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Progressive dysfunction and loss of striatalGABA<\/jats:styled-content>ergic medium spiny neurons (MSN<\/jats:styled-content>s) may account for some of the characteristic symptoms inHD<\/jats:styled-content>patients. Interestingly, inHD<\/jats:styled-content>,MSN<\/jats:styled-content>s expressing neuropeptide Y (NPY<\/jats:styled-content>) are spared and their numbers is even up\u2010regulated inHD<\/jats:styled-content>patients. Consistent with this, we report here on increased immuno\u2010linkedNPY<\/jats:styled-content>(IL<\/jats:styled-content>\u2010NPY<\/jats:styled-content>) levels in human cerebrospinal fluid (hCSF<\/jats:styled-content>) fromHD<\/jats:styled-content>patients (Control n = 10; early HD n = 9; mid HD n = 11). As this antibody\u2010based detection ofNPY<\/jats:styled-content>may provide false positive differences as a result of the antibody\u2010based detections of only fragments ofNPY<\/jats:styled-content>, the initial finding was validated by investigating the proteolytic stability ofNPY<\/jats:styled-content>inhCSF<\/jats:styled-content>using matrix\u2010assisted laser desorption\/ionization time\u2010of\u2010flight mass spectrometry (MALDI<\/jats:styled-content>\u2010TOF<\/jats:styled-content>\u2010MS<\/jats:styled-content>) and selective inhibitors. A comparison between resultingNPY<\/jats:styled-content>\u2010fragments and detailed epitope analysis verified significant differences inIL<\/jats:styled-content>\u2010NPY<\/jats:styled-content>1\u201336\/3\u201336<\/jats:sub>andNPY<\/jats:styled-content>1\u201330<\/jats:sub>levels betweenHD<\/jats:styled-content>patients and control subjects with no significant differences between early vs mid HD cases.Ex vivo<\/jats:italic>degradomics analysis demonstrated thatNPY<\/jats:styled-content>is initially degraded toNPY<\/jats:styled-content>1\u201330<\/jats:sub>by cathepsin D in bothHD<\/jats:styled-content>patients and control subjects. Yet,NPY<\/jats:styled-content>1\u201330<\/jats:sub>is then further differentially hydrolyzed by thimet oligopeptidase (TOP<\/jats:styled-content>) inHD<\/jats:styled-content>patients and by neprilysin (NEP<\/jats:styled-content>) in control subjects. Furthermore, alteredhCSF TOP<\/jats:styled-content>\u2010inhibitor Dynorphin A1\u201313<\/jats:sub>(Dyn\u2010A1\u201313<\/jats:sub>) andTOP<\/jats:styled-content>\u2010substrate Dyn\u2010A1\u20138<\/jats:sub>levels indicate an impaired Dyn\u2010A\u2010TOP<\/jats:styled-content>network inHD<\/jats:styled-content>patients. Thus, we conclude that elevatedIL<\/jats:styled-content>\u2010NPY<\/jats:styled-content>\u2010levels in conjunction withTOP<\/jats:styled-content>\u2010\/NEP<\/jats:styled-content>\u2010activity\/protein as well as Dyn\u2010A1\u201313<\/jats:sub>\u2010peptide levels may serve as a potential biomarker in humanCSF<\/jats:styled-content>of HD.<\/jats:p><\/jats:sec>image<\/jats:alt-text><\/jats:graphic><\/jats:boxed-text>Huntington's disease (HD) patients' cerebrospinal fluid (CSF) exhibits higher neuropeptide Y (NPY) levels. Further degradomics studies show that CSF\u2010NPY is initially degraded to NPY1\u201030 by Cathepsin D. The NPY1\u201030 fragment is then differentially degraded in HD vs control involving Neprilysin (NEP), Thimet Oligopeptidase (TOP), and TOP\u2010Dynorphin\u2010A network. Together, these findings may help in search for HD biomarkers.<\/jats:p><\/jats:sec>","DOI":"10.1111\/jnc.13624","type":"journal-article","created":{"date-parts":[[2016,3,26]],"date-time":"2016-03-26T16:53:53Z","timestamp":1459011233000},"page":"820-837","source":"Crossref","is-referenced-by-count":20,"title":["Neuropeptide Y (NPY<\/scp>) in cerebrospinal fluid from patients with Huntington's Disease: increasedNPY<\/scp>levels and differential degradation of theNPY<\/scp>1\u201330<\/sub>fragment"],"prefix":"10.1111","volume":"137","author":[{"given":"Leona","family":"Wagner","sequence":"first","affiliation":[{"name":"Deutschsprachige Selbsthilfegruppe f\u00fcr Alkaptonurie (DSAKU) e.V. 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