Kratzin, Hartmut Dieter

[["dc.bibliographiccitation.firstpage","53"],["dc.bibliographiccitation.journal","Mycoses"],["dc.bibliographiccitation.lastpage","56"],["dc.bibliographiccitation.volume","45"],["dc.contributor.author","Ntefidou, M."],["dc.contributor.author","Elsner, C."],["dc.contributor.author","Spreer, Annette"],["dc.contributor.author","Weinstock, N."],["dc.contributor.author","Kratzin, H. D."],["dc.contributor.author","Ruchel, R."],["dc.date.accessioned","2018-11-07T10:33:29Z"],["dc.date.available","2018-11-07T10:33:29Z"],["dc.date.issued","2002"],["dc.description.abstract","Activation of blood coagulation to a varying extent affect the course of domestic invasive mycoses. Upon invasion of blood vessels by Candida or aspergilli, occasionally thrombi are formed, which may cause septic embolism. In the course of mucormycosis (syn. zygomycosis) thrombotic occlusion of afflicted blood vessels and subsequent necrosis of dependent tissue regularly occurs. Coagulation during candidosis or aspergillosis may be triggered by secreted aspartic proteinases which are able to activate factor X as has been shown previously [1, 2]. During mucormycosis, severe blood coagulation apparently is due to paracoagulation of fibrinogen which is triggered by low concentrations of extracellular fungal subtilisin-like proteinase (Arp). The enzyme is also able to inactivate the major inhibitor 4 blood coagulation (antithrombin III). Recent findings on the action of Arp are discussed."],["dc.identifier.isi","000175485200010"],["dc.identifier.pmid","12073564"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/44625"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Wiley-blackwell"],["dc.relation.issn","0933-7407"],["dc.title","Blood coagulation with domestic deep-seated mycoses"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","261"],["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","Proteomics"],["dc.bibliographiccitation.lastpage","269"],["dc.contributor.author","Sussulini, Alessandra"],["dc.contributor.author","Dihazi, Hassan"],["dc.contributor.author","Muller Banzato, Claudio Eduardo"],["dc.contributor.author","Zezzi Arruda, Marco Aurelio"],["dc.contributor.author","Stühmer, Walter"],["dc.contributor.author","Ehrenreich, Hannelore"],["dc.contributor.author","Jahn, Olaf"],["dc.contributor.author","Kratzin, Hartmut D."],["dc.date.accessioned","2017-09-07T11:46:27Z"],["dc.date.available","2017-09-07T11:46:27Z"],["dc.date.issued","2011"],["dc.description.abstract","The molecular basis of bipolar disorder (BD) is still unknown as is the mechanism through which lithium, the therapy of choice, exerts its effects in treatment of BD. So far, no biomarkers exist to facilitate diagnosis of BD or treatment evaluation. To investigate whether BD and its treatment with lithium leaves a characteristic signature in the serum proteome, we used SELDI-TOF MS to analyze individual serum samples from BD patients treated with lithium (BD-plus-Li, n=15) or other drugs (BD-minus-Li, n=10) and from healthy controls (n=15). Interestingly, features of 28 kDa (one peak) and 14 kDa (three peaks) showed a decreased level in the BD-minus-Li group and a level restored to that of the control group in the BD-plus-Li group. To reveal the identity of these features, we subjected pooled serum samples from both BD groups to the 2-D DIGE technology and identified 28 kDa apolipoprotein A-I (apo A-I) and three 14 kDa fragments thereof as upregulated in the BD-plus-Li group. Immunoturbidimetry, a routine clinical assay, verified the characteristic apo A-I signature in individual serum samples. In conclusion, we propose apo A-I as a candidate marker that can visualize response to lithium treatment at the serum protein level."],["dc.identifier.doi","10.1002/pmic.201000371"],["dc.identifier.gro","3150515"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/7288"],["dc.language.iso","en"],["dc.notes.status","zu prüfen"],["dc.title","Apolipoprotein A-I as a candidate serum marker for the response to lithium treatment in bipolar disorder"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dc.type.peerReviewed","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1339"],["dc.bibliographiccitation.issue","4"],["dc.bibliographiccitation.journal","Molecular and Cellular Biology"],["dc.bibliographiccitation.lastpage","1346"],["dc.bibliographiccitation.volume","25"],["dc.contributor.author","Steinacker, Petra"],["dc.contributor.author","Schwarz, P."],["dc.contributor.author","Reim, K."],["dc.contributor.author","Brechlin, P."],["dc.contributor.author","Jahn, O."],["dc.contributor.author","Kratzin, H."],["dc.contributor.author","Aitken, A."],["dc.contributor.author","Wiltfang, J."],["dc.contributor.author","Aguzzi, A."],["dc.contributor.author","Bahn, E."],["dc.contributor.author","Baxter, Helen