{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,10,21]],"date-time":"2025-10-21T00:40:21Z","timestamp":1761007221809,"version":"build-2065373602"},"reference-count":64,"publisher":"Wiley","issue":"13","license":[{"start":{"date-parts":[[2015,8,11]],"date-time":"2015-08-11T00:00:00Z","timestamp":1439251200000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"funder":[{"name":"ARAMISE (French patients association for research on Multiple System Atrophy)"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Movement Disorders"],"published-print":{"date-parts":[[2015,11]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:sec><jats:title>Background<\/jats:title><jats:p>MSA is a sporadic progressive neurodegenerative disorder characterized by a variable combination of parkinsonism, cerebellar ataxia, and autonomic dysfunction. The pathological hallmark of MSA is the accumulation of alpha\u2010synuclein aggregates in the cytoplasm of oligodendrocytes along with neuronal loss and neuroinflammation, as well as blood\u2013brain barrier dysfunction and myelin deterioration. Matrix metalloproteinases are zinc\u2010dependent endopeptidases involved in the remodeling of the extracellular matrix, demyelination, and blood\u2013brain barrier permeability. Several lines of evidence indicate a role for these enzymes in various pathological processes, including stroke, multiple sclerosis, Parkinson's, and Alzheimer's disease.<\/jats:p><\/jats:sec><jats:sec><jats:title>Methods<\/jats:title><jats:p>This study aimed to assess potential alterations of matrix metalloproteinase\u20101, \u20102, \u20103, and \u20109 expression or activity in MSA postmortem brain tissue.<\/jats:p><\/jats:sec><jats:sec><jats:title>Results<\/jats:title><jats:p>Gelatin zymography revealed increased matrix metalloproteinase\u20102 activity in the putamen, but not in the frontal cortex, of MSA patients relative to controls. Immunohistochemistry revealed increased number of glial cells positive for matrix metalloproteinase\u20101, \u20102, and \u20103 in the putamen and frontal cortex of MSA patients. Double immunofluorescence revealed that matrix metalloproteinase\u20102 and \u20103 were expressed in astrocytes and microglia. Only matrix metalloproteinase\u20102 colocalized with alpha\u2010synuclein in oligodendroglial cytoplasmic inclusions.<\/jats:p><\/jats:sec><jats:sec><jats:title>Conclusion<\/jats:title><jats:p>These results demonstrate widespread alterations of matrix metalloproteinase expression in MSA and a pattern of increased matrix metalloproteinase\u20102 expression and activity affecting preferentially a brain region severely affected (putamen) over a relatively spared region (frontal cortex). Elevated matrix metalloproteinase expression may thus contribute to the disease process in MSA by promoting blood\u2013brain barrier dysfunction and\/or myelin degradation. \u00a9 2015 International Parkinson and Movement Disorder Society<\/jats:p><\/jats:sec>","DOI":"10.1002\/mds.26329","type":"journal-article","created":{"date-parts":[[2015,8,11]],"date-time":"2015-08-11T04:06:21Z","timestamp":1439265981000},"page":"1802-1812","source":"Crossref","is-referenced-by-count":6,"title":["Region\u2010<scp>S<\/scp>pecific <scp>A<\/scp>lterations of <scp>M<\/scp>atrix <scp>M<\/scp>etalloproteinase <scp>A<\/scp>ctivity in <scp>M<\/scp>ultiple <scp>S<\/scp>ystem <scp>A<\/scp>trophy"],"prefix":"10.1002","volume":"30","author":[{"given":"Fares","family":"Bassil","sequence":"first","affiliation":[{"name":"Universit\u00e9 de Bordeaux, Institut des Maladies Neurod\u00e9g\u00e9n\u00e9ratives, UMR 5293 Bordeaux France"},{"name":"CNRS, Institut des Maladies Neurod\u00e9g\u00e9n\u00e9ratives, UMR 5293 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