Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.4.21.7 (plasmin)
 9,023 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The isolation and characterization of placemental protein PP5 is described. The purification was achieved by use of immunoadsorbents. From the tissue of one human term placenta an average amount of 15 mg PP5 can be extracted. PP5 apparently is specific for the placenta; it could not be detected in extracts from other human tissues. In sera from pregnant women PP5 is not present or only in trace amounts (less than 0.1 mg%). In the ultracentrifuge PP5 was found to have a sedimentation coefficient of 2.8 S and a molecular weight of 36,600 daltons. Electrophoretically the protein migrates as a fast beta1-globulin. The isoelectric point was determined to be 4.6. PP5 is a glycoprotein and contains 19.8% carbohydrates (hexoses 10.0%, hexosamine 4.4%, fucose 0.4%, sialic acid 5.0%). The amino acid composition of the protein is reported, too. PP5 was found to inhibit the activity of trypsin and plasmin; the biological role of this protein therefore may be the inhibition of proteases.
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PMID:[Isolation and characterization of the placental protein pp5 (author's transl)]. 57 96

A number of proteins previously thought to be specific for the placenta or pregnancy have been identified in the fluids bathing both the oocyte and the sperm. In many cases their concentrations in follicular fluid and seminal plasma greatly exceeded those in the serum of nonpregnant women or men, and sometimes they even exceeded the levels in pregnancy sera. We report here the occurrence of PP5, PP12, PP14 and PAPP-A in follicular fluid and seminal plasma. In follicular fluid, the levels of PP5, PP12, and PAPP-A correlate with the estrogen concentration of the same fluid, and the PP12 and PAPP-A levels also bear a positive correlation to the progesterone concentration. The levels of PP12 and PAPP-A increase as the follicle grows, as do the levels of many steroid hormones. Therefore, the apparent correlations observed may be merely coincidental. However, circumstantial evidence from other reproductive organs indicates that the synthesis of PP12 and PAPP-A is stimulated by progesterone. Results of immunohistochemical staining show that PP12 and PAPP-A are localized in the luteinized granulosa cells and the corpus luteum. Previous studies indicate that PP5 and PAPP-A inhibit the action of proteolytic enzymes plasmin and elastase, which are believed to be involved in the mechanisms of ovulation. The study of the significance of these various placental proteins for human reproduction is only at its beginning. Clearly, elucidation of their function is the key to a more fundamental understanding of their role in the events governing ovulation and implantation.
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PMID:Pregnancy proteins in seminal plasma, seminal vesicles, preovulatory follicular fluid, and ovary. 389 67

Human tissue factor pathway inhibitor-2 (TFPI-2), also known as placental protein (PP5) and matrix-associated serine protease inhibitor (MSPI), is a 32-kDa extracellular matrix (ECM) protein consisting of three tandomly arranged Kunitz-type domains that inhibits plasmin, trypsin, chymotrypsin, cathepsin G and plasma kallikrein but not urokinase and tissue-type plasminogen activators or thrombin. Earlier studies in our laboratory revealed that the production of TFPI-2 is reduced or absent during the tumor progression of human gliomas. In the present study, we investigated the role of TFPI-2 in the invasiveness of the amelanotic melanoma cell line C-32. We stably transfected C-32 cells with a vector capable of expressing TFPI-2 in a sense orientation (0.7 kb). TFPI-2 protein production was then determined by western blotting and the mRNA level by northern blotting in parental and stably transfected (vector and sense) clones. The levels of TFPI-2 protein and mRNA were significantly higher in the sense clones, but neither was detected in parental and vector control clones. In addition, in vitro Matrigel invasion/migration assays revealed that the invasive behavior of sense clones was inhibited compared with the behavior of parental and vector clones. This is the first study to show that the upregulation of TFPI-2 plays a significant role in reducing the invasive behavior of human amelanotic melanomas.
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PMID:Role of tissue factor pathway inhibitor-2 (TFPI-2) in amelanotic melanoma (C-32) invasion. 1144 60