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neuroserpin

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{{Short description|Protein-coding gene in the species Homo sapiens}}

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Neuroserpin is a protein that in humans is encoded by the SERPINI1 gene.{{cite web | title = Entrez Gene: SERPINI1 serpin peptidase inhibitor, clade I (neuroserpin), member 1| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5274}}

It is associated with Familial encephalopathy with neuroserpin inclusion bodies.

Serine protease inhibitors of the serpin superfamily are involved in many cellular processes. Neuroserpin was first identified as a protein secreted from the axons of dorsal root ganglion neurons (Stoeckli et al., 1989). It is expressed in the late stages of neurogenesis during the process of synapse formation.[supplied by OMIM]

Interactions

SERPINI1 has been shown to interact with Tissue plasminogen activator.{{cite journal |last=Parmar |first=Parmjeet K |author2=Coates Leigh C |author3=Pearson John F |author4=Hill Rena M |author5=Birch Nigel P |date=September 2002 |title=Neuroserpin regulates neurite outgrowth in nerve growth factor-treated PC12 cells |journal=J. Neurochem. |volume=82 |issue=6 |pages=1406–15 | issn = 0022-3042| pmid = 12354288 |doi=10.1046/j.1471-4159.2002.01100.x |s2cid=23571680 |doi-access= }}