C."],["dc.contributor.author","Brose, N."],["dc.contributor.author","Otto, M."],["dc.date.accessioned","2017-09-07T11:43:02Z"],["dc.date.available","2017-09-07T11:43:02Z"],["dc.date.issued","2005"],["dc.description.abstract","The diagnosis of sporadic Creutzfeldt-Jakob disease (CJD) is based on typical clinical findings and is supported by a positive 14-3-3 Western blot of cerebrospinal fluid. However, it is not clear whether 14-3-3 indicates general neuronal damage or is of pathophysiological relevance in CJD. The fact that the 14-3-3 isoform spectrum in cerebrospinal fluid does not correspond to that found in the brain points to a regulated process. To investigate a possible role of 14-3-3 proteins in transmissible spongiform diseases, we generated a 14-3-3gamma-deficient mutant mouse line by using a classical knockout strategy. The anatomy and cage behavior of the mutant mice were normal. Western blot analyses of brain homogenates revealed no changes in the protein expression of other 14-3-3 isoforms (epsilon, beta, zeta, and eta). Proteomic analyses of mouse brains by two-dimensional differential gel electrophoresis showed that several proteins, including growth hormone, 1-Cys peroxiredoxin, CCT-zeta, glucose-6-phosphate isomerase, GRP170 precursor, and et-SNAP, were differentially expressed. Mutant and wild-type mice were inoculated either intracerebrally or intraperitoneally with the Rocky Mountain Laboratory strain of scrapie, but no differences were detected in the postinoculation survival rates. These results indicate that 14-3-3gamma is unlikely to play a causal role in CJD and related diseases."],["dc.identifier.doi","10.1128/MCB.25.4.1339-1346.2005"],["dc.identifier.gro","3143900"],["dc.identifier.isi","000226908000010"],["dc.identifier.pmid","15684385"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/1465"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.eissn","1098-5549"],["dc.relation.issn","0270-7306"],["dc.title","Unchanged survival rates of 14-3-3 gamma knockout mice after inoculation with pathological prion protein"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","225"],["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","The International Journal of Biochemistry & Cell Biology"],["dc.bibliographiccitation.lastpage","234"],["dc.bibliographiccitation.volume","32"],["dc.contributor.author","Steinacker, Petra"],["dc.contributor.author","Awni, L. A."],["dc.contributor.author","Becker, S."],["dc.contributor.author","Cole, T."],["dc.contributor.author","Reymann, S."],["dc.contributor.author","Hesse, D."],["dc.contributor.author","Kratzin, H. D."],["dc.contributor.author","Morris-Wortmann, C."],["dc.contributor.author","Schwarzer, C."],["dc.contributor.author","Thinnes, F. P."],["dc.contributor.author","Hilschmann, N."],["dc.date.accessioned","2018-11-07T10:31:09Z"],["dc.date.available","2018-11-07T10:31:09Z"],["dc.date.issued","2000"],["dc.description.abstract","Recent patch-clamp studies have shown that anti-porin antibodies, applied to the external side of excised plasma membrane patches of mammalian astrocytes, close chloride channels that are thought to be engaged in cell volume regulation. Frog oocytes are often used to study this basic cell function. Here we document the localisation of endogenous porin voltage-dependent anion-selective channels in Xenopus laevis oocyte plasma membranes. In confocal laser microscopy images a disjunctive pattern of fluorescing spots appear about 10 mu m apart. Labelling was prevented by preabsorption of the antibodies with synthetic peptides comprising the epitope of the antigen. Immune-gold marking of oocyte surfaces followed by silver enhancement of the gold particles lead to a plasma membrane labelling corresponding to that obtained by the confocal laser approach. The data suggests the presence of voltage-dependent, anion-selective channels in oocyte plasma membranes. This data should be borne in mind when frog oocytes are used to study the characteristics of endogenous or heterologously expressed ion channels or regulatory proteins. (C) 2000 Elsevier Science Ltd. All rights reserved."],["dc.identifier.doi","10.1016/S1357-2725(99)00124-7"],["dc.identifier.isi","000084963200010"],["dc.identifier.pmid","10687956"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/44035"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Pergamon-elsevier Science Ltd"],["dc.relation.issn","1357-2725"],["dc.title","The plasma membrane of Xenopus laevis oocytes contains voltage-dependent anion-selective porin channels"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","16711"],["dc.bibliographiccitation.issue","20"],["dc.bibliographiccitation.journal","Journal of Biological