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

Uteroglobin (UG) or blastokinin is a steroid-dependent low molecular weight secretory protein in the rabbit. This protein has many immunomodulatory properties. Recently, UG has been reported to be a potent phospholipase A2 (E.C. 3.1.1.4) inhibitor and this property may explain, at least in part, the immunomodulatory/antiinflammatory effects of this protein. Although UG has been detected in many reproductive and non-reproductive tissues of the rabbit it has not been reported in the circulation of this animal. Here, we present biochemical and immunochemical evidence for the presence of a low molecular weight circulating protein with progesterone binding and phospholipase A2 inhibitory properties similar to rabbit uterine UG. The major organs which contribute UG-like protein in circulation seem to be the tracheobronchial tree and to a lesser extent the uterus. The concentration of this protein is much higher in the vicinity of these organs as compared to peripheral circulation. Phospholipase A2 (PLA2)-catalyzed reaction is the major pathway of arachidonic acid production from cell membrane phospholipids. Arachidonic acid participates in the stimulation of guanylate cyclase, adenylate cyclase, protein kinase C and release of calcium from intracellular stores. These processes are thought to be involved in cellular signal transduction. Arachidonic acid is also essential for eicosanoid synthesis and many eicosanoids (e.g. prostaglandins, leukotrienes, etc.) are proinflammatory. Thus, the UG-like protein by inhibiting PLA2 may play a vital role in the regulation of cellular signal transduction, control of inflammation and platelet aggregation.
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PMID:Detection of a uteroglobin-like phospholipase A2 inhibitory protein in the circulation of rabbits. 274 26

Uteroglobin is a steroid hormone dependent, low molecular weight, secretory protein with many immunomodulatory properties. Immunomodulation by this protein may, at least in part, be related to its inhibitory effects on phospholipase A2 activity. Although uteroglobin is conclusively found in the rabbit, its presence in the human is controversial. Here, we present biochemical and immunological evidence for the detection of a uteroglobin-like protein in the wet epithelial living of the respiratory tract of human neonates. Because inhibition of phospholipase A2 may modulate tissue eicosanoid levels and since many eicosanoids (i.e. prostaglandins and leukotrienes etc.) are well known regulators of smooth muscle contractility, cellular migration and inflammatory processes, the discovery of this protein in the human respiratory tract may have important physiological implications.
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PMID:Detection of a rabbit uteroglobin-like protein in human neonatal tracheobronchial washings. 328 98

Uteroglobin, the primary secretory protein of rabbit uterine epithelium, was localized by the direct immunoperoxidase method in uteri of control ovariectomized rabbits and of ovariectomized rabbits injected with progesterone or estradiol-17 beta. In control rabbits, staining for uteroglobin was almost entirely abolished six weeks after bilateral ovariectomy. Two days following progesterone injection of ovariectomized rabbits, intense staining for uteroglobin could be detected within the endoplasmic reticulum, Golgi complexes, and compact secretory vesicles of most endometrial epithelial cells. Estradiol-17 beta injection resulted in a different intracellular pattern of uteroglobin distribution. Two days following treatment with that steroid hormone, intense staining for uteroglobin was localized within large apical mucous droplets and moderate staining was present in the endoplasmic reticulum and Golgi complexes of these cells. The increased mucin content of the endometrial epithelium following treatment with estradiol-17 beta was confirmed by a periodic acid-Schiff histochemical reaction in the presence of diastase. Quantitation by radioimmunoassay of uteroglobin production in vitro by uterine fragment confirmed that progesterone had a greater effect on enhancing uteroglobin production than estradiol-17 beta and that both steroid hormones did not have any effect after 30 min of incubation in vitro. We suggest that progesterone not only regulates uteroglobin production at the transcriptional level, but that it also regulates the mode of uteroglobin secretion by the induction of a different pathway, compared with the one used when estradiol-17 beta is administered alone.
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PMID:Estradiol-17 beta and progesterone regulate secretion of uteroglobin through different pathways. 330 31

Uteroglobin, a secretory protein of rabbit uterine epithelium, was localized by the direct immunoperoxidase method in control and hCG-induced pseudopregnant rabbits. In control rabbits, uteroglobin was confined to the apical cytoplasm of nearly all cells of the endometrial epithelium. The induction of pseudopregnancy resulted in a pronounced continuing increase, through 4 days post-hCG administration, in the absolute number of epithelial cells engaged in uteroglobin synthesis. Furthermore, the endoplasmic reticulum was more intensely stained for uteroglobin than in the epithelial cells of control rabbit endometrium. Thus, the increased production of uteroglobin, in response to hormonal stimulation, appears to be achieved both through an increase in the amount of uteroglobin synthesized by a given cell as well as by an increase in the number of cells involved in uteroglobin synthesis. Concurrent with the increase in the number of cells synthesizing uteroglobin, an increase in the number of unstained cells first appeared at the second day of pseudopregnancy, during the period of maximal epithelial proliferation. However, within those cells containing uteroglobin on the second day following injection with hCG, most staining was limited to the perinuclear membrane. At various times following hCG administration, a number of scattered cells, intensely stained for uteroglobin, were observed in the uterine epithelium. Based upon ultrastructural studies, failure to exclude trypan blue, and the presence of intra-mitochondrial uteroglobin, they were identified as either dead or dying cells.
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PMID:Uteroglobin production in the pseudopregnant rabbit uterus. Immunohistochemical studies. 332 45

