tailieunhanh - Báo cáo khoa học: Parkin deficiency disrupts calcium homeostasis by modulating phospholipase C signalling

Mutations in the E3 ubiquitin ligase parkin cause early-onset, autosomal-recessive juvenile parkinsonism (AJRP), presumably as a result of a lack of function that alters the level, activity, aggregation or localization of its sub-strates. Recently, we have reported that phospholipase Cc1 is a substrate for parkin. | Parkin deficiency disrupts calcium homeostasis by modulating phospholipase C signalling Anna Sandebring1 2 Nodi Dehvari1 Monica Perez-Manso1 Kelly Jean Thomas2 Elena Karpilovski1 Mark R. Cookson2 Richard F. Cowburn1 3 and Angel Cedazo-Minguez1 1 Karolinska Institutet Department of NVS KI-Alzheimer s Disease Research Center Stockholm Sweden 2 Laboratory of Neurogenetics NationalInstitute on Aging NIH Bethesda MD USA 3 AstraZeneca R D LocalDiscovery RA CNS Pain Control Disease Biology Sodertalje Sweden Keywords autosomalrecessive juvenile Parkinsonism calcium parkin Parkinson s disease phospholipase C Correspondence A. Cedazo-Minguez Karolinska Institutet Department of NVS KI-Alzheimer s Disease Research Center NOVUM Floor 5 141 57 Huddinge Sweden Fax 46 8 585 83880 Tel 46 8 585 83751 E-mail These authors contributed equally to this work Received 9 April2009 revised 24 June 2009 accepted 7 July 2009 doi Mutations in the E3 ubiquitin ligase parkin cause early-onset autosomal-recessive juvenile parkinsonism AJRP presumably as a result of a lack of function that alters the level activity aggregation or localization of its substrates. Recently we have reported that phospholipase Cy1 is a substrate for parkin. In this article we show that parkin mutants and siRNA parkin knockdown cells possess enhanced levels of phospholipase Cy1 phosphorylation basal phosphoinositide hydrolysis and intracellular Ca2 concentration. The protein levels of Ca2 -regulated protein kinase Ca were decreased in AJRP parkin mutant cells. Neomycin and dantrolene both decreased the intracellular Ca2 levels in parkin mutants in comparison with those seen in wild-type parkin cells suggesting that the differences were a consequence of altered phospholipase C activity. The protection of wild-type parkin against 6-hydroxydopamine 6OHDA toxicity was also established in ARJP mutants on pretreatment with dantrolene implying that a balancing Ca2 .

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