Chemistry"],["dc.bibliographiccitation.lastpage","16719"],["dc.bibliographiccitation.volume","276"],["dc.contributor.author","Kramer, Michael L."],["dc.contributor.author","Kratzin, H. D."],["dc.contributor.author","Schmidt, B."],["dc.contributor.author","Romer, A."],["dc.contributor.author","Windl, Otto"],["dc.contributor.author","Liemann, S."],["dc.contributor.author","Hornemann, S."],["dc.contributor.author","Kretzschmar, Hans A."],["dc.date.accessioned","2018-11-07T09:03:42Z"],["dc.date.available","2018-11-07T09:03:42Z"],["dc.date.issued","2001"],["dc.description.abstract","The prion protein is known to be a copper-binding protein, but affinity and stoichiometry data for the full-length protein at a physiological pH of 7 were lacking. Furthermore, it was unknown whether only the highly flexible N-terminal segment with its octarepeat region is involved in copper binding or whether the structured C-terminal domain is also involved, Therefore we systematically investigated the stoichiometry and affinity of copper binding to full-length prion protein PrP23-231 and to different N- and C-terminal fragments using electrospray ionization mass spectrometry and fluorescence spectroscopy. Our data indicate that the unstructured N-terminal segment is the cooperative copper-binding domain of the prion protein. The prion protein binds up to five copper(II) ions with half-maximal binding at similar to2 muM. This argues strongly for a direct role of the prion protein in copper metabolism, since it is almost saturated at about 5 muM, and the exchangeable copper Fool concentration in blood is about 8 muM."],["dc.identifier.doi","10.1074/jbc.M006554200"],["dc.identifier.isi","000168730400018"],["dc.identifier.pmid","11278306"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/24953"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Amer Soc Biochemistry Molecular Biology Inc"],["dc.relation.issn","0021-9258"],["dc.title","Prion protein binds copper within the physiological concentration range"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","4357"],["dc.bibliographiccitation.issue","20"],["dc.bibliographiccitation.journal","Proteomics"],["dc.bibliographiccitation.lastpage","4366"],["dc.bibliographiccitation.volume","8"],["dc.contributor.author","Brechlin, Peter"],["dc.contributor.author","Jahn, Olaf"],["dc.contributor.author","Steinacker, Petra"],["dc.contributor.author","Cepek, Lukas"],["dc.contributor.author","Kratzin, Hartmut"],["dc.contributor.author","Lehnert, Stefan"],["dc.contributor.author","Jesse, Sarah"],["dc.contributor.author","Mollenhauer, Brit"],["dc.contributor.author","Kretzschmar, Hans A."],["dc.contributor.author","Wiltfang, Jens"],["dc.contributor.author","Otto, Markus"],["dc.date.accessioned","2018-11-07T11:10:48Z"],["dc.date.available","2018-11-07T11:10:48Z"],["dc.date.issued","2008"],["dc.description.abstract","So far only the detection of 14-3-3 proteins in cerebrospinal fluid (CSF) is included in the diagnostic criteria for sporadic Creutzfeldt-jakob disease (sCJD). However, this assay cannot be used for screening because of the high rate of false positive results in sCJD, and often negative results in variant CJD. To facilitate the differential diagnosis of CJD, we applied 2-D differential gel-electrophoresis (2-D DIGE) as a quantitative proteomic screening system for CSF proteins. We compared 36 patients suffering from sCJD with 30 patients suffering from other neurodegenerative diseases. Sample preparation was optimized in consideration of the fact that CSF is composed of blood- and brain-derived proteins, and an improved 2-D DIGE protocol was established. Using this method in combination with protein identification by MALDI-TOF-MS, several known surrogate markers of sCJD like 14-3-3 protein, neuron-specific enolase, and lactate dehydrogenase were readily identified. Moreover, a not yet identified protein with an approximate molecular mass of 85 kDa was found as marker for sCJD with high diagnostic specificity and sensitivity. We conclude that our proteomic approach is useful to differentiate CJD from other neurodegenerative diseases and expect that CSF-optimized 2-D DIGE will find broad application in the search for other brain derived proteins in CSF."],["dc.identifier.doi","10.1002/pmic.200800375"],["dc.identifier.isi","000260717300021"],["dc.identifier.pmid","18814332"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/53290"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Wiley-Blackwell"],["dc.relation.issn","1615-9861"],["dc.relation.issn","1615-9853"],["dc.title","Cerebrospinal fluid-optimized two-dimensional difference gel electrophoresis (2-D DIGE) facilitates the differential diagnosis of Creutzfeldt-Jakob disease"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","61"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Medical