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Radioligand binding, enzymatic and immunoblotting experiments in membrane preparations of frontoparietal cortex, striatum, and hippocampus isolated from the ischemic hemisphere of mouse brain 24\u00a0h after reperfusion revealed statistically significant increase (\u2265\u00a0twofold) in quantity and activity of neurolysin compared with sham\u2010operated controls. Cerebellar membranes isolated from the ischemic hemisphere served as negative control supporting the observations that up\u2010regulation of neurolysin occurs in post\u2010ischemic brain regions. This study also documents sustained functional up\u2010regulation of neurolysin in frontoparietal cortical membranes for at least 7\u00a0days after stroke, which appears not to be transcriptionally or translationally regulated, but rather depends on translocation of cytosolic neurolysin to the membranes and mitochondria. Considering diversity of endogenous neurolysin substrates (neurotensin, bradykinin, angiotensins I\/\n                    <jats:styled-content style=\"fixed-case\">II<\/jats:styled-content>\n                    , substance P, hemopressin, dynorphin A(1\u20108), metorphamide, somatostatin) and the well\u2010documented role of these peptidergic systems in pathogenesis of stroke, resistance to ischemic injury and\/or post\u2010stroke brain recovery, our findings suggest that neurolysin may play a role in processes modulating the brain's response to stroke and its recovery after stroke.\n                    <jats:boxed-text content-type=\"graphic\" position=\"anchor\">\n                      <jats:graphic xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" mimetype=\"image\/png\" position=\"anchor\" specific-use=\"enlarged-web-image\" xlink:href=\"graphic\/jnc12513-fig-0007-m.png\">\n                        <jats:alt-text>image<\/jats:alt-text>\n                      <\/jats:graphic>\n                    <\/jats:boxed-text>\n                  <\/jats:p>\n                  <jats:p>We provide evidence that peptidase neurolysin is up\u2010regulated in the mouse brain membranes after stroke. Neurolysin metabolizes several neuropeptides in the brain (neurotensin, bradykinin, angiotensins I and II, substance P, hemopressin, dynorphin A(1\u20108), metorphamide, somatostatin), which have various functions in stroke pathophysiology. We hypothesize that neurolysin plays a key role in processes modulating the brain's response to stroke and its recovery after stroke.<\/jats:p>","DOI":"10.1111\/jnc.12513","type":"journal-article","created":{"date-parts":[[2013,10,27]],"date-time":"2013-10-27T08:02:52Z","timestamp":1382860972000},"page":"179-189","source":"Crossref","is-referenced-by-count":47,"title":["Functional up\u2010regulation of endopeptidase neurolysin during post\u2010acute and early recovery phases of experimental stroke in mouse brain"],"prefix":"10.1111","volume":"129","author":[{"given":"Mamoon","family":"Rashid","sequence":"first","affiliation":[{"name":"Department of Pharmaceutical Sciences Texas Tech University Health Sciences Center Amarillo Texas USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Naomi J.","family":"Wangler","sequence":"additional","affiliation":[{"name":"Department of Pharmaceutical Sciences Texas Tech University Health Sciences Center Amarillo Texas USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Li","family":"Yang","sequence":"additional","affiliation":[{"name":"Department of Pharmaceutical Sciences Texas Tech University Health Sciences Center Amarillo Texas USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Kaushik","family":"Shah","sequence":"additional","affiliation":[{"name":"Department of Pharmaceutical Sciences Texas Tech University Health Sciences Center Amarillo Texas USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Thiruma V.","family":"Arumugam","sequence":"additional","affiliation":[{"name":"Department of Physiology Yong Loo Lin School of Medicine National University of Singapore Singapore"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Thomas J.","family":"Abbruscato","sequence":"additional","affiliation":[{"name":"Department of Pharmaceutical Sciences Texas Tech University Health Sciences Center Amarillo Texas USA"},{"name":"Center for Blood Brain Barrier Research School of Pharmacy Texas Tech University Health Sciences Center Amarillo Texas USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Vardan T.","family":"Karamyan","sequence":"additional","affiliation":[{"name":"Department of Pharmaceutical Sciences Texas Tech University Health Sciences Center Amarillo Texas USA"},{"name":"Center for Blood Brain Barrier Research School of Pharmacy Texas Tech University Health Sciences Center Amarillo Texas USA"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"311","published-online":{"date-parts":[[2013,11,19]]},"reference":[{"key":"e_1_2_7_2_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.pneurobio.2012.11.004"},{"key":"e_1_2_7_3_1","doi-asserted-by":"publisher","DOI":"10.1016\/0306-4522(95)00198-R"},{"key":"e_1_2_7_4_1","doi-asserted-by":"publisher","DOI":"10.1111\/j.1471-4159.2005.03361.x"},{"key":"e_1_2_7_5_1","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.051633198"},{"key":"e_1_2_7_6_1","doi-asserted-by":"publisher","DOI":"10.1002\/ana.20845"},{"key":"e_1_2_7_7_1","doi-asserted-by":"publisher","DOI":"10.1097\/01.fjc.0000166307.86678.d1"},{"key":"e_1_2_7_8_1","doi-asserted-by":"crossref","first-page":"11274","DOI":"10.1016\/S0021-9258(18)67379-X","article-title":"Purification and characterization of a novel neurotensin\u2010degrading peptidase from rat brain synaptic membranes","volume":"261","author":"Checler F.","year":"1986","journal-title":"J. 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