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@ARTICLE{Rhnert:136528,
      author       = {Röhnert, Peter and Schmidt, Werner and Emmerlich, Patrick
                      and Goihl, Alexander and Wrenger, Sabine and Bank, Ute and
                      Nordhoff, Karsten and Täger, Michael and Ansorge, Siegfried
                      and Reinhold, Dirk and Striggow, Frank},
      title        = {{D}ipeptidyl peptidase {IV}, aminopeptidase {N} and
                      {DPIV}/{APN}-like proteases in cerebral ischemia.},
      journal      = {Journal of neuroinflammation},
      volume       = {9},
      number       = {1},
      issn         = {1742-2094},
      address      = {London},
      publisher    = {BioMed Central},
      reportid     = {DZNE-2020-02850},
      pages        = {557},
      year         = {2012},
      abstract     = {Cerebral 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.},
      keywords     = {Animals / Brain Ischemia: complications / Brain Ischemia:
                      drug therapy / Brain Ischemia: enzymology / CD13 Antigens:
                      genetics / CD13 Antigens: metabolism / Cerebral Infarction:
                      enzymology / Cerebral Infarction: etiology / Dipeptidyl
                      Peptidase 4: genetics / Dipeptidyl Peptidase 4: metabolism /
                      Dipeptidyl-Peptidases and Tripeptidyl-Peptidases: genetics /
                      Dipeptidyl-Peptidases and Tripeptidyl-Peptidases: metabolism
                      / Disease Models, Animal / Enzyme Inhibitors: therapeutic
                      use / Functional Laterality / Gene Expression Regulation,
                      Enzymologic: physiology / Glial Fibrillary Acidic Protein:
                      metabolism / Glycosphingolipids: therapeutic use / Male /
                      Phosphopyruvate Hydratase: metabolism / RNA, Messenger:
                      metabolism / Rats / Rats, Sprague-Dawley / Time Factors /
                      Enzyme Inhibitors (NLM Chemicals) / Glial Fibrillary Acidic
                      Protein (NLM Chemicals) / Glycosphingolipids (NLM Chemicals)
                      / RNA, Messenger (NLM Chemicals) /
                      inositolphosphorylceramide (NLM Chemicals) / CD13 Antigens
                      (NLM Chemicals) / Dipeptidyl-Peptidases and
                      Tripeptidyl-Peptidases (NLM Chemicals) / Dpp8 protein, rat
                      (NLM Chemicals) / Dipeptidyl Peptidase 4 (NLM Chemicals) /
                      Phosphopyruvate Hydratase (NLM Chemicals)},
      cin          = {AG Striggow},
      ddc          = {610},
      cid          = {I:(DE-2719)5000045},
      pnm          = {342 - Disease Mechanisms and Model Systems (POF3-342)},
      pid          = {G:(DE-HGF)POF3-342},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:22373413},
      pmc          = {pmc:PMC3359160},
      doi          = {10.1186/1742-2094-9-44},
      url          = {https://pub.dzne.de/record/136528},
}