Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.4.21.73 (urokinase-type plasminogen activator)
 10,685 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Rat endometrial stromal cells undergoing decidualization in vitro secrete urokinase-type plasminogen activator (uPA), and this secretion is regulated by prostaglandin E2. The present study was undertaken to determine whether uPA and plasminogen activator inhibitor-1 (PAI-1) mRNAs are expressed in vivo in the decidua of pregnant rats and in the deciduoma of "pseudopregnant" rats. Total RNA was prepared from nondecidualized and decidualized endometrial tissues at various stages of early pregnancy and examined by Northern blot analysis using specific cDNA probes for rat uPA and PAI-1. There was little uPA mRNA in the endometrium during the first 5 days of pregnancy (Day 1 = the presence of sperm in the vagina). A high level of uPA mRNA was detected on Day 7, and it declined thereafter. There was a gradual increase in PAI-1 mRNA in the decidua from Day 7 of pregnancy, reaching a peak level on Day 15 when the decidua was transformed into the maternal placenta. (RNA was not analyzed beyond Day 15 of pregnancy in this study.) In situ hybridization studies verified that uPA mRNA was present in the decidua adjacent to the implanting embryo on Day 7. Plasminogen activator inhibitor-1 mRNA was scattered in the decidualized endometrium, but greater amounts of PAI-1 mRNA were found in the fetal tissue on Day 10 of pregnancy. Northern blot analysis of RNA from the deciduoma produced in ovariectomized, steroid-treated rats by intrauterine injection of oil demonstrated a similar temporal pattern of expression of uPA mRNA; i.e., the level of uPA mRNA was highest on Day 7 and decreased thereafter. The level of PAI-1 mRNA in deciduoma was not detectable by Northern blot technique during the first 10 days of pseudopregnancy. These findings confirm that uPA mRNA is present in vivo in rat decidual cells, independent of the presence of a conceptus. By contrast, the level of PAI-1 mRNA in the uterus is probably influenced by the presence of the conceptus.
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PMID:Presence of urokinase plasminogen activator and plasminogen activator inhibitor-1 messenger ribonucleic acids in rat endometrium during decidualization in vivo. 886 64

We reported previously that TGF-beta 1 is a major immunosuppressive agent in human seminal plasma. TGF-beta 1 in seminal plasma is so abundant that it may represent the highest physiologic concentration of TGF-beta 1 reported for a biological fluid. The in vitro activation of TGF-beta 1 is detected at acidic pH. The acidic environment of the vagina is suggested as an in vivo physiological condition for the activation of seminal plasma latent TGF-beta 1. The present study demonstrates that Pefabloc [4-(2-aminoethyl)-benzenesulfonyl fluoride AEBSF]-inhibitable serine proteases are involved in the activation of latent TGF-beta 1. Pefabloc inhibits latent TGF-beta 1 activation in a dose- and time-dependent manner. The use of other protease inhibitors and specific antibodies reveals that, in addition to plasmin, substilisin-like endoproteases and tissue- and urokinase-type plasminogen activators participate in the activation of latent TGF-beta 1 in human seminal plasma.
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PMID:Plasmin, substilisin-like endoproteases, tissue plasminogen activator, and urokinase plasminogen activator are involved in activation of latent TGF-beta 1 in human seminal plasma. 987 32

The receptive phase of the endometrium seems to occur in close association with the appearance of pinopodes and endometrial integrins that may be activated by the interleukin-1 system (IL-1). Embryo attachment is the result of adhesion protein expression, and the invasion of the embryo is governed by proteolytic enzymes. Leukaemia inhibitory factor (LIF) is produced by natural killer lymphocytes that interact with the invading trophoblast. This may activate urokinase plasminogen activator (uPA) and gelatinase enzymes, which play a crucial role in trophoblast invasion. Oestrogen stimulates, while progesterone inhibits, LIF. The role of endometrial contractility in displacing human embryos from the Fallopian tube to the lumen cavity of the uterus or vagina in terms of pregnancy or wastage is still a matter of discussion. Endometriosis and its associated abnormal uterine contractions may be also linked to implantation failure. Unless new evidence emerges to indicate otherwise, it can be assumed that progesterone is, either in a direct (non-genomic: contractility) or indirect (genomic: decidualization) manner, the only determinant of endometrial priming necessary for embryo nidation.
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PMID:Implantation markers and endometriosis. 1627 10

The glycosylphosphatidylinositol (GPI)-anchored C4.4A was originally identified as a metastasis-associated protein by differential screening of rat pancreatic carcinoma cell lines. C4.4A is accordingly expressed in various human carcinoma lesions. Although C4.4A is a structural homolog of the urokinase receptor (uPAR), which is implicated in cancer invasion and metastasis, no function has so far been assigned to C4.4A. To assist future studies on its function in both physiological and pathophysiological conditions, the present study provide a global survey on C4.4A expression in the normal mouse by a comprehensive immunohistochemical mapping. This task was accomplished by staining paraffin-embedded tissues with a specific rabbit polyclonal anti-C4.4A antibody. In the adult mouse, C4.4A was predominantly expressed in the suprabasal layers of the squamous epithelia of the oral cavity, esophagus, non-glandular portion of the rodent stomach, anus, vagina, cornea, and skin. This epithelial confinement was particularly evident from the abrupt termination of C4.4A expression at the squamo-columnar transition zones found at the ano-rectal and utero-vaginal junctions, for example. During mouse embryogenesis, C4.4A expression first appears in the developing squamous epithelium at embryonic day 13.5. This anatomical location of C4.4A is thus concordant with a possible functional role in early differentiation of stratified squamous epithelia.
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PMID:Expression of C4.4A, a structural uPAR homolog, reflects squamous epithelial differentiation in the adult mouse and during embryogenesis. 2133 81