Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P11684 (Uteroglobin)
 114 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

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

Immunochemical methods were used to analyse sex-associated differences in urinary protein 1 concentration. Spot urine from seven normal men and seven women of reproductive age was collected in four sequentially divided fractions, and protein 1 concentration in each fraction was measured by an enzyme immunoassay using the sandwich method: protein 1 values in the first of the sequential urine samples from the male subjects were remarkably high (81.4 +/- 80.4 micrograms/l; mean +/- 1 SD), but were much lower in the remaining three fractions. In females, on the other hand, protein 1 values were low (0.7 +/- 0.4 microgram/l), were uniform in all four sequential fractions, and were close to those of the last three fractions of urine from male subjects. Based on this finding, protein 1 concentration was measured in 14 specimens of seminal plasma, where concentration of protein 1 was high (1259.1 +/- 1716.5 micrograms/l; range, 201.9 to 6580.0 micrograms/l). On Western blotting, protein 1 in seminal plasma had a molecular mass of M(r) 14,000, the same as that of protein 1 purified from the urine of patients with chronic renal failure of probable plasma origin, and of concentrated male urine collected at the initiation of voiding, which is thus thought to come mainly from genital tissue. Protein 1 was found to be in high concentration (434.8 +/- 504.6 micrograms/l) in five aspirated fluids collected at the ejaculatory duct after squeezing the prostate. Three prostate tissue extracts contained protein 1 concentrations ranging from 8.6 to 50.1 micrograms/l. Protein 1 is also present in seminal vesicle fluids (7.1 +/- 2.8 micrograms/l; range, 2.3 to 9.5 micrograms/l).(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Sex-associated differences in protein 1 values in urine: immunochemical detection of protein 1 in genital tissues. 816 92

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

Uteroglobin (UG) is a hormonally regulated secretory protein produced in the lung and urogenital system of rabbits. It is homologous to rat and human Clara cell 10 kD protein (CC10); however, there are significant differences in the tissue-specific expression between these species. Mouse CC10 (mCC10) protein has been less well characterized. In this study, we cloned and sequenced the cDNA encoding the mCC10 protein. The mouse cDNA showed 90, 52, and 51% amino acid homology to rat and human CC10 and rabbit UG cDNA, respectively. The cellular and tissue-specific expression of mCC10 was examined in adult and developing mice. Endogenous mCC10 expression was compared with transgenic mice expressing a fusion gene of the rabbit 3.3 kb UG promoter linked to human growth hormone (hGH) as an easily detectable marker. Northern blot analysis detected mCC10 mRNA only in the lung. hGH mRNA was detected in the lung in levels similar to the endogenous mCC10 transcripts. However, it was also present in trace quantities in the uterus and ovary of normal adult female mice and in the epididymus of adult male mice. hGH and mCC10 proteins were identified in the trachea and lung, where they were localized to Clara cells. Ultrastructurally, hGH was present in secretory granules in the Clara cell cytoplasm and appeared to be secreted into the airways. hGH was initially detectable in 16 day gestation developing mice; however, CC10 was not detectable until the eighteenth day of gestation. We have created an attractive model for comparing the cis-acting DNA elements governing the interspecies variation in tissue-specific expression of CC10.
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PMID:Cloning and tissue-specific expression of the cDNA for the mouse Clara cell 10 kD protein: comparison of endogenous expression to rabbit uteroglobin promoter-driven transgene expression. 839 59

The present experiment was designed to investigate the mode of action of indomethacin, a prostaglandin synthesis inhibitor, as an antifertility agent, and to examine a possible effect of indomethacin administered during the normal peri-implantation period on the protein content and progesterone concentration in plasma and uterine fluid in pseudopregnant rabbits. The results showed that treatment with indomethacin significantly reduced the plasma progesterone concentrations, decreased progesterone concentrations in uterine flushing, significantly decreased the total plasma proteins, and particularly decreased albumin in the plasma and in the uterine flushings. Uteroglobin production by the rabbit uterus was not affected by this treatment. It is concluded that the antifertility effect of indomethacin at the time of implantation is exerted by reducing progesterone concentrations in plasma and uterine fluid, possibly affecting steroidogenesis, and by reducing the percentage of albumin in plasma and in uterine fluid, probably by increasing renal excretion of albumin. These effects of indomethacin provide an environment within the uterus that would not support embryo implantation and development.
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PMID:Effect of indomethacin administered during the normal time of implantation on the progesterone and protein composition of plasma and uterine flushings of rabbits. 846 21

We used immunohistochemistry and electron microscopy to evaluate the differentiation of cells comprising atypical adenomatous hyperplasia (AAH; n = 26), early bronchioloalveolar lung carcinoma (BAC; n = 11), and overt BAC (n = 16), which are assumed to constitute a continuous spectrum of developmental steps of BAC. Surfactant apoprotein (SAP), a marker for type 2 alveolar cells, was expressed in cells from all the lesions of AAH, early BAC, and overt BAC. However, the proportion of SAP-positive cells decreased and their distribution became more heterogeneous with advancing lesion grade. Urine protein 1, which is identical to the Clara cell-specific 10 kDa protein, was expressed in 70% of overt BAC, whereas only 20% of early BAC showed weak reactivity and none of AAH lesions showed any reactivity at all. Ultrastructurally, type 2 alveolar cell differentiation was predominant among cells from AAH and early BAC. Our results suggest that precursor cells of BAC differentiate predominantly towards type 2 alveolar cells. Cells comprising overt BAC retain this differentiation phenotype, but to a reduced extent. In contrast, concomitantly with progression, cells with Clara cell differentiation emerge and their proportion increases. Such phenotypic changes may reflect metaplasia occurring in tumour cells during the development of BAC.
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PMID:Cytodifferentiation of atypical adenomatous hyperplasia and bronchioloalveolar lung carcinoma: immunohistochemical and ultrastructural studies. 942 29

