Felgenhauer, Klaus

[["dc.bibliographiccitation.firstpage","1138"],["dc.bibliographiccitation.issue","5"],["dc.bibliographiccitation.journal","The Journal of Infectious Diseases"],["dc.bibliographiccitation.lastpage","1141"],["dc.bibliographiccitation.volume","169"],["dc.contributor.author","Weber, Thomas"],["dc.contributor.author","Turner, Rodney W."],["dc.contributor.author","Frye, Stephan"],["dc.contributor.author","Ruf, Bernhard"],["dc.contributor.author","Haas, Judith"],["dc.contributor.author","Schielke, Eva"],["dc.contributor.author","Pohle, Hans-Dieter"],["dc.contributor.author","Lüke, Wolfgang"],["dc.contributor.author","Lüer, Wilfried"],["dc.contributor.author","Felgenhauer, Klaus"],["dc.contributor.author","Hunsmann, Gerhard"],["dc.date.accessioned","2022-10-06T13:34:57Z"],["dc.date.available","2022-10-06T13:34:57Z"],["dc.date.issued","1994"],["dc.identifier.doi","10.1093/infdis/169.5.1138"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/116019"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-602"],["dc.relation.eissn","1537-6613"],["dc.relation.issn","0022-1899"],["dc.relation.orgunit","Deutsches Primatenzentrum"],["dc.title","Specific Diagnosis of Progressive Multifocal Leukoencephalopathy by Polymerase Chain Reaction"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","49"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Journal of Neuroimmunology"],["dc.bibliographiccitation.lastpage","55"],["dc.bibliographiccitation.volume","116"],["dc.contributor.author","Felkel, C."],["dc.contributor.author","Scholl, U."],["dc.contributor.author","Mader, M."],["dc.contributor.author","Schwartz, P."],["dc.contributor.author","Felgenhauer, K."],["dc.contributor.author","Hardeland, Ruediger"],["dc.contributor.author","Beuche, W."],["dc.contributor.author","Weber, F."],["dc.date.accessioned","2018-11-07T09:07:20Z"],["dc.date.available","2018-11-07T09:07:20Z"],["dc.date.issued","2001"],["dc.description.abstract","Transmigration of human granulocytes across a basal lamina equivalent was studied in vitro. Transwell(R) inserts were coated with Matrigel(R), a reconstituted basement membrane. Granulocytes (2 x 10(6)) were applied to the upper chamber. As chemoattractant interleukin-8 (IL-8; 25 ng/ml) was added to the lower chamber. After 1 h of migration, cells were counted in the lower chamber. Specific hydroxamate inhibitors of MMPs (BB-3103, Ro 31-9790) or of serine proteases (Pefabloc(R), leupeptin) were added at various concentrations to both chambers before the start of migration. Additional experiments were performed with alpha (2)-macroglobulin, a natural inhibitor of MMPs and a monoclonal antibody which specifically blocks the activity of MMP-9. Migration of granulocytes through Matrigel could not be reduced significantly by any of the MMP inhibitors. A dose-dependent impairment of transmigration was only found with Pefabloc, however, this substance also induced severe morphological changes of the cells. The other inhibitor of serine proteases, leupeptin, did not influence migration at all. (C) 2001 Elsevier Science B.V. All rights reserved."],["dc.identifier.doi","10.1016/S0165-5728(01)00294-6"],["dc.identifier.isi","000168204100007"],["dc.identifier.pmid","11311329"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/25771"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Elsevier Science Bv"],["dc.relation.issn","0165-5728"],["dc.title","Migration of human granulocytes through reconstituted basement membrane is not dependent on matrix metalloproteinase-9 (MMP-9)"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","233"],["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","Journal of Neuroimmunology"],["dc.bibliographiccitation.lastpage","237"],["dc.bibliographiccitation.volume","116"],["dc.contributor.author","Maliszewska, M."],["dc.contributor.author","Mader, M."],["dc.contributor.author","Scholl, U."],["dc.contributor.author","Azeh, I."],["dc.contributor.author","Hardeland, Ruediger"],["dc.contributor.author","Felgenhauer, K."],["dc.contributor.author","Beuche, W."],["dc.contributor.author","Weber, F."],["dc.date.accessioned","2018-11-07T09:01:12Z"],["dc.date.available","2018-11-07T09:01:12Z"],["dc.date.issued","2001"],["dc.description.abstract","Determination