicle engorgement in polyomavirus large-T antigen transgenic mice. 137 29

Org 30850 (Ac-D-pClPhe1,2,D-Bal3,D-Lys6,D-Ala10-LHRH) is a novel LHRH antagonist, which is being developed for the treatment of hormone-dependent disorders. The activities of this compound with respect to its endocrinological properties and side-effects were tested in rats and the results were compared with one of the first LHRH antagonists: Ac-D-pClPhe1,2,D-Trp3,D-Arg6,D-Ala10-LHRH (Org 30276). A single subcutaneous (s.c.) dose of 0.3 micrograms/kg Org 30850 administered to rats in pro-estrus gave inhibition of ovulation in approx. 50% of the rats, whereas Org 30276 was approx. 4 times less potent. The effect of a single s.c. injection of Org 30850 on testosterone levels in young adult male rats was also studied. The administration of 250 micrograms/kg or higher of Org 30850 induced a significant decrease in testosterone levels after 3 h, this effect lasted for at least 48 h. Treatment of female rats for 14 days with a daily dose of 12 micrograms/kg Org 30850 decreased statistically significantly uterine and ovarian weights. At a daily dose of 50 micrograms/kg Org 30850 completely suppressed estrous cycles and significantly decreased estradiol and FSH serum levels. The LH levels were below the detection level in both control and treated animals on the (expected) second day of di-estrus. Treatment of male rats for 14 days (25-200 micrograms/kg) resulted in a dose-dependent reduction of the gonads, accessory sex organs, testosterone levels and gonadotrophins. The decrease in gonadal function in both sexes was reversible since the females proved to be as fertile as the controls 6 weeks after the last treatment and an almost complete recovery of the weight of testes, seminal vesicles and ventral prostate was observed in the males 4 weeks after cessation of treatment. In contrast to Org 30276, Org 30850 exerted very slight irritation at the site of injection and no edematous reactions in the extremities at a daily dose of up to 8 mg/kg in male rats. It is concluded that Org 30850 is a very potent LHRH antagonist without edematous reactions and with a more favourable therapeutic index than Org 30276.
J Steroid Biochem Mol Biol 1992 Aug
PMID:Properties of a potent LHRH antagonist (Org 30850) in female and male rats. 150 9

Mouse mammary tumor virus (MMTV) is an endogenous murine retrovirus that is expressed in the epithelial cells of the mammary and salivary glands, lungs, kidneys, and seminal vesicles and in the lymphoid cells of the spleen and thymus. Several studies have shown that the long terminal repeat (LTR) of this virus can direct the expression of reporter genes to the same tissues in transgenic mice. To determine whether multiple regulatory elements within the LTR are involved in this tissue-specific expression, we have established lines of transgenic mice containing transgenes that have deletions in the MMTV LTR. Deletions of all LTR sequences upstream of -364 or of LTR sequences from -165 to -665 both result in the expression of linked reporter genes such as the simian virus 40 early region or the bacterial enzyme chloramphenicol acetyltransferase in novel sites, such as the heart, brain, and skeletal muscle; expression of endogenous MMTV and transgenes containing the full-length LTR is not detected in these organs. Negative regulation appears to involve more than one region, since deletion of sequences between either -201 and -471 or -201 and -344, as well as sequences upstream of -364, results in inappropriate expression in heart, brain, and skeletal muscle. Therefore, a negative regulatory element(s) in the MMTV LTR can suppress transcription from the viral promoter in several different organs. This represents the first example of generalized negative regulatory elements that act in many different tissues in transgenic mice to prevent inappropriate expression of a gene.
Mol Cell Biol 1990 Nov
PMID:Negative regulation in correct tissue-specific expression of mouse mammary tumor virus in transgenic mice. 170 Feb 74

Run-on transcription in isolated nuclei has been used to study the effects of testosterone on gene expression in rat seminal vesicles. General transcriptional rates were increased by about 6-fold with an additional 2- to 3-fold differential stimulation of the genes for secretory proteins IV and V. These transcriptional changes are insufficient to explain overall changes in cellular mRNA levels, indicating that androgens must also have major effects on post-transcriptional processing of RNA transcripts or on mRNA stability. Analysis of nuclear RNA by Northern blotting with intron probes suggests substantial androgen effects on primary transcript processing.
Mol Cell Endocrinol 1991 Apr
PMID:Effects of androgens on the transcription of secretory protein genes in rat seminal vesicle. 172 91

