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PLAUR  -  plasminogen activator, urokinase receptor

Bos taurus

 
 
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High impact information on PLAUR

  • In addition to its role in lysosome biogenesis, the CI-MPR interacts with a number of different extracellular ligands at the cell surface, including latent transforming growth factor-beta, insulin-like growth factor-II, plasminogen, and urokinase-type plasminogen activator receptor (uPAR), to regulate cell growth and motility [1].
  • The three domains, which exhibit similar topology to each other and to the 46 kDa cation-dependent mannose 6-phosphate receptor, assemble into a compact structure with the uPAR/plasminogen and the carbohydrate-binding sites situated on opposite faces of the molecule [1].
  • Treatment of cells with phosphatidylinositol-specific phospholipase C, which cleaves glycosylphosphatidylinositol-linked proteins from the cell surface, blocked the uPA-induced tyrosine phosphorylation of FAK, indicating the requirement of an intact uPAR on the cell surface [2].
  • Although occupancy of the uPA receptor (uPAR) has been shown to alter cellular function and to induce gene expression, the signaling mechanism has not been characterized [2].
  • Taken together, these findings demonstrate that VEGF-induced angiogenesis is accompanied by increased uPAR expression and uPA activity on the endothelial cell surface [3].
 

Biological context of PLAUR

 

Anatomical context of PLAUR

  • Thrombin and other mitogens regulate the expression of the urokinase-type plasminogen activator receptor (uPAR) protein and mRNA levels in bovine vascular smooth muscle cells (SMC) [7].
  • Thus, PKC plays a role in the modulation of u-PA and u-PAR by PMA in bovine neutrophils [5].
 

Associations of PLAUR with chemical compounds

  • In REC, captopril upregulated the pro-survival proteins mortalin-2, uPA, and uPAR while downregulating the anti-growth sprouty-4 and tPA [8].
  • OBJECTIVE: To determine the effect of vitamin E supplementation on urokinase-plasminogen activator (u-PA) receptor (u-PAR) expression by neutrophils of dairy cows [9].
 

Other interactions of PLAUR

References

  1. Structure of uPAR, plasminogen, and sugar-binding sites of the 300 kDa mannose 6-phosphate receptor. Olson, L.J., Yammani, R.D., Dahms, N.M., Kim, J.J. EMBO J. (2004) [Pubmed]
  2. The urokinase-type plasminogen activator receptor mediates tyrosine phosphorylation of focal adhesion proteins and activation of mitogen-activated protein kinase in cultured endothelial cells. Tang, H., Kerins, D.M., Hao, Q., Inagami, T., Vaughan, D.E. J. Biol. Chem. (1998) [Pubmed]
  3. Vascular endothelial growth factor increases urokinase receptor expression in vascular endothelial cells. Mandriota, S.J., Seghezzi, G., Vassalli, J.D., Ferrara, N., Wasi, S., Mazzieri, R., Mignatti, P., Pepper, M.S. J. Biol. Chem. (1995) [Pubmed]
  4. VEGF-induced paracellular permeability in cultured endothelial cells involves urokinase and its receptor. Behzadian, M.A., Windsor, L.J., Ghaly, N., Liou, G., Tsai, N.T., Caldwell, R.B. FASEB J. (2003) [Pubmed]
  5. Expression of urokinase plasminogen activator receptor in resting and activated bovine neutrophils. Politis, I., Zavizjon, B., Cheli, F., Baldi, A. J. Dairy Res. (2002) [Pubmed]
  6. Vascular smooth muscle cell migration mediated by thrombin and urokinase receptor. Noda-Heiny, H., Sobel, B.E. Am. J. Physiol. (1995) [Pubmed]
  7. Mitogen crosstalk accompanying urokinase receptor expression in stimulated vascular smooth muscle cells. Reuning, U., Dixon, E.P., Little, S.P., Bang, N.U. FEBS Lett. (1996) [Pubmed]
  8. ACE inhibition actively promotes cell survival by altering gene expression. Hamdi, H.K., Castellon, R. Biochem. Biophys. Res. Commun. (2003) [Pubmed]
  9. Effects of vitamin E on urokinase-plasminogen activator receptor expression by bovine neutrophils. Politis, I., Hidiroglou, N., Cheli, F., Baldi, A. Am. J. Vet. Res. (2001) [Pubmed]
  10. Gonadotropin surge-induced up-regulation of the plasminogen activators (tissue plasminogen activator and urokinase plasminogen activator) and the urokinase plasminogen activator receptor within bovine periovulatory follicular and luteal tissue. Dow, M.P., Bakke, L.J., Cassar, C.A., Peters, M.W., Pursley, J.R., Smith, G.W. Biol. Reprod. (2002) [Pubmed]
 
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