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Gene Review

Serpine2  -  serine (or cysteine) peptidase inhibitor,...

Mus musculus

Synonyms: B230326M24Rik, GDN, Glia-derived nexin, PAI-1, PI-7, ...
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Disease relevance of Serpine2

  • The glomerular expression of PN-1 was substantially enhanced not only in lupus-like glomerulonephritis (induced by IgG3 monoclonal rheumatoid factors or occurring spontaneously in lupus-prone mice), but also in mild glomerular lesions associated with intracapillary thrombi induced by IgG3 anti-trinitrophenyl monoclonal antibodies [1].
  • These results suggest that thrombin may be involved in the progression of muscular dystrophy or the regeneration of muscle fibers after the onset of the disease and that the reduced level of PN-1 may enhance the activities stimulate the activities of muscle proteases, including dystrypsin, at a preclinical stage in mdx mice [2].
  • Since the experiments were planned in order to exclude the presence of protease-nexin in the incubation medium, these data suggest the existence of a plasminogen-independent novel receptor for the catalytic site of plasminogen activators, the number on the cell surface of which decreases in Rous sarcoma virus-transformed mouse fibroblasts [3].
  • Neurite outgrowth activity of protease nexin-1 on neuroblastoma cells requires thrombin inhibition [4].

Psychiatry related information on Serpine2

  • Absence of PN-1 results in altered semen protein composition, which leads to inadequate semen coagulation and deficient vaginal plug formation upon copulation [5].

High impact information on Serpine2


Biological context of Serpine2


Anatomical context of Serpine2

  • Consistent with these findings, abnormal PN-1 expression was found in the semen of men displaying seminal dysfunction [5].
  • In the embryonic spinal cord, PN-1 expression occurs in cells lining the neural canal that are different from the cells previously shown to express tPA [12].
  • In adults, few distinct neuronal cell populations like pyramidal cells of the layer V in the neocortex retained detectable levels of PN-1 expression [12].
  • These findings suggest a role for PN-1 in the maturation of the central nervous system, a phase that is accompanied by the appearance of different forms of PN-1 [12].
  • These analyses revealed distinct temporal and spatial PN-1 expression patterns in developing cartilage, lung, skin, urogenital tract, and central and peripheral nervous system [12].

Associations of Serpine2 with chemical compounds


Physical interactions of Serpine2

  • A Krox binding site regulates protease nexin-1 promoter activity in embryonic heart, cartilage and parts of the nervous system [18].

Regulatory relationships of Serpine2

  • 5. These results suggest that Krox factors are among the important transcription factors regulating protease nexin-1 expression and thereby intracellular proteolytic activity in embryonic heart, cartilage and parts of the nervous system [18].
  • We propose that protease nexin 1 inhibits the destruction of myotube matrix by inactivating the plasmin/plasminogen activation system and may be the physiologic regulator of this system during muscle development in vivo [19].

