pubmed-article:19229993 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:19229993 | lifeskim:mentions | umls-concept:C0013878 | lld:lifeskim |
pubmed-article:19229993 | lifeskim:mentions | umls-concept:C0004358 | lld:lifeskim |
pubmed-article:19229993 | lifeskim:mentions | umls-concept:C0027873 | lld:lifeskim |
pubmed-article:19229993 | lifeskim:mentions | umls-concept:C0292777 | lld:lifeskim |
pubmed-article:19229993 | lifeskim:mentions | umls-concept:C1510941 | lld:lifeskim |
pubmed-article:19229993 | lifeskim:mentions | umls-concept:C1521840 | lld:lifeskim |
pubmed-article:19229993 | pubmed:issue | 13 | lld:pubmed |
pubmed-article:19229993 | pubmed:dateCreated | 2009-8-31 | lld:pubmed |
pubmed-article:19229993 | pubmed:abstractText | Neuromyelitis optica (NMO) is an inflammatory autoimmune demyelinating disease of the central nervous system (CNS) which in autoantibodies produced by patients with NMO (NMO-IgG) recognize a glial water channel protein, Aquaporin-4 (AQP4) expressed as two major isoforms, M1- and M23-AQP4, in which the plasma membrane form orthogonal arrays of particles (OAPs). AQP4-M23 is the OAP-forming isoform, whereas AQP4-M1 alone is unable to form OAPs. The function of AQP4 organization into OAPs in normal physiology is unknown; however, alteration in OAP assemblies is reported for several CNS pathological states. In this study, we demonstrate that in the CNS, NMO-IgG is able to pull down both M1- and M23-AQP4 but experiments performed using cells selectively transfected with M1- or M23-AQP4 and native tissues show NMO-IgG epitope to be intrinsic in AQP4 assemblies into OAPs. Other OAP-forming water-channel proteins, such as the lens Aquaporin-0 and the insect Aquaporin-cic, were not recognized by NMO-IgG, indicating an epitope characteristic of AQP4-OAPs. Finally, water transport measurements show that NMO-IgG treatment does not significantly affect AQP4 function. In conclusion, our results suggest for the first time that OAP assemblies are required for NMO-IgG to recognize AQP4. | lld:pubmed |
pubmed-article:19229993 | pubmed:language | eng | lld:pubmed |
pubmed-article:19229993 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:19229993 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:19229993 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:19229993 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:19229993 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:19229993 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:19229993 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:19229993 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:19229993 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:19229993 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:19229993 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:19229993 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:19229993 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:19229993 | pubmed:month | Oct | lld:pubmed |
pubmed-article:19229993 | pubmed:issn | 1098-1136 | lld:pubmed |
pubmed-article:19229993 | pubmed:author | pubmed-author:RossiAndreaA | lld:pubmed |
pubmed-article:19229993 | pubmed:author | pubmed-author:PisaniFrances... | lld:pubmed |
pubmed-article:19229993 | pubmed:author | pubmed-author:TrojanoMariaM | lld:pubmed |
pubmed-article:19229993 | pubmed:author | pubmed-author:FrigeriAntoni... | lld:pubmed |
pubmed-article:19229993 | pubmed:author | pubmed-author:SveltoMariaM | lld:pubmed |
pubmed-article:19229993 | pubmed:author | pubmed-author:NicchiaGrazia... | lld:pubmed |
pubmed-article:19229993 | pubmed:author | pubmed-author:TortorellaCar... | lld:pubmed |
pubmed-article:19229993 | pubmed:author | pubmed-author:RuggieriMadda... | lld:pubmed |
pubmed-article:19229993 | pubmed:author | pubmed-author:LiaAnnaA | lld:pubmed |
pubmed-article:19229993 | pubmed:author | pubmed-author:MastrototaroM... | lld:pubmed |
pubmed-article:19229993 | pubmed:copyrightInfo | (c) 2009 Wiley-Liss, Inc. | lld:pubmed |
pubmed-article:19229993 | pubmed:issnType | Electronic | lld:pubmed |
pubmed-article:19229993 | pubmed:volume | 57 | lld:pubmed |
pubmed-article:19229993 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:19229993 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:19229993 | pubmed:pagination | 1363-73 | lld:pubmed |
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pubmed-article:19229993 | pubmed:year | 2009 | lld:pubmed |
pubmed-article:19229993 | pubmed:articleTitle | Aquaporin-4 orthogonal arrays of particles are the target for neuromyelitis optica autoantibodies. | lld:pubmed |
pubmed-article:19229993 | pubmed:affiliation | Department of General and Environmental Physiology and Centre of Excellence in Comparative Genomics (CEGBA), University of Bari, Bari, Italy. | lld:pubmed |
pubmed-article:19229993 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:19229993 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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