of matrix metalloproteinase-9 (MMP-9) in human cerebrospinal fluid (CSF) to study blood-brain barrier impairment and immune cell migration in inflammatory neurological diseases recently became a matter of major interest. Regularly, MMP-9 was determined qualitatively or semi-quantitatively by zymography (gelatin gel electrophoresis) or quantitatively by enzyme immunoassay (EIA). As yet, it was not possible by either method to detect MMP-9 in CSF of controls (patients without pathologically increased CSF parameters). We developed an ultrasensitive two-side enzyme-linked immunosorbent assay (ELISA) which allows for the first time to measure reliably MMP-9 concentrations in CSF of controls. This ELISA uses a monoclonal as capture and a polyclonal as detector antibody. The detection limit of the assay is below 10 pg/ml and the assay range is 15-2000 pg/ml. Intra-assay precision is 2.5% for low and 3.7% for high, inter-assay precision is 11% for low and 10.7% for high values, respectively. The determination of the MMP-9 concentration in 50 control CSF gave the following results: range, 22-146 pg/ml; median, 76 pg/ml. The measurement of native and recombinant MMP-9 was carried out with three commercially available ELISAs, most widely employed in MMP-9 research, and compared to the newly developed one. All ELISAs recognize recombinant MMP-9 by factors of 5-20 less sensitively than native MMP-9. (C) 2001 Elsevier Science B.V. All rights reserved."],["dc.identifier.doi","10.1016/S0165-5728(01)00304-6"],["dc.identifier.isi","000170148400013"],["dc.identifier.pmid","11438179"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/24358"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Elsevier Science Bv"],["dc.relation.issn","0165-5728"],["dc.title","Development of an ultrasensitive enzyme immunoassay for the determination of matrix metalloproteinase-9 (MMP-9) levels in normal human cerebrospinal fluid"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","3419"],["dc.bibliographiccitation.issue","16"],["dc.bibliographiccitation.journal","Neuroreport"],["dc.bibliographiccitation.lastpage","3422"],["dc.bibliographiccitation.volume","11"],["dc.contributor.author","Beuche, W."],["dc.contributor.author","Yushchenko, M."],["dc.contributor.author","Mader, M."],["dc.contributor.author","Maliszewska, M."],["dc.contributor.author","Felgenhauer, K."],["dc.contributor.author","Weber, F."],["dc.date.accessioned","2018-11-07T11:00:16Z"],["dc.date.available","2018-11-07T11:00:16Z"],["dc.date.issued","2000"],["dc.description.abstract","Matrix metalloproteinase-9 (MMP-9) and its specific inhibitor, tissue inhibitor of matrix metalloproteinase-1 (TIMP-1), were analysed by enzyme-linked immunosorbent assay (ELISA) and by zymography in serum and cerebrospinal fluid (CSF) of patients with amyotrophic lateral sclerosis (ALS). In contrast to patients with inflammatory diseases, MMP-9 levels were not elevated in CSF of ALS patients. In serum, however, compared to healthy donors, MMP-9 was significantly (p=0.0003) increased up to levels as high as those of viral meningoencephalitis (VM) or bacterial meningitis. (BM) patients. MMP-9 levels remained elevated during long-term observation of ALS patients. In the absence of an inflammatory response, the results indicate that the increase of MMP-9 in serum of ALS patients might be caused by upregulation of MMP-9 in denervated muscles or in degenerating peripheral nerves following motor neurone loss. NeuroReport 11:3419-3422 (C) 2000 Lippincott Williams & Wilkins."],["dc.identifier.doi","10.1097/00001756-200011090-00003"],["dc.identifier.isi","000165301600003"],["dc.identifier.pmid","11095490"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/50885"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Lippincott Williams & Wilkins"],["dc.relation.issn","0959-4965"],["dc.title","Matrix metalloproteinase-9 is elevated in serum of patients with amyotrophic lateral sclerosis"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","331"],["dc.bibliographiccitation.issue","7"],["dc.bibliographiccitation.journal","DMW - Deutsche Medizinische Wochenschrift"],["dc.bibliographiccitation.lastpage","334"],["dc.bibliographiccitation.volume","127"],["dc.contributor.author","Poser, Sigrid"],["dc.contributor.author","Zerr, I."],["dc.contributor.author","Felgenhauer, K."],["dc.date.accessioned","2018-11-07T10:31:54Z"],["dc.date.available","2018-11-07T10:31:54Z"],["dc.date.issued","2002"],["dc.identifier.doi","10.1055/s-2002-20153"],["dc.identifier.isi","000173968100006"],["dc.identifier.pmid","11845390"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/44219"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Georg Thieme Verlag Kg"],["dc.relation.issn","0012-0472"],["dc.title","New variant Creutzfeldt-Jakob disease"],["dc.type","review"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.journal","Deutsches Ärzteblatt"],["dc.bibliographiccitation.volume","33"],["dc.contributor.author","Otto, Markus"],["dc.contributor.author","Zerr, Inga"],["dc.contributor.author","Wiltfang, Jens"],["dc.contributor.author","Weber, Thomas"],["dc.contributor.author","Kretzschmar, H."],["dc.contributor.author","Poser, Sigrid"],["dc.contributor.author","Felgenhauer, K."],["dc.date.accessioned","2017-11-21T10:05:36Z"],["dc.date.available","2017-11-21T10:05:36Z"],["dc.date.issued","1999"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/10128"],["dc.language.iso","de"],["dc.notes.status","zu prüfen"],["dc.title","Laborchemische Verfahren in der Differentialdiagnose der Creutzfeldt-Jakob-Krankheit"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","244"],["dc.bibliographiccitation.issue","1-2"],["dc.bibliographiccitation.journal","Journal of Neuroimmunology"],["dc.bibliographiccitation.lastpage","251"],["dc.bibliographiccitation.volume","110"],["dc.contributor.author","Yushchenko, M."],["dc.contributor.author","Weber, F."],["dc.contributor.author","Mader, M."],["dc.contributor.author","Scholl, U."],["dc.contributor.author","Maliszewska, M."],["dc.contributor.author","Tumani, Hayrettin"],["dc.contributor.author","Felgenhauer, K."],["dc.contributor.author","Beuche, W."],["dc.date.accessioned","2018-11-07T09:14:24Z"],["dc.date.available","2018-11-07T09:14:24Z"],["dc.date.issued","2000"],["dc.description.abstract","Matrix metalloproteinase-9 (MMP-9) was investigated by enzyme-linked immunosorbent assay (ELISA) and zymography in III paired CSF and serum samples from patients with various neurological disorders. In 20 patients with blood-brain barrier (BBB) impairment but normal CSF cell count, elevated levels of MMP-9 were not observed by ELISA measurement. Another 11 patients characterized in the same way, exhibited only slightly increased MMP-9 levels. In contrast, in 12 patients with intact BBB but elevated CSF cell count, MMP-9 was increased too. It was shown by the more sensitive zymography that MMP-9 increased if CSF cell count exceeded five cells per mul. Spearman rank statistics revealed that MMP-9 concentration in CSF correlated with CSF cell count (r=0.755; P<0.0001), but not with CSF/serum albumin ratio (Q(AIb)) (r=0.212; P=0.057), a measure for BBB impairment, Moreover, the CSF/serum MMP-9 ratio (Q(MMP-9)) did not correlate with Q(AIb)(r=0.192; P=0.100). By use of a Boyden chamber, in which granulocytes migrated through a reconstituted basement membrane, it was demonstrated that the MMP-9 concentration in the lower chamber correlated very significantly with the number of accumulated cells (r(2)=0.7692; P<0.0001). The meaning of the increase of MMP-9 in CSF is critically discussed. (C) 2000 Elsevier Science B.V. All rights reserved."],["dc.identifier.doi","10.1016/S0165-5728(00)00339-8"],["dc.identifier.isi","000090030800028"],["dc.identifier.pmid","11024556"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/27400"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Elsevier Science Bv"],["dc.relation.issn","0165-5728"],["dc.title","Matrix metalloproteinase-9 (MMP-9) in human cerebrospinal fluid (CSF): elevated levels are primarily related to CSF cell count"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","176"],["dc.bibliographiccitation.issue","1-2"],["dc.bibliographiccitation.journal","Journal of