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

Uteroglobin(utg) is a potent phospholipase A2 inhibitor but is genetically distinct from lipocortins. The purpose of the present investigation was to biochemically and immunologically characterize the utg-like antigen from rabbit plasma and serum that were found to be highly positive by radioimmunoassay(RIA). The RIA standard curve of pure rabbit utg from the uterus is compared with utg-like protein in circulation, and the curves are parallel to each other. Concerning the western blot of utg-like protein as compared with utg standard, it is clear that there is a distinct protein band corresponding to the two monomers of utg(7 kDa). Moreover, the rise in endometrial utg synthesis that occurs upon progesterone(P) treatment in rabbits is paralleled by a dramatic decrease in endometrial PGE2, PGF2 alpha levels. The level of utg-like protein in circulation increased the level of this protein approximately three-fold in the serum (70 ng/ml without Pvs 216 ng/ml with P), whereas dexamethasone(Dex) increased it two-fold. To determine the source of this protein in circulation, we cannulated the uterine and the pulmonary veins of rabbits primed with different steroids. The levels of utg-like protein in the uterine venous plasma versus peripheral venous plasma were as follows: 379 ng/ml vs 216 ng/ml, treated P. The pulmonary venous plasma was compared with the peripheral venous samples (1240 ng/ml vs 127 ng/ml, treated Dex). The results of the present study indicate that utg-like protein is detectable in the circulation of the rabbit.
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PMID:[Uteroglobin: a phospholipase A2 inhibitory protein in rabbit blood]. 279 60

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

The effect of the synthetic steroid ZK 98.734, an anti-progesterone with high affinity for the progesterone receptor, on uteroglobin distribution in the rabbit endometrium has been studied by means of immunocytochemistry. Rabbits were treated with ZK 98.734 during the second, third and fourth day of pseudopregnancy. From the fifth up to the eighth day of pseudopregnancy the uteri were processed for immunocytochemistry using the peroxidase--antiperoxidase (PAP) and protein A--gold techniques. Uteroglobin synthesis and release could be inhibited by the anti-progesterone treatment. On day 5 and 6 there was no labelling of the uterine secretions and only a few diffusely labelled non-ciliated cells could be seen in the surface and glandular epithelium. The inhibition was reversible in so far as on day 7 and day 8 the rabbit endometrium exhibits a clear labelling of the uterine secretion as well as an increase in positive reaction in the epithelial cells lining the glands. In all treated animals the intracellular uteroglobin labelling was confined to the Golgi complex and secretory vesicles with a significant increase from the fifth to the eighth day of pseudopregnancy. Together with the described morphological changes these results indicate that ZK 98.734 is capable of inducing a delayed secretion in the rabbit endometrium, which is comparable to the delay in secretion caused by post-coital oestradiol treatment. However, the antigestagen effect is probably due to a different mechanism of endocrine interference with pre-implantation. The most exciting consequence, so far, is the prolongation of progesterone action after the anti-progesterone treatment had ended.
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PMID:Distribution of uteroglobin in the rabbit endometrium after treatment with an anti-progesterone (ZK 98.734): an immunocytochemical study. 354 57

The structure of uteroglobin, a progesterone binding protein from rabbit uterine fluid, was determined and refined at 1.34 A resolution to a conventional R-factor of 0.229. The accuracy of the co-ordinates is estimated to be 0.15 A. The isotropic temperature factor of individual atoms was refined and its average value is 11.9 A2 for the 548 non-hydrogen atoms of the protein monomer. A total of 83 water molecules was located in difference electron density maps and refined, first using a constant occupancy factor of 1 and then variable occupancy, the final (Q) being 0.63. The mean temperature factor of the water oxygen atoms is 26.4 A2. Uteroglobin is a dimer and its secondary structure consists of four alpha-helices per monomer that align in an anti-parallel fashion. There is one beta-turn between helix 2 and helix 3 (Lys26 to Glu29); 76% of the residues are part of the alpha-helices. In the core of the dimeric protein molecule, between the two monomers that are held together by two disulfide bridges, we have observed a closed cavity. Its length is 15.6 A and its width is 9 A; 14 water molecules could be positioned inside. In the "bottom" part of the protein, near the C terminus, we have observed a smaller cavity, occupied by two water molecules. The calculation of the molecular surface revealed four surface pockets whose possible functional implications are discussed below.
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PMID:Refinement of the C222(1) crystal form of oxidized uteroglobin at 1.34 A resolution. 365 5

Ovulation was induced in rabbits between Days 14 and 18 of pseudopregnancy by an intravenous injection of hCG. Induction of ovulation from Day 16 onwards led to normal progestational endometrial transformation. In rabbits injected on Day 14 or 15, a normal preimplantation endometrial morphology developed, but not earlier than 7 days after hCG (Day 14/15 + 7). Uteroglobin secretion was advanced during the second pseudopregnancy. After mating or artificial insemination, fertility was greatest on Day 18 of pseudopregnancy. Conception failed on Day 14 and embryo transfers were unsuccessful on Day 14 + 1. Transfers performed on Day 14 + 3, however, led to implantation and offspring, even though endometrial morphology did not correspond to the normal Day 3 preimplantational morphology at the time of transfer. We conclude that endometrial transformation typical of normal pseudopregnancy can be induced by ovulation during the regeneration phase of pseudopregnancy from Day 16 onwards; fertilization and implantation can be achieved as early as Day 15 of pseudopregnancy; an oestrous period with high mating activity and fertility occurs about 3 days later; and Day 14 after hCG represents a limited time of functional change from pseudopregnancy to a fertile uterine cycle in the rabbit.
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PMID:Transformation of endometrium and fertility in late stages of pseudopregnancy in the rabbit. 380 13

Uteroglobin, a steroid-dependent, small molecular weight (15K) protein in the rabbit, inhibited thrombin-induced aggregation of both rabbit and human gel-filtered platelets (GFP). GFP aggregation by arachidonic acid was not affected by uteroglobin. There were no effects of uteroglobin on thrombin-induced clotting of plasma or purified fibrinogen, or inhibition of thrombin by antithrombin III. Additionally, preliminary results suggest that uteroglobin does not interfere with binding of thrombin to platelets. We suggest that inhibition of platelet aggregation by uteroglobin may function in preventing thrombosis and ensuring free flow of blood through the microvasculature of the uterus and the placenta and may induce some of the antimotility effects of progesterone on the uterus.
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PMID:Inhibition of thrombin-induced platelet aggregation by uteroglobin. 382 55

Uteroglobin, the progesterone dependent pregnancy-characteristic endometrial protein in the rabbit, is found within the endometrial epithelium on the fourth and sixth day of pregnancy at the electron-microscopic level by use of the immunoperoxidase technique and a specific anti-uteroglobin serum from the sheep. As known from earlier studies, uteroglobin is the predominant protein synthesized of the endometrial secretion. In the present study, it is localized exclusively in the non-ciliated epithelial cells. A common route of secretory proteins within these cells is observed by uteroglobin labelling: rough endoplasmatic reticulum----Golgi complex----condensing vesicles----secretory products. Uteroglobin occurs in small vesicles on the trans-face of the Golgi complex, and in addition beneath the apical plasma membrane where it appears in membrane-bound vesicles, which apparently are extruded into the uterine lumen. Most of the uteroglobin is located in the luminal secretion. The distribution of intracellular uteroglobin is found only in cells of the basal endometrial gland, adjacent to the myometrium. The cytoplasm of uterine epithelial cells facing the cavum does not show uteroglobin reaction products.
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PMID:Immunocytochemical localization of uteroglobin in the rabbit endometrium. 390 21


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