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alpha-synuclein implicated in Parkinson's disease is present in extracellular biological fluids, including human plasma

Lookup NU author(s): Mark Gibson, Dr Jennifer Court, Dr Mark Cookson

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Abstract

Parkinson's disease (PD) and other related disorders are characterized by the accumulation of fibrillar aggregates of alpha-synuclein protein (alpha-syn) inside brain cells. It is likely that the formation of alpha-syn aggregates plays a seminal role in the pathogenesis of at least some of these diseases, because two different mutations in the gene encoding alpha-syn have been found in inherited forms of PD. alpha-Syn is mainly expressed by neuronal cells and is generally considered to exist as a cytoplasmic protein. Here, we report the unexpected identification of alpha-syn in conditioned culture media from untransfected and alpha-syn-transfected human neuroblastoma cells, as well as in human cerebrospinal fluid and blood plasma. The method used was immunocapture by using anti-alpha-syn antibodies coupled to magnetic beads, followed by detection on Western blots. In all cases, alpha-syn was identified as a single 15 kDa band, which co-migrated with a recombinant form of the protein and reacted with five different antibodies to alpha-syn. Our findings suggest that cells normally secrete alpha-syn into their surrounding media, both in vitro and in vivo. The detection of extracellular alpha-syn and/or its modified forms in body fluids, particularly in human plasma, offers new opportunities for the development of diagnostic tests for PD and related diseases.


Publication metadata

Author(s): El-Agnaf OMA, Salem SA, Paleologou KE, Cooper LJ, Fullwood NJ, Gibson MJ, Curran MD, Court JA, Mann DMA, Ikeda S, Cookson MR, Hardy J, Allsop D

Publication type: Article

Publication status: Published

Journal: FASEB Journal

Year: 2003

Volume: 17

Issue: 11

Pages: 1945-1961

ISSN (print): 0892-6638

ISSN (electronic):

Publisher: Federation of American Societies for Experimental Biology

URL: http://dx.doi.org/10.1096/fj.03-0098fje

DOI: 10.1096/fj.03-0098fje


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