Neuroimmunology"],["dc.bibliographiccitation.lastpage","181"],["dc.bibliographiccitation.volume","115"],["dc.contributor.author","Polak, T."],["dc.contributor.author","Schlaf, G."],["dc.contributor.author","Scholl, U."],["dc.contributor.author","Krome-Cesar, C."],["dc.contributor.author","Mader, M."],["dc.contributor.author","Felgenhauer, K."],["dc.contributor.author","Weber, F."],["dc.date.accessioned","2018-11-07T09:10:31Z"],["dc.date.available","2018-11-07T09:10:31Z"],["dc.date.issued","2001"],["dc.description.abstract","Although multiple sclerosis (MS) is considered primarily as a demyelinating disease, neuronal damage is abundant and correlates with the neurological deficit. Therefore, we investigated the frequency and characteristics of human T cells specific for synapsin-a neuronal protein highly conserved among species. Synapsin specific T cell responses were detected at a frequency similar to that of MBP specific T cells in MS patients, one patient with acute demyelinating encephalomyelitis (ADEM) and controls. Long-term T cell lines specific for synapsin exhibited a CD3(+), CD4(+), CD8(-) phenotype and produced high amounts of tumor-necrosis-factor-alpha (TNF-alpha) and interferon-gamma (IFN-gamma) after antigen specific stimulation, whereas lymphotoxin (LT), interleukin-4 (IL-4) and interleukin-10 (IL-10) were detectable in smaller quantities. (C) 2001 Elsevier Science B.V. All rights reserved."],["dc.identifier.doi","10.1016/S0165-5728(01)00251-X"],["dc.identifier.isi","000167946400020"],["dc.identifier.pmid","11282168"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/26509"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Elsevier Science Bv"],["dc.relation.issn","0165-5728"],["dc.title","Characterization of the human T cell response against the neuronal protein synapsin in patients with multiple sclerosis"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","75"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Epilepsy Research"],["dc.bibliographiccitation.lastpage","82"],["dc.bibliographiccitation.volume","36"],["dc.contributor.author","Steinhoff, Bernhard J."],["dc.contributor.author","Tumani, Hayrettin"],["dc.contributor.author","Otto, Markus"],["dc.contributor.author","Mursch, Kay"],["dc.contributor.author","Wiltfang, Jens"],["dc.contributor.author","Herrendorf, Gregor"],["dc.contributor.author","Bittermann, Hans-Joachim"],["dc.contributor.author","Felgenhauer, Klaus"],["dc.contributor.author","Paulus, Walter"],["dc.contributor.author","Markakis, Evangelos"],["dc.date.accessioned","2017-09-07T11:44:24Z"],["dc.date.available","2017-09-07T11:44:24Z"],["dc.date.issued","2002"],["dc.description.abstract","In the brain, S100 protein and neuron-specific enolase (NSE) are mainly found in glial cells and neurons, respectively. We investigated concentrations of S100 protein and NSE in cisternal cerebrospinal fluid obtained during implantation of foramen ovale electrodes in eight patients with temporal lobe epilepsy (TLE). In addition, the meningeal markers cystatin-C and β-trace as well as total protein were measured. Patients with trigeminal neuralgia (TN) undergoing glycerol rhizotomy served as controls. S100 protein and NSE levels ipsilateral to the site of seizure onset were significantly higher than in TN. Contralateral TLE values were also markedly but not significantly elevated. The meningeal markers cystatin-C and β-trace protein as well as total protein did not differ in TLE and TN. We conclude that interictal temporal lobe dysfunction corresponds with neuronal and glial marker elevations in the extracellular space and that site-specific elevations may predict the site of seizure origin biochemically."],["dc.identifier.doi","10.1016/s0920-1211(99)00026-1"],["dc.identifier.gro","3151649"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/8466"],["dc.language.iso","en"],["dc.notes.status","final"],["dc.notes.submitter","chake"],["dc.relation.issn","0920-1211"],["dc.title","Cisternal S100 protein and neuron-specific enolase are elevated and site-specific markers in intractable temporal lobe epilepsy"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dc.type.peerReviewed","no"],["dspace.entity.type","Publication"]]