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Query: UNIPROT:P11684 (Uteroglobin)
 114 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Uteroglobin was obtained from 5 day pregnant rabbits and purified to homogeneity by Sephadex G 75 and DEAE-cellulose chromatographies. Progesterone binding to uteroglobin was decreased by lyophilization and enhanced by SH-reducing agents. Dithiothreitol was more effective than dithioerythritol, and beta-mercaptoethanol was only active at 25 to 100 mM concentrations. SH-blocking agents (iodoacetate, iodoacetamide, phydroxymercuribenzoate and, dithiobisnitrobenzoic acid) inhibited binding. In the absence of SH-reducing agents only one in every 500 uteroglobin molecules bound the hormone, whereas under optimal conditions (20 mM dithiothreitol) one in every two molecules bound progesterone. There was no significant difference in equilibrium dissociation constants under these two conditions. Uteroglobin had a relatively high affinity for progesterone (KD=4.1 X 10(-7)M) but a threefold higher affinity for 5alpha-pregnane-3,20-dione (KD=1.3 X 10(-7)M). Estradiol was bound but non-specifically with a very low affinity, and its binding was not enhanced by SH-reducing agents. Hormonal specificity of binding to uteroglobin was different from that of binding to rabbit uterine progesterone receptor. Various synthetic progestagens (chlormadinone acetate, norethisterone, R5020) were bound to the latter but not to the former protein. Diethylstilbestrol had some affinity (15% of that of progesterone) for uteroglobin and no affinity for the progesterone receptor. Uteroglobin incubated in the presence or absence of cofactors (NADH and NADPH) with or without dithiothreitol did not metabolize progesterone.
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PMID:Interaction of uteroglobin with progesterone, 5alphapregnane-3,20-dione and estrogens. 1 Oct 93

1. The uterine luminal fluid of rabbits treated with estradiol and progesterone contains a protein factor with high affinity for [3-H] progesterone which is not present in the uterine secretion of control rabbits treated with estradiol. 2. This progesterone dependent factor is shown by gel filtration and polyacrylamide gel electrophoresis to be identical with the uterus specific protein uteroglobin, which seems to be required during the preimplantation phase. Uteroglobin specific antiserum, prepared in guinea pigs, completely inhibits the progesterone binding activity of the proteins of the uterine fluid. 3. Progesterone binding to uteroglobin is dependent upon millimolar concentrations of dithioerythritol. At saturation, one molecule of progesterone binds per uteroglobin molecule and the apparent association constant is 2 x 10-6 M-1 at 0 degrees C. 4. The progesterone binding species of uteroglobin exhibits a molecular weight of around 12 000 on polyacrylamide gels containing dodecylsulfate, and of 15 000 upon gel filtration, indicating a non-globular shape. This molecule is compased of two subunits of similar molecular size which are held together by a disulfide bridge among other forces.
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PMID:Binding of progesterone to the proteins of the uterine luminal fluid. Identification of uteroglobin as the binding protein. 16 37

Uteroglobin, a progesterone-induced uterine protein of the rabbit, is synthesized in cell-free systems as a precursor containing 21 additional amino-acids at its N-terminal end. The mRNA for pre-uteroglobin has been purified from the membrane-bound polysomes of induced endometrium and used as template for the synthesis of a full copy complementary DNA. Final purification of the cDNA was based on hybridization to the template mRNA up to a low value of r0t (0.01 M . s) and digestion of the non-hybridized cDNA by S1 nuclease. A comparison of the hybridization kinetics of the pre-uteroglobin cDNA and rabbit globin cDNA to their respective templates indicates a nucleotide sequence complexity of 650 for pre-uteroglobin mRNA, in agreement with the values obtained by sucrose gradient centrifugation and polyacrylamide gel electrophoresis in formamaide. The melting temperature of the hybrids of pre-uteroglobin cDNA to its template reflects the absence of mismatched sequences. This cDNA has been used to quantify pre-uteroglobin mRNA sequences in the endometrial RNA from control animals and from animals treated sequentially with estradiol and progesterone. In agreement with the induction of uteroglobin-synthesizing activity, there is a dramatic increase in the uterine content of pre-uteroglobin mRNA after hormonal treatment. Part of this effect can be accounted for by hormonally induced cell proliferation. When expressed on a DNA basis there is a 50--100-fold increase in the cellular content of pre-uteroglobin mRNA following hormonal treatment.
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PMID:Synthesis and characterization of a DNA complementary to pre-uteroglobin mRNA. 49 5

