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SERPINI1  -  serpin peptidase inhibitor, clade I...

Homo sapiens

Synonyms: Neuroserpin, PI-12, PI12, Peptidase inhibitor 12, Serpin I1, ...
 
 
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Disease relevance of SERPINI1

  • To clarify this issue, we investigated five families with typical neuroserpin inclusion bodies but with various neurological manifestations [1].
  • Immunostaining revealed that MCAO resulted in reduction of neuroserpin immunoreactivity in the ipsilateral hemisphere after 2 to 6 hours of ischemia [2].
  • However, treatment with neuroserpin in combination with tPA significantly (P<0.05) reduced BBB leakage, brain edema, and ischemic lesion volume compared with rats treated with tPA alone, although ischemic lesion volumes were the same in both groups before the treatment [2].
  • We tested the hypothesis that neuroserpin, a natural inhibitor of tPA, reduces tPA-induced neuronal toxicity and increases its therapeutic window for treatment of embolic stroke [2].
  • As in the other three members whose gene expression is altered during tumorigenesis, PI12 expression was found to be down-regulated in tumor brain tissues and in two brain cancer cell lines: U-87 MG and H4 [3].
 

Psychiatry related information on SERPINI1

 

High impact information on SERPINI1

 

Chemical compound and disease context of SERPINI1

 

Biological context of SERPINI1

 

Anatomical context of SERPINI1

 

Associations of SERPINI1 with chemical compounds

  • Neuroserpin is a member of the serine proteinase inhibitor (serpin) gene family that reacts preferentially with tissue-type plasminogen activator (tPA) and is primarily localized to neurons in regions of the brain where tPA is also found [4].
  • DNA sequence analysis of exons 2 to 9 of the neuroserpin gene in the proband showed the published normal neuroserpin sequence except for the presence of both adenine and cytosine at the first position of codon 52, that indicates heterozygosity for both the normal Ser(AGT) and variant Arg(CGT) at this position in the expressed protein [13].
  • Using real-time quantitative PCR, we demonstrated increased neuroserpin mRNA expression in rat frontal cortex after chronic treatment with several classes of antidepressants, including imipramine, fluoxetine, sertraline, and venlafaxine [14].
 

Regulatory relationships of SERPINI1

 

Other interactions of SERPINI1

  • The decreases in mRNA abundance for MDH1 (P = 0.006), HINT1 (P = 0.050), and neuroserpin (P = 0.005) in DLPFC of male individuals with schizophrenia is consistent with prior reports [16].
  • The serpinopathies include alpha(1)-antitrypsin (SERPINA1) deficiency and the newly characterized familial encephalopathy with neuroserpin inclusion bodies (FENIB) resulting from mutations in the neuroserpin (SERPINI1) gene [17].
  • These data provide an alternative method for the inactivation of mutant neuroserpin as a proteinase inhibitor in FENIB and demonstrate a second pathway for the formation of intracellular polymers in association with disease [18].
  • Neuroserpin is a novel serine protease inhibitor of the serpin family [11].
  • Neuroserpin Portland (Ser52Arg) is trapped as an inactive intermediate that rapidly forms polymers: implications for the epilepsy seen in the dementia FENIB [19].
 