The expression of the prolactin (PRL) receptor gene was studied in rabbit tissues by Northern blot and S1 mapping analysis of mRNA preparations. Rabbit mammary gland contained three major (10.5, 3.4, and 2.7 kb) and one minor (6.2 kb) prolactin receptor poly(A)+ RNA transcripts all of which contain the entire coding sequence of the long form of PRL receptor. Each of these mammary mRNAs hybridized equally well with cDNA sequences encoding either the NH2 terminal, middle, or COOH terminal part of the rabbit mammary PRL receptor. The four mRNAs differed only in their 5'- and 3'-untranslated regions. The 10.5 kb mammary transcript was further shown to represent a primary transcript of nuclear origin. Among the various rabbit tissues tested, male and female adrenals, mammary gland, ovaries, and jejunum contained the highest level of prolactin receptor mRNA. The prolactin receptor gene was also expressed at moderate to weak abundance in uterus, liver, kidney, pancreas, testis and seminal vesicles. No prolactin receptor mRNA species were detected in adult muscle, lung, total brain, placental cotyledons and spleen, and in thymus from young animals. In all the rabbit tissues examined, the same four PRL receptor poly(A)+ RNA transcripts identified in the mammary gland were expressed and no additional transcript(s) were detected. Variations in the relative proportion of the 10.5 kb transcript and the two smaller transcripts were observed, while the ratio of the 3.4 and 2.7 kb mRNAs remained unchanged. These findings ask for the role of these different transcripts generated in the rabbit, all of which encode the same long form of PRL receptor precursor but have heterogenous 5'- and 3'-untranslated regions. Moreover, they suggest that the various forms of PRL receptor mRNA originate through differential splicing of a single PRL receptor gene.
Mol Cell Endocrinol 1991 May
PMID:Prolactin receptor gene expression in the rabbit: identification, characterization and tissue distribution of several prolactin receptor messenger RNAs encoding a unique precursor. 181 2

The endocrine profile and the effects on spermatogenesis of the new antiandrogen, Casodex [2RS)-4-cyano-3-(4-fluorophenylsulphonyl)-2-anilide, CAS) were evaluated in the adult rat. In the first experiment rats were administered CAS at daily doses of 10, 20 and 40 mg/kg for 14 days. For comparison groups receiving flutamide (FL, 10 mg/kg) and ethane dimethane sulphonate (EDS) were included. Unlike FL, administration of CAS (10 and 20 mg/kg) did not significantly raise serum concentrations of gonadotropic hormones and testosterone. With 40 mg/kg CAS gonadotropin secretion, but not testosterone levels, were elevated on day 15. Administration of CAS lowered the weight of the seminal vesicles and coagulating glands comparable to the administration of the Leydig cell toxin EDS. In contrast to FL a significant loss of germ cells in stage VII of spermatogenesis was observed with CAS. In a second experiment the ability of FL and CAS to block testicular androgen action was compared in rats with reduced testicular androgen production induced by a gonadotropin-releasing hormone antagonist. Both antiandrogens markedly enhanced spermatogenic involution as revealed by quantitative flow cytometric analysis of germ cell numbers. The study demonstrates that (a) CAS is a peripherally selective antiandrogen and (b) CAS might provide a feasible approach to study androgen dependence of spermatogenesis in the presence of normal FSH levels.
J Steroid Biochem Mol Biol 1991 Mar
PMID:Evaluation of a peripherally selective antiandrogen (Casodex) as a tool for studying the relationship between testosterone and spermatogenesis in the rat. 184 93

A group of four similar proteins, BSP-A1, BSP-A2, BSP-A3, and BSP-30-kDa, represent the major acidic proteins found in bovine seminal plasma (BSP). These proteins are secretory products of the seminal vesicles; they bind to spermatozoa upon ejaculation and could represent decapacitation factors. It has been shown that the glycosaminoglycans present in the female reproductive tract are involved in the capacitation of spermatozoa. Therefore, it was of interest to investigate whether BSP-A1, -A2, -A3, and -30-kDa proteins of bovine seminal fluid interact with heparin. Chromatography of alcohol precipitates of bovine seminal fluid on a heparin-Sepharose column resolved these proteins into three peaks. Peaks 1 and 2 (retarded proteins) were eluted upon extensive washing of the column with 0.05 M phosphate buffer, pH 7.4 (equilibrating buffer), and accounted for approximately 25% of the applied proteins. Proteins in peak 3 represented adsorbed proteins and were eluted with phosphate buffer containing 1 M NaCl. Proteins in each peak were characterized by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) under reducing conditions. Peak 1 contained proteins with molecular weights ranging from 8 to 350 kDa, peak 2 contained a single protein with a molecular weight of 14 kDa, and peak 3 contained proteins with molecular weights of 15.5, 16, 25, and 30 kDa. The proteins in peak 3 were further resolved into unadsorbed (peak 4) and adsorbed (peak 5) proteins on a gelatin-Agarose column. Separation of the proteins of peak 3 and peak 5 by polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate and reducing agents followed by transfer to nitrocellulose and probing with antibodies against the previously well-characterized BSP proteins indicated the presence of BSP-A1, BSP-A2, BSP-A3, and BSP-30-kDa proteins.(ABSTRACT TRUNCATED AT 250 WORDS)
Mol Reprod Dev 1990 Aug
PMID:Identification of heparin-binding proteins in bovine seminal plasma. 217 88


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