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Gene Review

PLAU  -  plasminogen activator, urokinase

Sus scrofa

 
 
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Disease relevance of PLAU

 

High impact information on PLAU

  • Plasminogen activator (PA) production in LLC-PK1 pig kidney cell culture is induced to high levels by calcitonin and vasopressin, both of which stimulate adenylate cyclase, or by other compounds that also raise intracellular cAMP levels [5].
  • Pretreatment with high concentrations of cycloheximide did not block calcitonin-induced PA-mRNA synthesis, indicating that PA gene activation was a primary transcriptional result of calcitonin stimulation and did not require new protein synthesis [5].
  • We tested this hypothesis by measuring PA-mRNA sequences in the Xenopus oocyte translation system which showed a 15-20-fold enhanced PA-synthesizing capacity when supplied with poly(A)+RNA from induced cells, above that obtained from uninduced cell RNA [5].
  • Secretion of a progesterone-induced inhibitor of plasminogen activator by the porcine uterus [6].
  • The increase in PA production, but not morphological change, depended on genetic transcription and translation, being inhibited by actinomycin and/or cycloheximide [7].
 

Chemical compound and disease context of PLAU

 

Biological context of PLAU

 

Anatomical context of PLAU

 

Associations of PLAU with chemical compounds

 

Physical interactions of PLAU

 

Regulatory relationships of PLAU

 

Other interactions of PLAU

 

Analytical, diagnostic and therapeutic context of PLAU

  • The rapidity and sensitivity of the plasminogen activator determination and other cellular responses may make it possible in the future to use this cell stain in a convenient bioassay for calcitonins and their analogues [16].
  • Using biosynthetic labeling of proteins with 35S-methionine, immunoprecipitation and sodium dodecyl sulfate-polyacrylamide gel electrophoresis, we showed that sinusoidal endothelial cells produce and secrete plasminogen activator inhibitor type 1 from the beginning of culture [27].
  • However, in the culture medium of platelet-treated aortic EC, a new lysis band of 92 kDa appeared with no associated amidolytic activity suggesting that the 48 kDa plasminogen activator secreted by the aortic EC after treatment with platelets is complexed to the inhibitor PAI1 [31].
  • Tissue plasminogen activator activity, however, increased only in the 60-min SC AXC group during clamping (P =.02), and 5 minutes (P =.05) and 30 minutes (P =.06) after unclamping, compared with both control groups [32].
  • Western blot analysis suggested that follicular PA activity was represented principally by two forms of tissue type PA (t-PA) each with a pI of 7.8 and with molecular masses of 72,000 and 78,000 daltons, respectively [33].