Other interactions of Serpine2


Analytical, diagnostic and therapeutic context of Serpine2


  1. Protease nexin 1 in the murine kidney: glomerular localization and up-regulation in glomerulopathies. Moll, S., Schaeren-Wiemers, N., Wohlwend, A., Pastore, Y., Fulpius, T., Monard, D., Sappino, A.P., Schifferli, J.A., Vassalli, J.D., Izui, S. Kidney Int. (1996) [Pubmed]
  2. Expression of trypsin-like proteases and protease nexin-1 in mdx mouse muscles. Sawada, H., Kikukawa, Y., Ban, S., Kakudo, T., Yokosawa, H. Biochem. Biophys. Res. Commun. (2004) [Pubmed]
  3. Receptors for plasminogen activator, urokinase, in normal and Rous sarcoma virus-transformed mouse fibroblasts. Del Rosso, M., Dini, G., Fibbi, G. Cancer Res. (1985) [Pubmed]
  4. Neurite outgrowth activity of protease nexin-1 on neuroblastoma cells requires thrombin inhibition. Gurwitz, D., Cunningham, D.D. J. Cell. Physiol. (1990) [Pubmed]
  5. Male fertility defects in mice lacking the serine protease inhibitor protease nexin-1. Murer, V., Spetz, J.F., Hengst, U., Altrogge, L.M., de Agostini, A., Monard, D. Proc. Natl. Acad. Sci. U.S.A. (2001) [Pubmed]
  6. Cells regulate their mitogenic response to thrombin through release of protease nexin. Low, D.A., Scott, R.W., Baker, J.B., Cunningham, D.D. Nature (1982) [Pubmed]
  7. Protease-nexin I as an androgen-dependent secretory product of the murine seminal vesicle. Vassalli, J.D., Huarte, J., Bosco, D., Sappino, A.P., Sappino, N., Velardi, A., Wohlwend, A., Ernø, H., Monard, D., Belin, D. EMBO J. (1993) [Pubmed]
  8. Proteolytic action of thrombin is required for electrical activity-dependent synapse reduction. Liu, Y., Fields, R.D., Festoff, B.W., Nelson, P.G. Proc. Natl. Acad. Sci. U.S.A. (1994) [Pubmed]
  9. Sexually dimorphic expression of protease nexin-1 and vanin-1 in the developing mouse gonad prior to overt differentiation suggests a role in mammalian sexual development. Grimmond, S., Van Hateren, N., Siggers, P., Arkell, R., Larder, R., Soares, M.B., de Fatima Bonaldo, M., Smith, L., Tymowska-Lalanne, Z., Wells, C., Greenfield, A. Hum. Mol. Genet. (2000) [Pubmed]
  10. Tissue-specific cancer-related serpin gene cluster at human chromosome band 3q26. Chang, W.S., Chang, N.T., Lin, S.C., Wu, C.W., Wu, F.Y. Genes Chromosomes Cancer (2000) [Pubmed]
  11. Protease nexin-1 is expressed at the mouse met-/mesencephalic junction and FGF signaling regulates its promoter activity in primary met-/mesencephalic cells. Küry, P., Schaeren-Wiemers, N., Monard, D. Development (1997) [Pubmed]
  12. Variable and multiple expression of Protease Nexin-1 during mouse organogenesis and nervous system development. Mansuy, I.M., van der Putten, H., Schmid, P., Meins, M., Botteri, F.M., Monard, D. Development (1993) [Pubmed]
  13. Endogenous serine protease inhibitor modulates epileptic activity and hippocampal long-term potentiation. Lüthi, A., Van der Putten, H., Botteri, F.M., Mansuy, I.M., Meins, M., Frey, U., Sansig, G., Portet, C., Schmutz, M., Schröder, M., Nitsch, C., Laurent, J.P., Monard, D. J. Neurosci. (1997) [Pubmed]
  14. Localization of protease nexin-1 gene Spi4 between villin and acetylcholine receptor gamma genes on mouse Chromosome 1. Voss, G.C., Botteri, F., Monard, D., Jockusch, H. Mamm. Genome (1996) [Pubmed]
  15. Released protease-nexin regulates cellular binding, internalization, and degradation of serine proteases. Low, D.A., Baker, J.B., Koonce, W.C., Cunningham, D.D. Proc. Natl. Acad. Sci. U.S.A. (1981) [Pubmed]
  16. Evidence that a variety of cultured cells secrete protease nexin and produce a distinct cytoplasmic serine protease-binding factor. Eaton, D.L., Baker, J.B. J. Cell. Physiol. (1983) [Pubmed]
  17. Potential triple helix-mediated inhibition of IGF-I gene expression significantly reduces tumorigenicity of glioblastoma in an animal model. Shevelev, A., Burfeind, P., Schulze, E., Rininsland, F., Johnson, T.R., Trojan, J., Chernicky, C.L., Hélène, C., Ilan, J., Ilan, J. Cancer Gene Ther. (1997) [Pubmed]
  18. A Krox binding site regulates protease nexin-1 promoter activity in embryonic heart, cartilage and parts of the nervous system. Ernø, H., Küry, P., Botteri, F.M., Monard, D. Mech. Dev. (1996) [Pubmed]
  19. Protease nexin I, a serpin, inhibits plasminogen-dependent degradation of muscle extracellular matrix. Rao, J.S., Kahler, C.B., Baker, J.B., Festoff, B.W. Muscle Nerve (1989) [Pubmed]
  20. Expression of mRNA for plasminogen activators and protease nexin-1 in innervated and denervated mouse skeletal muscle. Magnusson, C., Högklint, L., Libelius, R., Tågerud, S. J. Neurosci. Res. (2001) [Pubmed]
  21. Regulation of prothrombin, thrombin receptor, and protease nexin-1 expression during development and after denervation in muscle. Kim, S., Buonanno, A., Nelson, P.G. J. Neurosci. Res. (1998) [Pubmed]
  22. Two populations of layer v pyramidal cells of the mouse neocortex: development and sensitivity to anesthetics. Christophe, E., Doerflinger, N., Lavery, D.J., Molnár, Z., Charpak, S., Audinat, E. J. Neurophysiol. (2005) [Pubmed]
  23. Apoptotic, injury-induced cell death in cultured mouse murine motor neurons. Citron, B.A., Zhang, S.X., Smirnova, I.V., Festoff, B.W. Neurosci. Lett. (1997) [Pubmed]
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