Organization of the human synphilin-1 gene, a candidate for Parkinson's disease

We have recently identified a protein we called synphilin-1, which interact s ill vivo with alpha-synuclein. Mutations in alpha-synuclein cause familia l Parkinson's disease (PD). Alpha-synuclein protein is present in the patho logic lesions of familial and sporadic PD, and diffuse Lewy body disease, i ndicating an important pathogenic role for alpha-synuclein, Here we describ e the structure of the human synphilin-1 gene (SNCAIP). The open reading fr ame of this gene is contained within ten exons. We have designed primers to amplify each SNCAIP exon, so these primers can now be used to screen fur m utations or polymorphisms in patients with Parkinson's disease or related d iseases. We found a highly polymorphic GT repeat within intron 5 of SNCAIP, suitable for linkage analysis of families with PD. We have mapped SNCAIP l ocus to Chromosome (Chr) 5q23.1-23.3 near markers WI-4673 and AFMB352XH5. I n addition, using immunohistochemistry in human postmortem brain tissue, we found that synphilin-1 protein is present in neuropil, similar to alpha-sy nuclein protein, Because of its association with alpha-synuclein, synphilin -1 may be a candidate for involvement in Parkinson's disease or other relat ed disorders.