Uteroglobin (UG) is a steroid-inducible, multifunctional, secreted protein with antiinflammatory and antichemotactic properties. Recently, we have reported a high affinity UG-binding protein (putative receptor), on several cell types, with an apparent molecular mass of 190 kDa (Kundu, G. C., Mantile, G., Miele, L., Cordella-Miele, E., and Mukherjee, A. B. (1996) Proc. Natl. Acad. Sci. U. S. A. 93, 2915-2919). Since UG is a homodimer in which the 70 amino acid subunits are connected by two disulfide bonds, we sought to determine whether UG monomers also interact with the 190-kDa UG-binding protein and if so, whether it has the same biological activity as the dimer. Surprisingly, we discovered that in addition to the 190-kDa species, another protein, with an apparent molecular mass of 49 kDa, binds reduced UG with high affinity and specificity. Both 49- and 190-kDa proteins are readily detectable on nontransformed NIH 3T3 and some murine cancer cells (e. g. mastocytoma, sarcoma, and lymphoma), while lacking on others (e.g. fibrosarcoma). Most interestingly, pretreatment of the cells, which express the binding proteins, with reduced UG dramatically suppresses extracellular matrix (ECM) invasion, when such treatment had no effect on fibrosarcoma cells that lack the UG-binding proteins. Tissue-specific expression studies confirmed that while both 190- and 49-kDa UG-binding proteins are present in bovine heart, spleen, and the liver, only the 190-kDa protein is detectable in the trachea and in the lung. Neither the 190-kDa nor the 49-kDa protein was detectable in the aorta. Purification of these binding proteins from bovine spleen by UG-affinity chromatography and analysis by SDS-polyacrylamide gel electrophoresis followed by silver staining identified two protein bands with apparent molecular masses of 40 and 180 kDa, respectively. Treatment of the NIH 3T3 cells with specific cytokines (i.e. interleukin-6) and other agonists (i.e. lipopolysaccharide) caused a substantially increased level of 125I-UG binding but the same cells, when treated with platelet-derived growth factor, tumor necrosis factor-alpha, interferon-gamma, and phorbol 12-myristate 13-acetate, did not alter the UG binding. Taken together, these findings raise the possibility that UG, through its binding proteins, plays critical roles in the regulation of cellular motility and ECM invasion.
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PMID:Uteroglobin (UG) suppresses extracellular matrix invasion by normal and cancer cells that express the high affinity UG-binding proteins. 971 16

Uteroglobin (UG) is a multifunctional, secreted protein that has receptor-mediated functions. The human UG (hUG) gene is mapped to chromosome 11q12.2-13.1, a region frequently rearranged or deleted in many cancers. Although high levels of hUG expression are characteristic of the mucosal epithelia of many organs, hUG expression is either drastically reduced or totally absent in adenocarcinomas and in viral-transformed epithelial cells derived from the same organs. In agreement with these findings, in an ongoing study to evaluate the effects of aging on UG-knockout mice, 16/16 animals developed malignant tumors, whereas the wild-type littermates (n = 25) remained apparently healthy even after 11/2 years. In the present investigation, we sought to determine the effects of induced-expression of hUG in human cancer cells by transfecting several cell lines derived from adenocarcinomas of various organs with an hUG-cDNA construct. We demonstrate that induced hUG expression reverses at least two of the most important characteristics of the transformed phenotype (i.e., anchorage-independent growth on soft agar and extracellular matrix invasion) of only those cancer cells that also express the hUG receptor. Similarly, treatment of the nontransfected, receptor-positive adenocarcinoma cells with purified recombinant hUG yielded identical results. Taken together, these data define receptor-mediated, autocrine and paracrine pathways through which hUG reverses the transformed phenotype of cancer cells and consequently, may have tumor suppressor-like effects.
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PMID:Loss of transformed phenotype in cancer cells by overexpression of the uteroglobin gene. 1009 46

Uteroglobin is a progesterone binding protein, a member of the antiflammin gene family and possibly a novel cytokine. Initially, uteroglobin was identified as the major protein of rabbit uterine secretion during the phase of preimplantation. Counterparts of the rabbit uteroglobin or its gene are described in rat, mouse, hamster, hare, pig, horse and human. While uteroglobin appears as one of the most extensively studied proteins, particularly its physico-chemical properties, including its crystal structure and its gene, the true physiological role of this protein still remains to be unravelled. Essential to understanding the significance of human uteroglobin in reproductive organs, particularly in the endometrium, is a knowledge of the spatial and chronological expression of this secretory protein. Our studies on 115 volunteers combined reverse transcription-polymerase chain reaction (RT-PCR), immunohistochemistry and quantitative assessment by an enzyme-linked immunosorbent assay for uteroglobin. The expression, localization and release of uteroglobulin in the human endometrium are presented. Secretory uteroglobin is found in endometrial tissue homogenates in highest levels of expression during the early luteal phase (days 15-19, 340 pg/mg total protein). In turn, uteroglobin is released into the uterine lumen in peak amounts during the receptive phase of the menstrual cycle (mid-luteal phase, days 20-23, secretion level 833.4 pg/mg total protein). Our immunohistochemical studies match with these results, as uteroglobin is located during the early and mid-luteal phase in the apical compartments of endometrial gland cells. These observations strongly suggest an involvement of uteroglobin in endometrial preparations for implantation.
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PMID:Expression of uteroglobin in the human endometrium. 1058 71


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