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000136528 0247_ $$2doi$$a10.1186/1742-2094-9-44
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000136528 041__ $$aEnglish
000136528 082__ $$a610
000136528 1001_ $$aRöhnert, Peter$$b0
000136528 245__ $$aDipeptidyl peptidase IV, aminopeptidase N and DPIV/APN-like proteases in cerebral ischemia.
000136528 260__ $$aLondon$$bBioMed Central$$c2012
000136528 264_1 $$2Crossref$$3online$$bSpringer Science and Business Media LLC$$c2012-02-28
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000136528 520__ $$aCerebral inflammation is a hallmark of neuronal degeneration. Dipeptidyl peptidase IV, aminopeptidase N as well as the dipeptidyl peptidases II, 8 and 9 and cytosolic alanyl-aminopeptidase are involved in the regulation of autoimmunity and inflammation. We studied the expression, localisation and activity patterns of these proteases after endothelin-induced occlusion of the middle cerebral artery in rats, a model of transient and unilateral cerebral ischemia.Male Sprague-Dawley rats were used. RT-PCR, immunohistochemistry and protease activity assays were performed at different time points, lasting from 2 h to 7 days after cerebral ischemia. The effect of protease inhibitors on ischemia-dependent infarct volumes was quantified 7 days post middle cerebral artery occlusion. Statistical analysis was conducted using the t-test.Qualitative RT-PCR revealed these proteases in ipsilateral and contralateral cortices. Dipeptidyl peptidase II and aminopeptidase N were up-regulated ipsilaterally from 6 h to 7 days post ischemia, whereas dipeptidyl peptidase 9 and cytosolic alanyl-aminopeptidase were transiently down-regulated at day 3. Dipeptidyl peptidase 8 and aminopeptidase N immunoreactivities were detected in cortical neurons of the contralateral hemisphere. At the same time point, dipeptidyl peptidase IV, 8 and aminopeptidase N were identified in activated microglia and macrophages in the ipsilateral cortex. Seven days post artery occlusion, dipeptidyl peptidase IV immunoreactivity was found in the perikarya of surviving cortical neurons of the ipsilateral hemisphere, whereas their nuclei were dipeptidyl peptidase 8- and amino peptidase N-positive. At the same time point, dipeptidyl peptidase IV, 8 and aminopeptidase N were targeted in astroglial cells. Total dipeptidyl peptidase IV, 8 and 9 activities remained constant in both hemispheres until day 3 post experimental ischemia, but were increased (+165%) in the ipsilateral cortex at day 7. In parallel, aminopeptidase N and cytosolic alanyl-aminopeptidase activities remained unchanged.Distinct expression, localization and activity patterns of proline- and alanine-specific proteases indicate their involvement in ischemia-triggered inflammation and neurodegeneration. Consistently, IPC1755, a non-selective protease inhibitor, revealed a significant reduction of cortical lesions after transient cerebral ischemia and may suggest dipeptidyl peptidase IV, aminopeptidase N and proteases with similar substrate specificity as potentially therapy-relevant targets.
000136528 536__ $$0G:(DE-HGF)POF3-342$$a342 - Disease Mechanisms and Model Systems (POF3-342)$$cPOF3-342$$fPOF III$$x0
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000136528 650_7 $$2NLM Chemicals$$aEnzyme Inhibitors
000136528 650_7 $$2NLM Chemicals$$aGlial Fibrillary Acidic Protein
000136528 650_7 $$2NLM Chemicals$$aGlycosphingolipids
000136528 650_7 $$2NLM Chemicals$$aRNA, Messenger
000136528 650_7 $$2NLM Chemicals$$ainositolphosphorylceramide
000136528 650_7 $$0EC 3.4.11.2$$2NLM Chemicals$$aCD13 Antigens
000136528 650_7 $$0EC 3.4.14.-$$2NLM Chemicals$$aDipeptidyl-Peptidases and Tripeptidyl-Peptidases
000136528 650_7 $$0EC 3.4.14.-$$2NLM Chemicals$$aDpp8 protein, rat
000136528 650_7 $$0EC 3.4.14.5$$2NLM Chemicals$$aDipeptidyl Peptidase 4
000136528 650_7 $$0EC 4.2.1.11$$2NLM Chemicals$$aPhosphopyruvate Hydratase
000136528 650_2 $$2MeSH$$aAnimals
000136528 650_2 $$2MeSH$$aBrain Ischemia: complications
000136528 650_2 $$2MeSH$$aBrain Ischemia: drug therapy
000136528 650_2 $$2MeSH$$aBrain Ischemia: enzymology
000136528 650_2 $$2MeSH$$aCD13 Antigens: genetics
000136528 650_2 $$2MeSH$$aCD13 Antigens: metabolism
000136528 650_2 $$2MeSH$$aCerebral Infarction: enzymology
000136528 650_2 $$2MeSH$$aCerebral Infarction: etiology
000136528 650_2 $$2MeSH$$aDipeptidyl Peptidase 4: genetics
000136528 650_2 $$2MeSH$$aDipeptidyl Peptidase 4: metabolism
000136528 650_2 $$2MeSH$$aDipeptidyl-Peptidases and Tripeptidyl-Peptidases: genetics
000136528 650_2 $$2MeSH$$aDipeptidyl-Peptidases and Tripeptidyl-Peptidases: metabolism
000136528 650_2 $$2MeSH$$aDisease Models, Animal
000136528 650_2 $$2MeSH$$aEnzyme Inhibitors: therapeutic use
000136528 650_2 $$2MeSH$$aFunctional Laterality
000136528 650_2 $$2MeSH$$aGene Expression Regulation, Enzymologic: physiology
000136528 650_2 $$2MeSH$$aGlial Fibrillary Acidic Protein: metabolism
000136528 650_2 $$2MeSH$$aGlycosphingolipids: therapeutic use
000136528 650_2 $$2MeSH$$aMale
000136528 650_2 $$2MeSH$$aPhosphopyruvate Hydratase: metabolism
000136528 650_2 $$2MeSH$$aRNA, Messenger: metabolism
000136528 650_2 $$2MeSH$$aRats
000136528 650_2 $$2MeSH$$aRats, Sprague-Dawley
000136528 650_2 $$2MeSH$$aTime Factors
000136528 7001_ $$0P:(DE-2719)9000421$$aSchmidt, Werner$$b1$$udzne
000136528 7001_ $$aEmmerlich, Patrick$$b2
000136528 7001_ $$aGoihl, Alexander$$b3
000136528 7001_ $$aWrenger, Sabine$$b4
000136528 7001_ $$aBank, Ute$$b5
000136528 7001_ $$aNordhoff, Karsten$$b6
000136528 7001_ $$aTäger, Michael$$b7
000136528 7001_ $$aAnsorge, Siegfried$$b8
000136528 7001_ $$aReinhold, Dirk$$b9
000136528 7001_ $$0P:(DE-2719)9000420$$aStriggow, Frank$$b10$$eLast author$$udzne
000136528 77318 $$2Crossref$$3journal-article$$a10.1186/1742-2094-9-44$$b : Springer Science and Business Media LLC, 2012-02-28$$n1$$p557$$tJournal of Neuroinflammation$$v9$$x1742-2094$$y2012
000136528 773__ $$0PERI:(DE-600)2156455-3$$a10.1186/1742-2094-9-44$$gVol. 9, no. 1, p. 557$$n1$$p557$$q9:1<557$$tJournal of neuroinflammation$$v9$$x1742-2094$$y2012
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000136528 9141_ $$y2012
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