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Serpina3n  -  serine (or cysteine) peptidase inhibitor,...

Rattus norvegicus

Synonyms: CPI-26, CPi-26, Contrapsin-like protease inhibitor 6, SPI-2.2, SPI-3, ...
 
 
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Disease relevance of Serpina3n

 

High impact information on Serpina3n

 

Biological context of Serpina3n

 

Anatomical context of Serpina3n

 

Associations of Serpina3n with chemical compounds

 

Regulatory relationships of Serpina3n

 

Other interactions of Serpina3n

  • They were synthesized as precursors of comparable sizes (45 kDa), which were post-translationally modified by N-glycosylation at three (SPI-3) or four (SPI-1 and SPI-2) sites [11].
  • SPI-1 and SPI-2 mRNAs were of similar sizes (1.8 kb), and were smaller than that of SPI-3 (2.2 kb); the difference corresponded to a longer, 3'-end untranslated sequence [11].
  • Animals mounted both positive and negative acute phase responses at all ages, but responses were blunted in young animals, reaching adult levels by days 7-19. alpha 1-Antitrypsin mRNA had no response, and Spi 2.2 mRNA had 50% the rise seen in adults on days 3 and 7 [12].
 

Analytical, diagnostic and therapeutic context of Serpina3n

  • Additionally, we show induction of SPI-3 mRNA in rat liver by in situ hybridization using a specific oligonucleotide probe [13].
  • RT-PCR analysis confirmed that SPI-3 mRNA expression in rat beta-cells is increased by IL-1 at an early stage (2 h), with maximal accumulation during 6-12 h and decline after 24 h [7].
  • To identify the transcription factors involved in regulation of the SPI-3 promoter-chloramphenicol acetyltransferase constructs we overexpressed Signal Transducer and Activator of Transcription (STAT) proteins (STAT1, STAT3, STAT5B, and STAT6) and CAAT enhancer-binding protein beta [4].
  • A combination of ISH and immunohistochemistry (IHC) were performed to prove the colocalization of SPI-3 mRNA and either glial fibrillary acidic protein (GFAP) or OX-42 [2].

References

  1. Induction of SPI-3 mRNA, encoding a serine protease inhibitor, in gerbil hippocampus after transient forebrain ischemia. Tsuda, M., Kitagawa, K., Imaizumi, K., Wanaka, A., Tohyama, M., Takagi, T. Brain Res. Mol. Brain Res. (1996) [Pubmed]
  2. Expression of serine protease inhibitor 3 in ocular tissues in endotoxin-induced uveitis in rat. Takamiya, A., Takeda, M., Yoshida, A., Kiyama, H. Invest. Ophthalmol. Vis. Sci. (2001) [Pubmed]
  3. Effect of selenium and vitamin E deficiency on differential gene expression in rat liver. Fischer, A., Pallauf, J., Gohil, K., Weber, S.U., Packer, L., Rimbach, G. Biochem. Biophys. Res. Commun. (2001) [Pubmed]
  4. Two separate signal transducer and activator of transcription proteins regulate transcription of the serine proteinase inhibitor-3 gene in hepatic cells. Kordula, T., Ripperger, J., Morella, K.M., Travis, J., Baumann, H. J. Biol. Chem. (1996) [Pubmed]
  5. Inflammation induces serine protease inhibitor 3 expression in the rat pineal gland. Takamiya, A., Takeda, M., Yoshida, A., Kiyama, H. Neuroscience (2002) [Pubmed]
  6. Molecular cloning and characterization of rat contrapsin-like protease inhibitor and related proteins. Ohkubo, K., Ogata, S., Misumi, Y., Takami, N., Ikehara, Y. J. Biochem. (1991) [Pubmed]
  7. IL-1beta induces serine protease inhibitor 3 (SPI-3) gene expression in rat pancreatic beta-cells. Detection by differential display of messenger RNA. Chen, M.C., Schuit, F., Pipeleers, D.G., Eizirik, D.L. Cytokine (1999) [Pubmed]
  8. Homologous rat hepatic protease inhibitor genes show divergent functional responses to inflammation. Schwarzenberg, S.J., Yoon, J.B., Sharp, H.L., Seelig, S. Am. J. Physiol. (1989) [Pubmed]
  9. Regulation of Spi 2.1 and 2.2 gene expression after turpentine inflammation: discordant responses to IL-6. Berry, S.A., Bergad, P.L., Stolz, A.M., Towle, H.C., Schwarzenberg, S.J. Am. J. Physiol. (1999) [Pubmed]
  10. Amyloid beta-(1-40) stimulates cyclic GMP production via release of kinins in primary cultured endothelial cells. Wirth, K.J., Fink, E., Rudolphi, K., Heitsch, H., Deutschländer, N., Wiemer, G. Eur. J. Pharmacol. (1999) [Pubmed]
  11. Molecular characterization of three rat liver serine-protease inhibitors affected by inflammation and hypophysectomy. Protein and mRNA analysis and cDNA cloning. Pages, G., Rouayrenc, J.F., Le Cam, G., Mariller, M., Le Cam, A. Eur. J. Biochem. (1990) [Pubmed]
  12. Developmental regulation of the hepatic acute phase response. Schwarzenberg, S.J., Potter, C.J., Berry, S.A. Am. J. Physiol. (1991) [Pubmed]
  13. Rat contrapsins are the type II acute phase proteins: regulation by interleukin 6 on the mRNA level. Kordula, T., Bugno, M., Lason, W., Przewlocki, R., Koj, A. Biochem. Biophys. Res. Commun. (1994) [Pubmed]
 
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