Mycology"],["dc.bibliographiccitation.lastpage","71"],["dc.bibliographiccitation.volume","40"],["dc.contributor.author","Schoen, C."],["dc.contributor.author","Reichard, Utz"],["dc.contributor.author","Monod, Michel"],["dc.contributor.author","Kratzin, H. D."],["dc.contributor.author","Ruchel, R."],["dc.date.accessioned","2018-11-07T10:32:18Z"],["dc.date.available","2018-11-07T10:32:18Z"],["dc.date.issued","2002"],["dc.description.abstract","An extracellular aspartic proteinase (Rmap) from Rhizopus microsporus var. rhizopodiformis was detected in the culture supernatant of a fungal isolate from a case of rhinocerebral mucormycosis (case HA). The proteinase was purified to near homogeneity by ion exchange and affinity chromatography on pepstatin agarose. Based on its N-terminus the RMAP gene was cloned and found to code for 388 amino acids. The preproenzyme has an aminoterminal leader sequence of 65 amino acids, whereas the mature enzyme consists of 323 amino acids. The deduced amino-acid sequence of the preproenzyme was 82% homologous to an extracellular aspartic proteinase of Rhizopus niveus. Low stringency Southern blot analysis of R. microsporus DNA suggested the presence of other homologous genes. Expression of Rmap in Pichia pastoris was achieved, and the recombinant enzyme was active in the yeast culture supernatant. Both enzyme preparations exhibited a similar optimum of activity in the pH 2.5 region. Furthermore, Rmap was shown to activate bovine blood coagulation factor X at slightly acidic pH in vitro. Expression of the proteinase during mycosis was proven by a specific immune response of patient HA."],["dc.identifier.doi","10.1080/mmy.40.1.61.71"],["dc.identifier.isi","000173949300009"],["dc.identifier.pmid","11860014"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/44317"],["dc.language.iso","en"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.relation.issn","1369-3786"],["dc.title","Molecular cloning of an extracellular aspartic proteinase from Rhizopus microsporus and evidence for its expression during infection"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","845"],["dc.bibliographiccitation.issue","7"],["dc.bibliographiccitation.journal","Laboratory Investigation"],["dc.bibliographiccitation.lastpage","856"],["dc.bibliographiccitation.volume","84"],["dc.contributor.author","Tolson, J."],["dc.contributor.author","Bogumil, R."],["dc.contributor.author","Brunst, E."],["dc.contributor.author","Beck, H."],["dc.contributor.author","Elsner, R."],["dc.contributor.author","Humeny, A."],["dc.contributor.author","Kratzin, H."],["dc.contributor.author","Deeg, M."],["dc.contributor.author","Kuczyk, M."],["dc.contributor.author","Mueller, Georg Anton"],["dc.contributor.author","Mueller, C. A."],["dc.contributor.author","Flad, T."],["dc.date.accessioned","2018-11-07T10:47:47Z"],["dc.date.available","2018-11-07T10:47:47Z"],["dc.date.issued","2004"],["dc.description.abstract","The molecular analysis of serum is an important field for the definition of potential diagnostic markers or disease-related protein alterations. Novel proteomic technologies such as the mass spectrometric-based surface-enhanced laser desorption/ionization (SELDI) ProteinChip(R), technique facilitate a rapid and reproducible analysis of such protein mixtures and affords the researcher a new dimension in the search for biomarkers of disease. Here, we have applied this technology to the study of a cohort of serum samples from well-characterized renal cell carcinoma patients for the identification of such proteins by comparison to healthy controls. We detected and characterized haptoglobin 1 a and serum amyloid alpha-1 (SAA-1) as disease related, in addition to an as-yet-unidentified marker of 10.84 kDa. Of particular note is the detection of multiple variants of SAA-1 in multiplex that have not been described in the sera of cancer patients. SAA-1 is detected as full-length protein, des-Arginine and des-Arginine/des-Serine variants at the N terminus by SELDI. In addition, we could also detect a low-abundant variant minus the first five N-terminal amino acids. Such variants may impact the function of the protein. We conclude the technique to be a reproducible, fast and simple mode for the discovery and analysis of marker proteins of disease in serum."],["dc.identifier.doi","10.1038/labinvest.3700097"],["dc.identifier.isi","000222991700004"],["dc.identifier.pmid","15107802"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/48048"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Nature Publishing Group"],["dc.relation.issn","0023-6837"],["dc.title","Serum protein profiling by SELDI mass spectrometry: detection of multiple variants of serum amyloid alpha in renal cancer patients"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]