CPLX2: diferenças entre revisões

Origem: Wikipédia, a enciclopédia livre.
Conteúdo apagado Conteúdo adicionado
FlaBot (discussão | contribs)
m Bot: Adicionando: en:CPLX2
Linha 1: Linha 1:
A '''complexina 2''' (também conhecida como '''CPLX2'''), é um [[gene]] humano.<ref name="entrez">{{cite web | title = Entrez Gene: CPLX2 complexin 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10814| accessdate = }}</ref>
A '''complexina 2''' (também conhecida como '''CPLX2'''), é uma proteína que em seres humanos é codificada pelo [[gene]] ''CPLX2''.<ref name="entrez">{{cite web | title = Entrez Gene: CPLX2 complexin 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10814| accessdate = }}</ref>


As proteínas codificadas pela família genética complexina/sinapsina são proteínas citosólicas que actuam na [[exocitose]] de vesículas sinápticas. Estas proteínas ligam-se à sintaxina, parte do receptor SNAP. O produto proteíco deste gene liga-se ao receptor SNAP, causando a sua disrupção e assim causando a libertação de transmissor. Duas variantes de transcriptos codificando a mesma proteína foram encontradas para este gene.<ref name="entrez">{{cite web | title = Entrez Gene: CPLX2 complexin 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10814| accessdate = }}</ref>
As proteínas codificadas pela família genética complexina/sinapsina são proteínas citosólicas que actuam na [[exocitose]] de vesículas sinápticas. Estas proteínas ligam-se à sintaxina, parte do receptor SNAP. O produto proteíco deste gene liga-se ao receptor SNAP, causando a sua disrupção e assim causando a libertação de transmissor. Duas variantes de transcriptos codificando a mesma proteína foram encontradas para este gene.<ref name="entrez">{{cite web | title = Entrez Gene: CPLX2 complexin 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10814| accessdate = }}</ref>
Linha 5: Linha 5:
==Referências==
==Referências==
<references/>
<references/>

