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

Uteroglobin is a small steroid-binding protein that is differentially regulated by steroid hormones in several tissues of the rabbit. In endometrium, the levels of uteroglobin mRNA increase after progesterone administration due to an enhanced rate of transcription of the uteroglobin gene. As a prerequisite for understanding the molecular mechanisms that modulate uteroglobin gene expression, we have isolated and characterized the uteroglobin gene. We first synthesized, cloned, and sequenced a uteroglobin cDNA that was used to screen a rabbit gene library and to show that the uteroglobin gene is not reiterated in the rabbit genome. We obtained three recombinant phages containing uteroglobin gene sequences and covering 35 kilobases of the rabbit genome. The uteroglobin gene is 3 kilobases long and is composed of three short exons separated by a long and a short intron. The complete coding sequence, the short intron, part of the large intron, and the flanking sequences have been subjected to sequence analysis. The salient features of the nucleotide sequence, including the absence of a canonical "T-A-T-A box," are discussed. A possible relationship is considered between the exon-intron structure of the gene and the known structure and function of uteroglobin.
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PMID:Isolation and structure of the gene for the progesterone-inducible protein uteroglobin. 695 97

1. Uteroglobin-like antigens were found in the lung and uterus of the hare (Lepus) and the pika (Ochotona). These antigens presented an immunoreactivity indistinguishable from that of rabbit uteroglobin, as determined by radioimmunoassay. 2. The molecular weight and the subunit composition of these antigens were similar to those of rabbit uteroglobin as analyzed by SDS gel-electrophoresis. 3. Similar amounts of uteroglobin-like immunoreactivity were found in the respective lungs and uteri of hare and rabbit whereas the concentration of immunoreactivity in the pika organs was several-fold lower.
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PMID:Uteroglobin-like antigens in species of Lagomorpha. 706 7

Uteroglobin is a predominant protein in the rabbit uterus, where it is induced by progesterone, and occurs also in the lung, where its level is constitutive. A recombinant plasmid containing uteroglobin complementary DNA (cDNA) has been constructed previously from partially purified uteroglobin mRNA. In this study, the cloned uteroglobin cDNA has been used as a probe to determine the cellular content of uteroglobin mRNA at different times in early pregnancy in both rabbit uterus and lung. By RNA-excess hybridization to poly A-enriched RNA and to total nucleic acid extracts an increase in steady-state uteroglobin mRNA level was detected, from approximately 250 molecules/uterine epithelial cell in non-pregnant rabbits to approximately 6800 molecules/cell on day 4 of pregnancy, after which the levels declined progressively up to day 8. The pulmonary level of uteroglobin mRNA was about 400 molecules/cell and did not change significantly with day of pregnancy. The major factor in regulating the production of uteroglobin in the uterus of pregnant rabbits is the accumulation and subsequent depletion of its mRNA.
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PMID:Hybridization analysis of steady-state levels of uteroglobin mRNA in rabbit uterus and lung during early pregnancy. 711 50

The physiological androgen, 5 alpha-dihydrotestosterone (DHT), enhances a progesterone-regulated protein (uteroglobin) synthesis in the rabbit uterus. In order to clarify the induction mechanism(s), rabbits were treated for 5 days with DHT alone or concomitantly with a nonsteroidal antiandrogen, RU 23908, or with different doses of estradiol. Uteroglobin content was measured in the uterine fluid by radioimmunoassay and uteroglobin mRNA activity in uterine tissues using cell-free translation in vitro. Uteroglobin induction elicited by DHT was inhibited by a small dose of estradiol, but not by antiandrogen. These results support the idea tha androgens bring about their action on uteroglobin synthesis via a mechanism involving uterine progesterone receptor.
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PMID:5 alpha-Dihydrotestosterone-induced uteroglobin synthesis in rabbit uterus is not inhibited by antiandrogen administration but is prevented by estradiol. 728 83

The synthesis of uteroglobin in rabbit lung was studied after the administration of glucocorticoids to intact adult animals as well as during the late stages of rabbit development. The synthesis of uteroglobin was compared with levels of translatable uteroglobin mRNA in the lung. Uteroglobin synthesis was determined both by incorporation of [25S]methionine into the protein by lung explants incubated in vitro and by radioimmunoassay measurements of uteroglobin concentration in lung. Lung poly(A)-containing mRNA, isolated by oligo(dT)--cellulose chromatography, was translated in cell-free systems and the activity of uteroglobin mRNA was determined after immunoprecipitation. Dexamethasone administration increased about 2-fold the synthesis of lung uteroglobin compared with the controls. The effect of cortisol was more moderate. Both glucocorticoids did not affect the degradation rate of lung uteroglobin, but produced increases in the translatable levels of uteroglobin mRNA parallel to those observed for uteroglobin synthesis. During the late stages of rabbit development, both the synthesis of lung uteroglobin and the translatable levels of its mRNA increase in parallel about 12-fold in a biphasic fashion. A first increase occurred between 2 days before and 2 days after birth. Starting at 5 days of age, there was a second increase in both parameters, which at 12 days of age reached values close to those observed in adult rabbits. Our results suggest that the rate of lung uteroglobin synthesis could be mainly determined by the translatable levels of its mRNA.
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PMID:Glucocorticoid and developmental regulation of uteroglobin synthesis in rabbit lung. 734 64