Embryo mortality and altered uterine luminal proteins were studied in progesterone-treated rabbits. Progesterone was injected into rabbits on Days -2, -1, and 0 (the day of mating) at doses of .5, 1, and 1 mg, respectively. Normal fertilization rates resulted, however, embryonic death occurred by Day 4. Embryos in progesterone-treated does for up to 3 days survived normally when transferred to normal recipients, whereas Day 4 embryos from treated does exhibited a reduced ability to implant. The uterine fluid (UF) protein pattern was examined on Days 1-7 after mating. Total UF protein levels were significantly greater (p less than .05) in treated animals on Day 4 than in controls. Uteroglobin secretion was significantly advanced (p less than .05) in the treated animals by Day 3. Examination revealed a delay in the time of the arrival of embryos into the uterus in progesterone-treated rabbits. This delay, coupled with the earlier secretion of uteroglobin in the treated- rabbits, suggested a possible asynchrony of approximately 1 day between embryo arrival in the uterus and certain uterine proteins. Embryonic development in vitro and in vivo was examined after exposure to UF collected at various gestational stages. More normal Day 3 morulae placed in UF from Day 3 control and Day 2 progesterone-treated rabbits developed than similar morulae placed in UF from Day 2 controls and Day 3 progesterone-treaded does. Therefore, partial physiologic synchrony was achieved, suggesting that ''asynchronous'' UF can be embryotoxic. It is concluded that the ability of does to produce young at a pregnancy immediately following a progesterone-treated pregnancy was not impaired.
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PMID:Embryo mortality and altered uterine luminal proteins in progesterone-treated rabbits. 55 59

Uteroglobin, a steroid-binding protein of the uterine secretion of the rabbit which is induced by progesterone, comprises two identical polypeptide chains of 70 amino acid residues linked by two disulfide bonds. The primary structure has been determined by using both automated and manual methods of Edman degradation. Overlapping peptides were isolated from tryptic, and CNBr digests. The sequence is not homologous to any known protein except for a small acidic region (residues 22-29) resembling a sequence found in somatotropin. The C-terminal half is relatively basic. Implications for the secondary structure are discussed.
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PMID:Amino acid sequence of progesterone-induced rabbit uteroglobin. 56 83

Uteroglobin is a protein secreted by the rabbit uterus in response to progesterone. In cell-free translation systems, the mRNA for uteroglobin codes for a protein larger in size than the secreted protein. To investigate the relationship between these two forms, the NH2-terminal sequences of pre-uteroglobin and of uteroglobin have been determined. Uteroglobin was purified from rabbit uterine flushings and pre-uteroglobin was obtained by immunoprecipitation of the products of translation of poly(A)-rich endometrial RNA in the wheat germ system in the presence of single or multiple radioactive amino acids. Sequencing was performed by automated Edman degradation and the residue at each cycle was identified by chromatography. The larger size of pre-uteroglobin is accounted for by a 21-amino-acid leader sequence, containing 15 hydrophobic residues, at the NH2 terminus. The sequence Thr-Leu-Ala-Leu occurs twice in the leader region. In common with other secretory proteins, the transient hydrophobic extension at the NH2 terminus of pre-uteroglobin may function to assist transfer of the nascent peptide into the lumen of the endoplasmic reticulum, as proposed in the "signal" hypothesis.
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PMID:Progesterone-induced secretory protein. NH2-Terminal sequence of pre-uteroglobin. 76 58

Rabbit embryos were grown in vitro from the 2- and 4-celled stage to expanded blastocysts. Proteins from the blastocysts were analyzed for specific uterine proteins as well as for bovine serum albumin (BSA), a constituent of the medium. Immunological methods revealed the presence of rabbit albumin and larger amounts of BSA. Uteroglobin, the prevailing protein fraction present in blastocyst fluid of embryos that developed in vivo was not detected in blastocysts in vitro. Prealbumin and beta-glycoprotein were also absent. From the data presented, it appears that the blastocyst does not have the capacity to synthesize detectable concentrations of uterglobin and/or other specific uterine proteins.
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PMID:Uteroglobin and other proteins in rabbit blastocyst fluid after development in vivo and in vitro. 80 28