References

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Further reading

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  • {{cite journal |author1=Yepes M |author2=Lawrence DA |title=Neuroserpin: a selective inhibitor of tissue-type plasminogen activator in the central nervous system. |journal=Thromb. Haemost. |volume=91 |issue= 3 |pages= 457–64 |year= 2004 |pmid= 14983220 |doi= 10.1160/TH03-12-0766 |s2cid=39118265 }}
  • {{cite journal |vauthors=Schrimpf SP, Bleiker AJ, Brecevic L, etal |title=Human neuroserpin (PI12): cDNA cloning and chromosomal localization to 3q26. |journal=Genomics |volume=40 |issue= 1 |pages= 55–62 |year= 1997 |pmid= 9070919 |doi= 10.1006/geno.1996.4514 }}
  • {{cite journal |vauthors=Hastings GA, Coleman TA, Haudenschild CC, etal |title=Neuroserpin, a brain-associated inhibitor of tissue plasminogen activator is localized primarily in neurons. Implications for the regulation of motor learning and neuronal survival. |journal=J. Biol. Chem. |volume=272 |issue= 52 |pages= 33062–7 |year= 1998 |pmid= 9407089 |doi=10.1074/jbc.272.52.33062 |doi-access=free }}
  • {{cite journal |vauthors=Davis RL, Shrimpton AE, Holohan PD, etal |title=Familial dementia caused by polymerization of mutant neuroserpin. |journal=Nature |volume=401 |issue= 6751 |pages= 376–9 |year= 1999 |pmid= 10517635 |doi= 10.1038/43894 |s2cid=4413322 |doi-access=free }}
  • {{cite journal |vauthors=Chang WS, Chang NT, Lin SC, etal |title=Tissue-specific cancer-related serpin gene cluster at human chromosome band 3q26. |journal=Genes Chromosomes Cancer |volume=29 |issue= 3 |pages= 240–55 |year= 2000 |pmid= 10992299 |doi=10.1002/1098-2264(2000)9999:9999<::AID-GCC1029>3.0.CO;2-A |s2cid=23441111 }}
  • {{cite journal |author1=Belorgey D |author2=Crowther DC |author3=Mahadeva R |author4=Lomas DA |title=Mutant Neuroserpin (S49P) that causes familial encephalopathy with neuroserpin inclusion bodies is a poor proteinase inhibitor and readily forms polymers in vitro. |journal=J. Biol. Chem. |volume=277 |issue= 19 |pages= 17367–73 |year= 2002 |pmid= 11880376 |doi= 10.1074/jbc.M200680200 |doi-access=free }}
  • {{cite journal |vauthors=Davis RL, Shrimpton AE, Carrell RW, etal |title=Association between conformational mutations in neuroserpin and onset and severity of dementia. |journal=Lancet |volume=359 |issue= 9325 |pages= 2242–7 |year= 2002 |pmid= 12103288 |doi=10.1016/S0140-6736(02)09293-0 |s2cid=10722760 }}
  • {{cite journal |author1=Barker-Carlson K |author2=Lawrence DA |author3=Schwartz BS |title=Acyl-enzyme complexes between tissue-type plasminogen activator and neuroserpin are short-lived in vitro. |journal=J. Biol. Chem. |volume=277 |issue= 49 |pages= 46852–7 |year= 2003 |pmid= 12228252 |doi= 10.1074/jbc.M207740200 |doi-access=free }}
  • {{cite journal |vauthors=Parmar PK, Coates LC, Pearson JF, etal |title=Neuroserpin regulates neurite outgrowth in nerve growth factor-treated PC12 cells. |journal=J. Neurochem. |volume=82 |issue= 6 |pages= 1406–15 |year= 2002 |pmid= 12354288 |doi=10.1046/j.1471-4159.2002.01100.x |s2cid=23571680 |doi-access= }}
  • {{cite journal |vauthors=Strausberg RL, Feingold EA, Grouse LH, etal |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 | pmc=139241 |bibcode=2002PNAS...9916899M |doi-access=free }}
  • {{cite journal |author1=Miranda E |author2=Römisch K |author3=Lomas DA |title=Mutants of neuroserpin that cause dementia accumulate as polymers within the endoplasmic reticulum. |journal=J. Biol. Chem. |volume=279 |issue= 27 |pages= 28283–91 |year= 2004 |pmid= 15090543 |doi= 10.1074/jbc.M313166200 |doi-access=free }}
  • {{cite journal |vauthors=Teesalu T, Kulla A, Simisker A, etal |title=Tissue plasminogen activator and neuroserpin are widely expressed in the human central nervous system. |journal=Thromb. Haemost. |volume=92 |issue= 2 |pages= 358–68 |year= 2005 |pmid= 15269833 |doi= 10.1160/TH02-12-0310 }}
  • {{cite journal |vauthors=Belorgey D, Sharp LK, Crowther DC, etal |title=Neuroserpin Portland (Ser52Arg) is trapped as an inactive intermediate that rapidly forms polymers: implications for the epilepsy seen in the dementia FENIB. |journal=Eur. J. Biochem. |volume=271 |issue= 16 |pages= 3360–7 |year= 2004 |pmid= 15291813 |doi= 10.1111/j.1432-1033.2004.04270.x |doi-access= }}
  • {{cite journal |vauthors=Gerhard DS, Wagner L, Feingold EA, etal |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 | pmc=528928 }}
  • {{cite journal |author1=Onda M |author2=Belorgey D |author3=Sharp LK |author4=Lomas DA |title=Latent S49P neuroserpin forms polymers in the dementia familial encephalopathy with neuroserpin inclusion bodies. |journal=J. Biol. Chem. |volume=280 |issue= 14 |pages= 13735–41 |year= 2005 |pmid= 15664988 |doi= 10.1074/jbc.M413282200 |doi-access=free }}
  • {{cite journal |vauthors=Rual JF, Venkatesan K, Hao T, etal |title=Towards a proteome-scale map of the human protein-protein interaction network. |journal=Nature |volume=437 |issue= 7062 |pages= 1173–8 |year= 2005 |pmid= 16189514 |doi= 10.1038/nature04209 |bibcode=2005Natur.437.1173R |s2cid=4427026 }}
  • {{cite journal |vauthors=Kinghorn KJ, Crowther DC, Sharp LK, etal |title=Neuroserpin binds Abeta and is a neuroprotective component of amyloid plaques in Alzheimer disease. |journal=J. Biol. Chem. |volume=281 |issue= 39 |pages= 29268–77 |year= 2006 |pmid= 16849336 |doi= 10.1074/jbc.M600690200 |doi-access= free }}
  • {{cite journal |vauthors=Chen PY, Chang WS, Chou RH, etal |title=Two non-homologous brain diseases-related genes, SERPINI1 and PDCD10, are tightly linked by an asymmetric bidirectional promoter in an evolutionarily conserved manner. |journal=BMC Mol. Biol. |volume=8 |pages= 2 |year= 2007 |pmid= 17212813 |doi= 10.1186/1471-2199-8-2 | pmc=1796892 |doi-access=free }}
  • {{cite journal |vauthors=Gourfinkel-An I, Duyckaerts C, Camuzat A, etal |title=Clinical and neuropathologic study of a French family with a mutation in the neuroserpin gene. |journal=Neurology |volume=69 |issue= 1 |pages= 79–83 |year= 2007 |pmid= 17606885 |doi= 10.1212/01.wnl.0000265052.99144.b5 |s2cid=39704442 }}

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External links

  • The MEROPS online database for peptidases and their inhibitors: [http://merops.sanger.ac.uk/cgi-bin/merops.cgi?id=I04.025 I04.025]

{{PDB Gallery|geneid=5274}}

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