==Leitura de apoio==

{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Abe T |title=[The mechanism of neurotransmitter release: role of synaphin/complexin in synaptic vesicle exocytosis] |journal=Tanpakushitsu Kakusan Koso |volume=47 |issue= 7 |pages= 794–800 |year= 2002 |pmid= 12058476 |doi= }}
*{{cite journal | author=Christensen VL, Johnston NP |title=Effect of time of day of insemination and the position of the egg in the oviduct on the fertility of turkeys. |journal=Poult. Sci. |volume=56 |issue= 2 |pages= 458–62 |year= 1978 |pmid= 605033 |doi= }}
*{{cite journal | author=Morgans CW, Brandstätter JH, Kellerman J, ''et al.'' |title=A SNARE complex containing syntaxin 3 is present in ribbon synapses of the retina. |journal=J. Neurosci. |volume=16 |issue= 21 |pages= 6713–21 |year= 1996 |pmid= 8824312 |doi= }}
*{{cite journal | author=Harrison PJ, Eastwood SL |title=Preferential involvement of excitatory neurons in medial temporal lobe in schizophrenia. |journal=Lancet |volume=352 |issue= 9141 |pages= 1669–73 |year= 1998 |pmid= 9853440 |doi=10.1016/S0140-6736(98)03341-8 }}
*{{cite journal | author=Ishizuka T, Saisu H, Odani S, ''et al.'' |title=Distinct regional distribution in the brain of messenger RNAs for the two isoforms of synaphin associated with the docking/fusion complex. |journal=Neuroscience |volume=88 |issue= 1 |pages= 295–306 |year= 1999 |pmid= 10051208 |doi=10.1016/S0306-4522(98)00223-1 }}
*{{cite journal | author=Yamada M, Saisu H, Ishizuka T, ''et al.'' |title=Immunohistochemical distribution of the two isoforms of synaphin/complexin involved in neurotransmitter release: localization at the distinct central nervous system regions and synaptic types. |journal=Neuroscience |volume=93 |issue= 1 |pages= 7–18 |year= 1999 |pmid= 10430466 |doi=10.1016/S0306-4522(99)00104-9 }}
*{{cite journal | author=Pabst S, Hazzard JW, Antonin W, ''et al.'' |title=Selective interaction of complexin with the neuronal SNARE complex. Determination of the binding regions. |journal=J. Biol. Chem. |volume=275 |issue= 26 |pages= 19808–18 |year= 2000 |pmid= 10777504 |doi= 10.1074/jbc.M002571200 }}
*{{cite journal | author=Eastwood SL, Cotter D, Harrison PJ |title=Cerebellar synaptic protein expression in schizophrenia. |journal=Neuroscience |volume=105 |issue= 1 |pages= 219–29 |year= 2001 |pmid= 11483314 |doi=10.1016/S0306-4522(01)00141-5 }}
*{{cite journal | author=Eastwood SL, Harrison PJ |title=Synaptic pathology in the anterior cingulate cortex in schizophrenia and mood disorders. A review and a Western blot study of synaptophysin, GAP-43 and the complexins. |journal=Brain Res. Bull. |volume=55 |issue= 5 |pages= 569–78 |year= 2001 |pmid= 11576753 |doi=10.1016/S0361-9230(01)00530-5 }}
*{{cite journal | author=Pabst S, Margittai M, Vainius D, ''et al.'' |title=Rapid and selective binding to the synaptic SNARE complex suggests a modulatory role of complexins in neuroexocytosis. |journal=J. Biol. Chem. |volume=277 |issue= 10 |pages= 7838–48 |year= 2002 |pmid= 11751907 |doi= 10.1074/jbc.M109507200 }}
*{{cite journal | author=Sawada K, Young CE, Barr AM, ''et al.'' |title=Altered immunoreactivity of complexin protein in prefrontal cortex in severe mental illness. |journal=Mol. Psychiatry |volume=7 |issue= 5 |pages= 484–92 |year= 2002 |pmid= 12082566 |doi= 10.1038/sj.mp.4000978 }}
*{{cite journal | author=Hu K, Carroll J, Rickman C, Davletov B |title=Action of complexin on SNARE complex. |journal=J. Biol. Chem. |volume=277 |issue= 44 |pages= 41652–6 |year= 2003 |pmid= 12200427 |doi= 10.1074/jbc.M205044200 }}
*{{cite journal | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |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 }}
*{{cite journal | author=Edwardson JM, Wang CT, Gong B, ''et al.'' |title=Expression of mutant huntingtin blocks exocytosis in PC12 cells by depletion of complexin II. |journal=J. Biol. Chem. |volume=278 |issue= 33 |pages= 30849–53 |year= 2003 |pmid= 12807877 |doi= 10.1074/jbc.M304615200 }}
*{{cite journal | author=Ota T, Suzuki Y, Nishikawa T, ''et al.'' |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40–5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 }}
*{{cite journal | author=Gerhard DS, Wagner L, Feingold EA, ''et al.'' |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 | author=Eastwood SL, Harrison PJ |title=Decreased expression of vesicular glutamate transporter 1 and complexin II mRNAs in schizophrenia: further evidence for a synaptic pathology affecting glutamate neurons. |journal=[[Schizophrenia Research|Schizophr. Res.]] |volume=73 |issue= 2-3 |pages= 159–72 |year= 2005 |pmid= 15653259 |doi= 10.1016/j.schres.2004.05.010 }}
*{{cite journal | author=DiProspero NA, Chen EY, Charles V, ''et al.'' |title=Early changes in Huntington's disease patient brains involve alterations in cytoskeletal and synaptic elements. |journal=J. Neurocytol. |volume=33 |issue= 5 |pages= 517–33 |year= 2005 |pmid= 15906159 |doi= 10.1007/s11068-004-0514-8 }}
}}
{{refend}}


{{esboço-genética}}
{{esboço-genética}}

Revisão das 20h53min de 24 de dezembro de 2010

A complexina 2 (também conhecida como CPLX2), é uma proteína que em seres humanos é codificada pelo gene CPLX2.[1]

As proteínas codificadas pela família genética complexina/sinapsina são proteínas citosólicas que actuam na exocitose de vesículas sinápticas. Estas proteínas ligam-se à sintaxina, parte do receptor SNAP. O produto proteíco deste gene liga-se ao receptor SNAP, causando a sua disrupção e assim causando a libertação de transmissor. Duas variantes de transcriptos codificando a mesma proteína foram encontradas para este gene.[1]