In a BCG vaccination trial in an area of Uganda endemic for Mycobacterium ulcerans disease ("Buruli Ulcer"), 8,856 persons were examined for the disease in mid-1970 and tuberculin tested; BCG was given by intradermal injection to a random 50% of all those with negative, low or middle grade tuberculin reactions; Twelve months later the study group was re-examined for M. ulcerans lesions and, subsequently, new cases of the disease were detected, using a hospital registration system, to December 1974. One hundred and forty-nine patients with onset since July 1970 were thus ascertained and BCG was found to offer an overall protection of 47% against the disease, similar to that observed in a previous smaller trial by the Uganda Buruli Group (UBG, 1969). However, the protective effect was confined to those with tuberculin reactions of less than 4 mm before vaccination and was apparent only in the first year of the study. BCG offered no additional protection to those with previous M. ulcerans disease or an existing BCG scar at entry into the trial, although both these groups appeared to be protected against the disease, the protective effects being 88% and 82% respectively. An initial tuberculin reaction of 4 mm (or greater) offered some protection against the disease (37%). Lesions developing in the vaccinated group, or in those with initial tuberculin reactions of 4 mm or more, were smaller than those in unvaccinated persons. No relationship was found between the protective effect of BCG and either the prevalence of persons with evidence of previous M. ulcerans disease in different geographical areas, or the incidence of new cases in different areas during the first year of the study. A decline in the incidence was observed over the study period. The findings are consistent with BCG producing only short-lasting protection against M. ulcerans disease. However, long-lasting protection and a delay in onset of the disease in vaccinated persons, as suggested by the UBG in 1969, cannot be excluded on the basis of the data currently available from this trial.
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PMID:The protective effect of BCG against Mycobacterium ulcerans disease: a controlled trial in an endemic area of Uganda. 84 47

Uteroglobin was measured under various hormonal conditions: pregnancy, pseudopregnancy, pseudopregnancy with exogenous progesterone, pseudopregnancy with exogenous 20alpha-hydroxyprogesterone, ovariectomy with exogenous progesterone, ovariectomy with exogenous estrogen, ovariectomy with exogenous estrogen and progesterone, and ovariectomy with either exogenous progesterone or estrogen and progesterone, plus uterine trauma. In pregnant females, uteroglobin levels diminished sharply after day 9. In pseudopregnancy, high concentrations were maintained through day 14. Although exogenous progesterone did not prevent this decrease in pseudopregnant females, re-elevation occurred in the continued presence of progesterone. A similar pattern of decline and re-elevation was found in ovariectomized females that received injections of estrogen and progesterone. With an increase in estrogen dosage, the period of uteroglobin secretion was shorter and the magnitude lower. Ovariectomized females receiving only progesterone did not manifest a clear uteroglobin diminution. Uterine trauma on day 7 of exogenous steroid administration to ovariectomized females was followed by a diminution in uteroglobin. At the dosage level used, administration of 20alpha-hydroxyprogesterone did not affect the peak uteroglobin secretion occurring on day 5 of pseudopregnancy. Ovariectomized females receiving estrogen or sesame oil vehicle had barely detectable levels of uteroglobin. A uteroglobin-estrogen complex is suggested as a possible inhibitor of uteroglobin synthesis by a feedback inhibition pathway in pseudopregnant females and in ovariectomized females treated with progesterone plus estrogen. In pregnant females, a uteroglobin-estrogen complex and/or the uterine decidual response to implantation could control uteroglobin synthesis.
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PMID:Factors in diminution of uteroglobin secretion in the rabbit. 124 43

The rat Clara cell 17 kDa protein (previously referred to as the rat Clara cell 10 kDa protein) has been reported to inhibit phospholipase A2 and papain, and to also bind progesterone. It has been isolated from rat lung lavage fluid and crystallized in the space group P6(5)22. The structure has been determined to 3.0 A resolution using the molecular replacement method. Uteroglobin, whose amino acid sequence is 55.7% identical, was used as the search model. The structure was then refined using restrained least-squares and simulated annealing methods. The R-factor is 22.5%. The protein is a covalently bound dimer. Two disulfide bonds join the monomers together in an antiparallel manner such that the dimer encloses a large internal hydrophobic cavity. The hydrophobic cavity is large enough to serve as the progesterone binding site, but access to the cavity is limited. Each monomer is composed of four alpha-helices. The main-chain structure of the Clara cell protein closely resembles that of uteroglobin, but the nature of many of the exposed side-chains differ. This is true, particularly in a hypervariable region between residues 23 and 36, and in the H1H4 pocket.
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PMID:Refined structure of rat Clara cell 17 kDa protein at 3.0 A resolution. 156 Apr 60


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