References

  1. Evaluation of epithelial tissue plasminogen activator as a thrombolytic agent in a rabbit model of venous thrombosis. Electricwala, A., Emeis, J.J., Atkinson, T. J. Pharmacol. Exp. Ther. (1986) [Pubmed]
  2. Prevention of adult respiratory distress syndrome with plasminogen activator in pigs. Hardaway, R.M., Williams, C.H., Marvasti, M., Farias, M., Tseng, A., Pinon, I., Yanez, D., Martinez, M., Navar, J. Crit. Care Med. (1990) [Pubmed]
  3. Relationship between release of plasminogen activator and estrogen by blastocysts and secretion of plasmin inhibitor by uterine endometrium in the pregnant pig. Fazleabas, A.T., Geisert, R.D., Bazer, F.W., Roberts, R.M. Biol. Reprod. (1983) [Pubmed]
  4. Fibrinolysis therapy achieved with tissue plasminogen activator and aspiration of the liquefied clot after experimental intracerebral hemorrhage: rapid reduction in hematoma volume but intensification of delayed edema formation. Rohde, V., Rohde, I., Thiex, R., Ince, A., Jung, A., Dückers, G., Gröschel, K., Röttger, C., Küker, W., Müller, H.D., Gilsbach, J.M. J. Neurosurg. (2002) [Pubmed]
  5. Hormonal regulation of plasminogen activator mRNA production in porcine kidney cells. Nagamine, Y., Sudol, M., Reich, E. Cell (1983) [Pubmed]
  6. Secretion of a progesterone-induced inhibitor of plasminogen activator by the porcine uterus. Mullins, D.E., Bazer, F.W., Roberts, R.M. Cell (1980) [Pubmed]
  7. Induction of plasminogen activator synthesis by antibodies. Becker, D., Ossowski, L., Reich, E. J. Exp. Med. (1981) [Pubmed]
  8. Latex D-dimer signal in in situ femoral vein thrombus in swine and effect of minidose exogenous tissue plasminogen activator bolus. Robinson, V.J., Pineda, G.E., Salah, A.K., Pipkin, W.L., Corley, J.H., Jonah, M.H., Gossage, J.R. Chest (2005) [Pubmed]
  9. Effects of hypoxia and acidosis on vascular plasminogen activator release in the pig ear perfusion system. Tappy, L., Hauert, J., Bachmann, F. Thromb. Res. (1984) [Pubmed]
  10. cDNA and gene nucleotide sequence of porcine plasminogen activator. Nagamine, Y., Pearson, D., Altus, M.S., Reich, E. Nucleic Acids Res. (1984) [Pubmed]
  11. Plasminogen activator, fibronectin, lymphotoxin sensitivity, and natural skin reactivity relationships to guinea pig cell tumorigenicity. McCabe, R.P., Evans, C.H. J. Natl. Cancer Inst. (1982) [Pubmed]
  12. A new genetic approach for studying hormonal regulation of urokinase-type plasminogen activator gene expression in LLC-PK1 cells. Hofstetter, P., Kikinis, Z., Altus, M.S., Pearson, D., Nagamine, Y. Mol. Cell. Biol. (1987) [Pubmed]
  13. Role of tissue-specific transcription factor LFB3 in a cyclic AMP-responsive enhancer of the urokinase-type plasminogen activator gene in LLC-PK1 cells. Soubt, M.K., Marksitzer, R., Menoud, P.A., Nagamine, Y. Mol. Cell. Biol. (1998) [Pubmed]
  14. The distal hinge of the reactive site loop and its proximity: a target to modulate plasminogen activator inhibitor-1 activity. Bijnens, A.P., Gils, A., Stassen, J.M., Komissarov, A.A., Knockaert, I., Brouwers, E., Shore, J.D., Declerck, P.J. J. Biol. Chem. (2001) [Pubmed]
  15. Biochemical actions of glucocorticoids on macrophages in culture. Specific inhibition of elastase, collagenase, and plasminogen activator secretion and effects on other metabolic functions. Werb, Z. J. Exp. Med. (1978) [Pubmed]
  16. Calcitonin stimulates plasminogen activator in porcine renal tubular cells: LLC-PK1. Dayer, J.M., Vassalli, J.D., Bobbitt, J.L., Hull, R.N., Reich, E., Krane, S.M. J. Cell Biol. (1981) [Pubmed]
  17. Mr 25,000 heparin-binding protein from guinea pig brain is a high molecular weight form of basic fibroblast growth factor. Moscatelli, D., Joseph-Silverstein, J., Manejias, R., Rifkin, D.B. Proc. Natl. Acad. Sci. U.S.A. (1987) [Pubmed]
