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Sökning: WFRF:(Hernandez Diaz S) > (2005-2009) > Accumulation of ubi...

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FältnamnIndikatorerMetadata
00004321naa a2200493 4500
001oai:lup.lub.lu.se:752553b2-c44c-42d4-9de7-adab2423de99
003SwePub
008160401s2009 | |||||||||||000 ||eng|
009oai:prod.swepub.kib.ki.se:119257866
0247 a https://lup.lub.lu.se/record/14768852 URI
0247 a https://doi.org/10.1073/pnas.09064631062 DOI
0247 a http://kipublications.ki.se/Default.aspx?queryparsed=id:1192578662 URI
040 a (SwePub)lud (SwePub)ki
041 a engb eng
042 9 SwePub
072 7a art2 swepub-publicationtype
072 7a ref2 swepub-contenttype
1001 a Maynard, Christa J.u Karolinska Institutet4 aut
2451 0a Accumulation of ubiquitin conjugates in a polyglutamine disease model occurs without global ubiquitin/proteasome system impairment
264 c 2009-08-18
264 1b Proceedings of the National Academy of Sciences,c 2009
520 a Aggregation-prone proteins have been suggested to overwhelm and impair the ubiquitin/proteasome system (UPS) in polyglutamine (polyQ) disorders, such as Huntington's disease (HD). Overexpression of an N-terminal fragment of mutant huntingtin (N-mutHtt), an aggregation-prone polyQ protein responsible for HD, obstructs the UPS in cellular models. Furthermore, based on the accumulation of polyubiquitin conjugates in brains of R6/2 mice, which express human N-mutHtt and are one of the most severe polyQ disorder models, it has been proposed that UPS dysfunction is a consistent feature of this pathology, occurring in both in vitro and in vivo models. Here, we have exploited transgenic mice that ubiquitously express a ubiquitin fusion degradation proteasome substrate to directly assess the functionality of the UPS in R6/2 mice or the slower onset R6/1 mice. Although expression of N-mutHtt caused a general inhibition of the UPS in PC12 cells, we did not observe an increase in the levels of proteasome reporter substrate in the brains of R6/2 and R6/1 mice. We show that the increase in ubiquitin conjugates in R6/2 mice can be primarily attributed to an accumulation of large ubiquitin conjugates that are different from the conjugates observed upon UPS inhibition. Together our data show that polyubiquitylated proteins accumulate in R6/2 brain despite a largely operative UPS, and suggest that neurons are able to avoid or compensate for the inhibitory effects of N-mutHtt.
650 7a MEDICIN OCH HÄLSOVETENSKAPx Medicinska och farmaceutiska grundvetenskaperx Neurovetenskaper0 (SwePub)301052 hsv//swe
650 7a MEDICAL AND HEALTH SCIENCESx Basic Medicinex Neurosciences0 (SwePub)301052 hsv//eng
653 a protein degradation
653 a Huntington
653 a neurodegeneration
7001 a Bottcher, Claudia4 aut
7001 a Ortega, Zaira4 aut
7001 a Smith, Rubenu Lund University,Lunds universitet,Institutionen för experimentell medicinsk vetenskap,Medicinska fakulteten,Department of Experimental Medical Science,Faculty of Medicine4 aut0 (Swepub:lu)mphy-rsm
7001 a Florea, Bogdan I.4 aut
7001 a Diaz-Hernandez, Miguel4 aut
7001 a Brundin, Patriku Lund University,Lunds universitet,Institutionen för experimentell medicinsk vetenskap,Medicinska fakulteten,Department of Experimental Medical Science,Faculty of Medicine4 aut0 (Swepub:lu)mphy-pbr
7001 a Overkleeft, Hermen S.4 aut
7001 a Li, Jia-Yiu Lund University,Lunds universitet,Neural plasticitet och reparation,Forskargrupper vid Lunds universitet,Neural Plasticity and Repair,Lund University Research Groups4 aut0 (Swepub:lu)mphy-jli
7001 a Lucas, Jose J.4 aut
7001 a Dantuma, Nico P.u Karolinska Institutet4 aut
7102 a Karolinska Institutetb Institutionen för experimentell medicinsk vetenskap4 org
7730 t Proceedings of the National Academy of Sciencesd : Proceedings of the National Academy of Sciencesg 106:33, s. 13986-13991q 106:33<13986-13991x 1091-6490x 0027-8424
8564 u http://dx.doi.org/10.1073/pnas.0906463106x freey FULLTEXT
8564 u https://www.pnas.org/content/pnas/106/33/13986.full.pdf
8564 8u https://lup.lub.lu.se/record/1476885
8564 8u https://doi.org/10.1073/pnas.0906463106
8564 8u http://kipublications.ki.se/Default.aspx?queryparsed=id:119257866

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