Referências

Leitura de apoio

  • Abe T (2002). «[The mechanism of neurotransmitter release: role of synaphin/complexin in synaptic vesicle exocytosis]». Tanpakushitsu Kakusan Koso. 47 (7): 794–800. PMID 12058476 
  • Christensen VL, Johnston NP (1978). «Effect of time of day of insemination and the position of the egg in the oviduct on the fertility of turkeys.». Poult. Sci. 56 (2): 458–62. PMID 605033 
  • Morgans CW, Brandstätter JH, Kellerman J; et al. (1996). «A SNARE complex containing syntaxin 3 is present in ribbon synapses of the retina.». J. Neurosci. 16 (21): 6713–21. PMID 8824312 
  • Harrison PJ, Eastwood SL (1998). «Preferential involvement of excitatory neurons in medial temporal lobe in schizophrenia.». Lancet. 352 (9141): 1669–73. PMID 9853440. doi:10.1016/S0140-6736(98)03341-8 
  • Ishizuka T, Saisu H, Odani S; et al. (1999). «Distinct regional distribution in the brain of messenger RNAs for the two isoforms of synaphin associated with the docking/fusion complex.». Neuroscience. 88 (1): 295–306. PMID 10051208. doi:10.1016/S0306-4522(98)00223-1 
  • Yamada M, Saisu H, Ishizuka T; et al. (1999). «Immunohistochemical distribution of the two isoforms of synaphin/complexin involved in neurotransmitter release: localization at the distinct central nervous system regions and synaptic types.». Neuroscience. 93 (1): 7–18. PMID 10430466. doi:10.1016/S0306-4522(99)00104-9 
  • Pabst S, Hazzard JW, Antonin W; et al. (2000). «Selective interaction of complexin with the neuronal SNARE complex. Determination of the binding regions.». J. Biol. Chem. 275 (26): 19808–18. PMID 10777504. doi:10.1074/jbc.M002571200 
  • Eastwood SL, Cotter D, Harrison PJ (2001). «Cerebellar synaptic protein expression in schizophrenia.». Neuroscience. 105 (1): 219–29. PMID 11483314. doi:10.1016/S0306-4522(01)00141-5 
  • Eastwood SL, Harrison PJ (2001). «Synaptic pathology in the anterior cingulate cortex in schizophrenia and mood disorders. A review and a Western blot study of synaptophysin, GAP-43 and the complexins.». Brain Res. Bull. 55 (5): 569–78. PMID 11576753. doi:10.1016/S0361-9230(01)00530-5 
  • Pabst S, Margittai M, Vainius D; et al. (2002). «Rapid and selective binding to the synaptic SNARE complex suggests a modulatory role of complexins in neuroexocytosis.». J. Biol. Chem. 277 (10): 7838–48. PMID 11751907. doi:10.1074/jbc.M109507200 
  • Sawada K, Young CE, Barr AM; et al. (2002). «Altered immunoreactivity of complexin protein in prefrontal cortex in severe mental illness.». Mol. Psychiatry. 7 (5): 484–92. PMID 12082566. doi:10.1038/sj.mp.4000978 
  • Hu K, Carroll J, Rickman C, Davletov B (2003). «Action of complexin on SNARE complex.». J. Biol. Chem. 277 (44): 41652–6. PMID 12200427. doi:10.1074/jbc.M205044200 
  • Strausberg RL, Feingold EA, Grouse LH; et al. (2003). «Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.». Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. PMC 139241Acessível livremente. PMID 12477932. doi:10.1073/pnas.242603899 
  • Edwardson JM, Wang CT, Gong B; et al. (2003). «Expression of mutant huntingtin blocks exocytosis in PC12 cells by depletion of complexin II.». J. Biol. Chem. 278 (33): 30849–53. PMID 12807877. doi:10.1074/jbc.M304615200 
  • Ota T, Suzuki Y, Nishikawa T; et al. (2004). «Complete sequencing and characterization of 21,243 full-length human cDNAs.». Nat. Genet. 36 (1): 40–5. PMID 14702039. doi:10.1038/ng1285 
  • Gerhard DS, Wagner L, Feingold EA; et al. (2004). «The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).». Genome Res. 14 (10B): 2121–7. PMC 528928Acessível livremente. PMID 15489334. doi:10.1101/gr.2596504 
  • Eastwood SL, Harrison PJ (2005). «Decreased expression of vesicular glutamate transporter 1 and complexin II mRNAs in schizophrenia: further evidence for a synaptic pathology affecting glutamate neurons.». Schizophr. Res. 73 (2-3): 159–72. PMID 15653259. doi:10.1016/j.schres.2004.05.010 
  • DiProspero NA, Chen EY, Charles V; et al. (2005). «Early changes in Huntington's disease patient brains involve alterations in cytoskeletal and synaptic elements.». J. Neurocytol. 33 (5): 517–33. PMID 15906159. doi:10.1007/s11068-004-0514-8 
Ícone de esboço Este artigo sobre Genética é um esboço. Você pode ajudar a Wikipédia expandindo-o.