The Clara cell phospholipid-binding protein, previously referred to as CC10, is a homodimeric protein of M(r) 15,800. It is secreted into the bronchioalveolar lining layer in mammalian lung. A combination of X-ray crystallography and chemical analysis was used to determine that phosphatidylcholine and phosphatidylinositol are bound to the protein as isolated from human lung lavage. We now report the crystal structure of the protein-phospholipid complex at 1.9 A resolution. The phospholipid is bound inside the protein's large hydrophobic cavity. A model is proposed for the manner in which a channel may open to provide access to the cavity, allowing the binding or potential release of phospholipid.
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PMID:Structure of a human Clara cell phospholipid-binding protein-ligand complex at 1.9 A resolution. 766 82

Lung cancer is a leading cause of tumor-related deaths in humans but its origin and development are poorly understood. To study the biology of these tumors, appropriate animal and cell culture models will be of eminent importance. Uteroglobin is a marker protein for the nonciliated epithelial Clara cells lining the respiratory and terminal bronchioli of the lung. We have used the promoter and 5'-flanking sequences of the rabbit uteroglobin gene to target expression of the SV40 T antigen to the lung of transgenic mice. All transgenic founders as well as the descendants from an established line, UT7.1, developed multifocal bronchioloalveolar adenocarcinomas originating from Clara cells. At least three different stages in tumor development with progressive loss of the differentiated phenotype can be distinguished by immunohistochemical data and in situ hybridization. Only in the initial stage did bronchiolar cells express both uteroglobin and SV40 T antigen, whereas at later stages, only SV40 T antigen was detected, and the most advanced tumors were negative for both proteins. Starting from the lungs of UT7.1 mice, a bronchiolar cell line was established that maintains the features of differentiated Clara cells. This system provides a useful model for further studying the development and progression of lung adenocarcinomas in vivo and in vitro.
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PMID:A transgenic mouse model for lung adenocarcinoma. 771 90

Uteroglobin, a progesterone-binding secretory protein, was shown to bind retinoic acid and retinol in a non-saturable manner, at least up to concentrations of retinoids of 20 microM. Binding is increased about 10-fold by previous reduction of uteroglobin with 10 mM dithiothreitol and it is not affected by previous saturation of the progesterone binding site, suggesting different binding sites for the steroid and the retinoids. The results are discussed in relation to a possible physiological role for this protein.
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PMID:Binding of retinoids to uteroglobin. 805 May 75

The distribution of uteroglobin mRNA has been investigated in the endometrial compartments of the rabbit uterus during early pregnancy (day 0.5 p.c.--day 12 p.c.) using nonradioactive in situ hybridization. Digoxigenin-dUTP labeled oligodesoxy-nucleotide-probes (24mer) and an anti-digoxigenin-antibody conjugated with alkaline phosphatase were developed and used. It could be shown, that uteroglobin mRNA localization is restricted to the endometrial epithelium. There are differences in the extent of uteroglobin mRNA expression within the epithelial cells, which is in accord with our interpretation on the existence of different epithelial cell populations. From day 0.5 p.c. to day 9 p.c. the cells of the basal glands express uteroglobin mRNA continuously, whereas the proliferating surface epithelium shows a remarkable fluctuating pattern of uteroglobin mRNA expression. On day 2 p.c. the whole surface epithelium starts to express the uteroglobin message, and up to day 5 p.c. all these cells show a high level of uteroglobin mRNA expression, which drops significantly on day 6 p.c., when significant changes in the cyto-morphology of the surface epithelium for implantation occur. On day 7 p.c., there is no more uteroglobin mRNA expression in the surface epithelium, however remaining expression in the basal glands. The latter is evident up to day 9 p.c. From day 10 p.c. onwards, neither the luminal nor the deep glandular epithelium express any uteroglobin mRNA. Our observations on the cellular level have been continued in parallel studies on endometrial homogenates by Northern Blot analysis of uteroglobin mRNA (600 bases). Finally, it is discussed whether Uteroglobin mRNA may be an useful marker for the differentiation of various endometrial epithelial cell populations.
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PMID:Localization of uteroglobin mRNA by nonradioactive in situ hybridization in the pregnant rabbit endometrium. 830 87

To study the interplay of steroid hormones and oncogenes in the control of endometrial cell proliferation and differentiation we have generated cell lines derived from rat endometrium by expressing the immortalizing oncogenes adeno E1A or SV40 large T antigen. These lines are positive for mesenchymal markers and contain very few characteristic epithelial proteins. Cell lines expressing a temperature-sensitive mutant of SV40 T antigen exhibit a temperature-dependent morphology and growth behavior, but do not manifest an epithelial phenotype at the non-permissive temperature. Cell lines additionally infected with retroviral vectors carrying the v-Ha-ras oncogene (p21rasArg-12) no longer express collagen type III and recover part of their epithelial potential by expressing cytokeratins and/or cadherin E. Some of these cells also express characteristic decidual marker proteins such as desmin, whereas others express glandular epithelial markers such as uteroglobin. Uteroglobin mRNA levels in these cells are increased by glucocorticoids. The parental temperature-sensitive cells do not contain progesterone receptor but become positive for progesterone receptor at the permissive temperature after infection with the v-Ha-ras-expressing retrovirus. Our results indicate that there is a fluent transition and overlapping between mesenchymal, glandular epithelial and decidual phenotypes of endometrial cells, suggesting that these three cell types are derived from the same stem/precursor cells. The v-Ha-ras oncogene product appears to act on the differentiation pathway at an early step prior to the distinction between decidual and glandular epithelial lineage.
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PMID:Expression of epithelial phenotype is enhanced by v-Ha-ras in rat endometrial cells immortalized by SV40 T antigen. 839 60


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