Analytical, diagnostic and therapeutic context of SERPINI1

References

  1. Association between conformational mutations in neuroserpin and onset and severity of dementia. Davis, R.L., Shrimpton, A.E., Carrell, R.W., Lomas, D.A., Gerhard, L., Baumann, B., Lawrence, D.A., Yepes, M., Kim, T.S., Ghetti, B., Piccardo, P., Takao, M., Lacbawan, F., Muenke, M., Sifers, R.N., Bradshaw, C.B., Kent, P.F., Collins, G.H., Larocca, D., Holohan, P.D. Lancet (2002) [Pubmed]
  2. Adjuvant treatment with neuroserpin increases the therapeutic window for tissue-type plasminogen activator administration in a rat model of embolic stroke. Zhang, Z., Zhang, L., Yepes, M., Jiang, Q., Li, Q., Arniego, P., Coleman, T.A., Lawrence, D.A., Chopp, M. Circulation (2002) [Pubmed]
  3. 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]
  4. Neuroserpin: a selective inhibitor of tissue-type plasminogen activator in the central nervous system. Yepes, M., Lawrence, D.A. Thromb. Haemost. (2004) [Pubmed]
  5. Accumulation of mutant neuroserpin precedes development of clinical symptoms in familial encephalopathy with neuroserpin inclusion bodies. Galliciotti, G., Glatzel, M., Kinter, J., Kozlov, S.V., Cinelli, P., Rülicke, T., Sonderegger, P. Am. J. Pathol. (2007) [Pubmed]
  6. Familial dementia caused by polymerization of mutant neuroserpin. Davis, R.L., Shrimpton, A.E., Holohan, P.D., Bradshaw, C., Feiglin, D., Collins, G.H., Sonderegger, P., Kinter, J., Becker, L.M., Lacbawan, F., Krasnewich, D., Muenke, M., Lawrence, D.A., Yerby, M.S., Shaw, C.M., Gooptu, B., Elliott, P.R., Finch, J.T., Carrell, R.W., Lomas, D.A. Nature (1999) [Pubmed]
  7. Cell toxicity and conformational disease. Carrell, R.W. Trends Cell Biol. (2005) [Pubmed]
  8. Sugar and alcohol molecules provide a therapeutic strategy for the serpinopathies that cause dementia and cirrhosis. Sharp, L.K., Mallya, M., Kinghorn, K.J., Wang, Z., Crowther, D.C., Huntington, J.A., Belorgey, D., Lomas, D.A. FEBS J. (2006) [Pubmed]
  9. Neuroserpin, a brain-associated inhibitor of tissue plasminogen activator is localized primarily in neurons. Implications for the regulation of motor learning and neuronal survival. Hastings, G.A., Coleman, T.A., Haudenschild, C.C., Stefansson, S., Smith, E.P., Barthlow, R., Cherry, S., Sandkvist, M., Lawrence, D.A. J. Biol. Chem. (1997) [Pubmed]
  10. Mutants of neuroserpin that cause dementia accumulate as polymers within the endoplasmic reticulum. Miranda, E., Römisch, K., Lomas, D.A. J. Biol. Chem. (2004) [Pubmed]
  11. Human neuroserpin (PI12): cDNA cloning and chromosomal localization to 3q26. Schrimpf, S.P., Bleiker, A.J., Brecevic, L., Kozlov, S.V., Berger, P., Osterwalder, T., Krueger, S.R., Schinzel, A., Sonderegger, P. Genomics (1997) [Pubmed]
  12. Neuroserpin regulates neurite outgrowth in nerve growth factor-treated PC12 cells. Parmar, P.K., Coates, L.C., Pearson, J.F., Hill, R.M., Birch, N.P. J. Neurochem. (2002) [Pubmed]
  13. Biochemical characterization of a neuroserpin variant associated with hereditary dementia. Yazaki, M., Liepnieks, J.J., Murrell, J.R., Takao, M., Guenther, B., Piccardo, P., Farlow, M.R., Ghetti, B., Benson, M.D. Am. J. Pathol. (2001) [Pubmed]
  14. Induction of neuroserpin expression in rat frontal cortex after chronic antidepressant treatment and electroconvulsive treatment. Tanaka, S., Yamada, M., Kitahara, S., Higuchi, T., Honda, K., Kamijima, K., Yamada, M. Nihon shinkei seishin yakurigaku zasshi = Japanese journal of psychopharmacology. (2006) [Pubmed]
  15. Acyl-enzyme complexes between tissue-type plasminogen activator and neuroserpin are short-lived in vitro. Barker-Carlson, K., Lawrence, D.A., Schwartz, B.S. J. Biol. Chem. (2002) [Pubmed]
  16. Gene expression of metabolic enzymes and a protease inhibitor in the prefrontal cortex are decreased in schizophrenia. Vawter, M.P., Shannon Weickert, C., Ferran, E., Matsumoto, M., Overman, K., Hyde, T.M., Weinberger, D.R., Bunney, W.E., Kleinman, J.E. Neurochem. Res. (2004) [Pubmed]
  17. Familial conformational diseases and dementias. Crowther, D.C. Hum. Mutat. (2002) [Pubmed]
  18. Latent S49P neuroserpin forms polymers in the dementia familial encephalopathy with neuroserpin inclusion bodies. Onda, M., Belorgey, D., Sharp, L.K., Lomas, D.A. J. Biol. Chem. (2005) [Pubmed]
  19. Neuroserpin Portland (Ser52Arg) is trapped as an inactive intermediate that rapidly forms polymers: implications for the epilepsy seen in the dementia FENIB. Belorgey, D., Sharp, L.K., Crowther, D.C., Onda, M., Johansson, J., Lomas, D.A. Eur. J. Biochem. (2004) [Pubmed]
  20. Mutant Neuroserpin (S49P) that causes familial encephalopathy with neuroserpin inclusion bodies is a poor proteinase inhibitor and readily forms polymers in vitro. Belorgey, D., Crowther, D.C., Mahadeva, R., Lomas, D.A. J. Biol. Chem. (2002) [Pubmed]
  21. Tissue plasminogen activator and neuroserpin are widely expressed in the human central nervous system. Teesalu, T., Kulla, A., Simisker, A., Sirén, V., Lawrence, D.A., Asser, T., Vaheri, A. Thromb. Haemost. (2004) [Pubmed]
  22. Neuroserpin (PI-12) is upregulated in high-grade prostate cancer and is associated with survival. Hasumi, H., Ishiguro, H., Nakamura, M., Sugiura, S., Osada, Y., Miyoshi, Y., Fujinami, K., Yao, M., Hamada, K., Yamada-Okabe, H., Kubota, Y., Uemura, H. Int. J. Cancer (2005) [Pubmed]
 
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