{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,25]],"date-time":"2026-09-25T04:56:34Z","timestamp":1790312194033,"version":"4.1.0"},"reference-count":50,"publisher":"Wiley","issue":"7","license":[{"start":{"date-parts":[[2006,4,5]],"date-time":"2006-04-05T00:00:00Z","timestamp":1144195200000},"content-version":"vor","delay-in-days":4,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":["onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["Eur J of Neuroscience"],"published-print":{"date-parts":[[2006,4]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>Dysfunction of the ubiquitin\u2010proteasome system occurs in the substantia nigra (SN) in Parkinson's disease (PD). However, it is unknown whether this is a primary cause or a secondary consequence of other components of the pathogenic process. We have investigated in nonhuman primates whether initiating cell death through mitochondrial complex\u2003I inhibition using 1\u2010methyl\u20104\u2010phenyl\u20101,2,3,6\u2010tetrahydropyridine hydrochloride (MPTP) altered proteasomal activity or the proteasomal components in the SN. Chymotrypsin\u2010like, trypsin\u2010like and peptidylglutamyl\u2010peptide hydrolase (PGPH) activating of 20S proteasome were decreased in SN homogenates of MPTP\u2010treated marmosets compared to na\u00efve animals. Western blotting revealed a marked decrease in the expression of 20S\u2010\u03b1 subunits, but no change in 20S\u2010\u03b2 subunits in the SN of MPTP\u2010treated marmoset compared to na\u00efve animals. There was a marked decrease in the expression of the proteasome activator 700 (PA700) and proteasome activator 28 (PA28) regulatory complexes. The 20S\u2010\u03b14 subunit immunoreactivity was decreased in the nucleus of colocalized tyrosine hydroxylase (TH)\u2010positive cells of MPTP\u2010treated animals compared to na\u00efve animals but no difference in the intensity of 20S\u2010\u03b21i subunit staining. Immunoreactivity for PA700\u2010Rpt5 and PA28\u2010\u03b1 subunits within surviving TH\u2010positive cells of MPTP\u2010treated marmoset was reduced compared to na\u00efve controls. Overall, the changes in proteasomal function and structure occurring follow MPTP\u2010induced destruction of the SN in common marmosets were very similar to those found in PD. This suggests that altered proteasomal function in PD could be a consequence of other pathogenic processes occurring in SN as opposed to initiating cell death as previously suggested.<\/jats:p>","DOI":"10.1111\/j.1460-9568.2006.04718.x","type":"journal-article","created":{"date-parts":[[2006,4,5]],"date-time":"2006-04-05T13:46:57Z","timestamp":1144244817000},"page":"1766-1774","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":34,"title":["MPTP treatment of common marmosets impairs proteasomal enzyme activity and decreases expression of structural and regulatory elements of the 26S proteasome"],"prefix":"10.1111","volume":"23","author":[{"given":"B\u2010Y.","family":"Zeng","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"M. 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