Uteroglobin, a steroid-dependent secretory protein first discovered in the rabbit uterus during early pregnancy, is a potent phospholipase A2 inhibitor. We found that uteroglobin also inhibited human and rabbit phagocyte chemotaxis in response to formyl peptide attractants in a dose-dependent manner. Half-maximal inhibition was at 1.2 microM. Uteroglobin did not compete with a formyl peptide for its receptor but inhibited internalization of radiolabeled formyl peptide. Uteroglobin appears to inhibit chemotaxis by a mechanism different from that of dansylcadaverine, a well studied inhibitor of endocytosis. Unlike dansylcadaverine, uteroglobin did not have any effect upon the synthesis of phosphatidylcholine or phosphatidylinositol. It is suggested that uteroglobin may protect trophoblastic cells from the defense system of the host not only by binding to antigenic determinants of embryonic cells but also by impairing migration of phagocytes, one of the primary components of the immune defense system. These results may explain why embryonic cells do not elicit an inflammatory response in the uterine endometrium during pregnancy.
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PMID:Inhibition of phagocyte chemotaxis by uteroglobin, an inhibitor of blastocyst rejection. 333 40

Uteroglobin (UG) is a secretory protein produced by the rabbit endometrium and its production is increased during cell differentiation which occurs during early pregnancy or pseudopregnancy. In the present study, the optimal conditions for UG production by rabbit endometrial epithelial cells in culture were examined. Metabolic labeling studies showed the incorporation of [35S]methionine into UG molecules by the endometrial epithelial cells in culture. Accumulation of UG in culture media was linear for at least a period of 24 h. These cells do not catabolize exogenously added radiolabeled UG. Endometrial cells obtained from virgin female rabbits at different times after the administration of human CG (hCG) and put in culture were found to make different amounts of UG. The maximal UG production was found in cells taken from pseudopregnant rabbits 4 days after hCG administration. Cycloheximide (28 micrograms/ml) inhibited the production of UG by the cells in culture whereas actinomycin-D (5 micrograms/ml) and cordycipin (50 micrograms/ml) increased its production. Inhibition of DNA synthesis by hydroxyurea (10(-3) M) did not affect the UG production. The production of UG was significantly less when cells were cultured on attached or floating collagen gels as compared to cells grown on plastic Petri dishes. The amino acid content of Ham's F-12 medium was shown to be adequate for maximal UG production; lowering this amino acid concentration decreased the amount of UG accumulated in the medium over a 24-h period. Increasint the number of cultured cells per dish resulted in an increased UG production per cell.
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PMID:Uteroglobin production by cultured rabbit uterine epithelial cells. 683 58

Uteroglobin (UG) is a potent immunomodulatory and antiinflammatory secretory protein with high levels detected in human prostate tissue. We used three human prostate cancer cell lines (DU-145, PC3-M, and LNCaP) to test the hypothesis that UG may modulate invasiveness of prostatic carcinoma cells in the Boyden chamber assay for invasion through a reconstituted basement membrane preparation. Fibroblast-conditioned medium was used as the chemoattractant. The most invasive cell line was DU-145, followed by PC3-M, whereas the androgen-dependent LNCaP cell line exhibited extremely low invasive potential. Pretreatment of DU-145 and PC3-M cells for 24 h with 0.01, 0.1, or 1.0 microM recombinant UG had no effect on basal invasiveness but inhibited fibroblast-conditioned medium-stimulated invasion in a dose-dependent manner, reaching up to 60.2 and 87.9% inhibition of DU-145 and PC3-M, respectively. UG had no effect on either cell-reconstituted basement membrane adhesion or simple chemotaxis in the absence of reconstituted basement membrane. UG also strongly inhibited the biphasic release of [14C]-labeled arachidonic acid from fibroblast-conditioned medium-stimulated DU-145 cells. These results suggest that UG may modulate prostate tumor cell invasiveness and that the mechanism may include inhibition of the arachidonic acid signal cascade.
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PMID:Recombinant human uteroglobin inhibits the in vitro invasiveness of human metastatic prostate tumor cells and the release of arachidonic acid stimulated by fibroblast-conditioned medium. 803 85

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

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

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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