  18. Generation of macrophage migration inhibitory activity by plasminogen activators. Roblin, R.O., Hammond, M.E., Bensky, N.D., Dvorak, A.M., Dvorak, H.F., Black, P.H. Proc. Natl. Acad. Sci. U.S.A. (1977) [Pubmed]
  19. Cryptic and active plasminogen activators secreted by line 10 tumor cells in culture. Orenstein, N.S., Buczynski, A., Dvorak, H.F. Cancer Res. (1983) [Pubmed]
  20. Recombinant soluble form of PSGL-1 accelerates thrombolysis and prevents reocclusion in a porcine model. Kumar, A., Villani, M.P., Patel, U.K., Keith, J.C., Schaub, R.G. Circulation (1999) [Pubmed]
  21. Interleukin-1 beta and interleukin-1 alpha stimulate the plasminogen activator activity and prostaglandin E2 levels of human synovial cells. Leizer, T., Clarris, B.J., Ash, P.E., van Damme, J., Saklatvala, J., Hamilton, J.A. Arthritis Rheum. (1987) [Pubmed]
  22. Leydig cell and extracellular matrix effects on Sertoli cell function: biochemical and morphologic studies. Reventos, J., Perrard-Sapori, M.H., Chatelain, P.G., Saez, J.M. J. Androl. (1989) [Pubmed]
  23. In vitro regulation of pig Sertoli cell growth and function: effects of fibroblast growth factor and somatomedin-C. Jaillard, C., Chatelain, P.G., Saez, J.M. Biol. Reprod. (1987) [Pubmed]
  24. In vitro interactions between Sertoli cells and steroidogenic cells. Perrard-Sapori, M.H., Chatelain, P., Vallier, P., Saez, J.M. Biochem. Biophys. Res. Commun. (1986) [Pubmed]
  25. Enhanced stability of urokinase-type plasminogen activator mRNA in metastatic breast cancer MDA-MB-231 cells and LLC-PK1 cells down-regulated for protein kinase C--correlation with cytoplasmic heterogeneous nuclear ribonucleoprotein C. Nanbu, R., Montero, L., D'Orazio, D., Nagamine, Y. Eur. J. Biochem. (1997) [Pubmed]
  26. Somatomedin-C/insulin-like growth factor 1: a differentiating factor of testicular function. Chatelain, P., Perrard-Sapori, M.H., Jaillard, C., Naville, D., Ruitton, A., Saez, J. International journal of radiation applications and instrumentation. Part B, Nuclear medicine and biology. (1987) [Pubmed]
  27. Contribution of sinusoidal endothelial liver cells to liver fibrosis: expression of transforming growth factor-beta 1 receptors and modulation of plasmin-generating enzymes by transforming growth factor-beta 1. Rieder, H., Armbrust, T., Meyer zum Büschenfelde, K.H., Ramadori, G. Hepatology (1993) [Pubmed]
  28. Ca2+ potentiates cAMP-dependent expression of urokinase-type plasminogen activator gene through a calmodulin- and protein kinase C-independent mechanism. Ziegler, A., Hagmann, J., Kiefer, B., Nagamine, Y. J. Biol. Chem. (1990) [Pubmed]
  29. Platelet plasminogen activator inhibitor: purification and characterization of interaction with plasminogen activators and activated protein C. Fay, W.P., Owen, W.G. Biochemistry (1989) [Pubmed]
  30. Keratinocyte growth factor stimulation of gelatinase (matrix metalloproteinase-9) and plasminogen activator in histiotypic epithelial cell culture. Putnins, E.E., Firth, J.D., Uitto, V.J. J. Invest. Dermatol. (1995) [Pubmed]
  31. Modulation of endothelial cells fibrinolytic activity by platelets. Menashi, S., He, L., Soria, C., Soria, J., Thomaidis, A., Legrand, Y. Thromb. Haemost. (1991) [Pubmed]
  32. Activation of fibrinolytic pathways is associated with duration of supraceliac aortic cross-clamping. Haithcock, B.E., Shepard, A.D., Raman, S.B., Conrad, M.F., Pandurangi, K., Fanous, N.H. J. Vasc. Surg. (2004) [Pubmed]
  33. Changes in and partial identification of the plasminogen activator and plasminogen activator inhibitor systems during ovarian follicular maturation in the pig. Politis, I., Srikandakumar, A., Turner, J.D., Tsang, B.K., Ainsworth, L., Downey, B.R. Biol. Reprod. (1990) [Pubmed]
 
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