Schäfer, Katrin

[["dc.bibliographiccitation.firstpage","700"],["dc.bibliographiccitation.issue","8"],["dc.bibliographiccitation.journal","Microcirculation"],["dc.bibliographiccitation.lastpage","710"],["dc.bibliographiccitation.volume","22"],["dc.contributor.author","Czepluch, Frauke S."],["dc.contributor.author","Vogler, Melanie"],["dc.contributor.author","Kuschicke, Hendrik"],["dc.contributor.author","Meier, Julia"],["dc.contributor.author","Gogiraju, Rajinikanth"],["dc.contributor.author","Katschinski, Dörthe M."],["dc.contributor.author","Riggert, Joachim"],["dc.contributor.author","Hasenfuß, Gerd"],["dc.contributor.author","Schaefer, Katrin"],["dc.date.accessioned","2017-09-07T11:43:27Z"],["dc.date.available","2017-09-07T11:43:27Z"],["dc.date.issued","2015"],["dc.description.abstract","Objective: The zinc finger transcription factor KLF4 is known to control diverse EC functions. Methods: The functional role of KLF4 for angiogenesis and its association with CAD was examined in HUVECs and human CECs. Results: In two different angiogenesis assays, siRNA-mediated KLF4 downregulation impaired HUVEC sprouting and network formation. Conversely, KLF4 overexpression increased HUVEC sprouting and network formation. Similar findings were observed after incubation of HUVECs with CdM from KLF4 cDNA-transfected cells, suggesting a role of paracrine factors for mediating angiogenic KLF4 effects. In this regard, VEGF expression was increased in KLF4-overexpressing HUVECs, whereas its expression was reduced in HUVECs transfected with KLF4 siRNA. To examine the relevance of our in vitro findings for human endothelial dysfunction, we analyzed the expression of KLF4 in CECs of patients with stable CAD. Flow cytometry analyses revealed decreased numbers of KLF4-positive CECs in peripheral blood from CAD patients compared to healthy controls. Conclusions: Our findings suggest that KLF4 may represent a potential biomarker for EC dysfunction. In the future, (therapeutic) modulation of KLF4 may be useful in regulating EC function during vascular disease processes."],["dc.identifier.doi","10.1111/micc.12226"],["dc.identifier.gro","3141793"],["dc.identifier.isi","000365387200003"],["dc.identifier.pmid","26214161"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/1135"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.eissn","1549-8719"],["dc.relation.issn","1073-9688"],["dc.title","Circulating Endothelial Cells Expressing the Angiogenic Transcription Factor Kruppel-Like Factor 4 are Decreased in Patients with Coronary Artery Disease"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.issue","18"],["dc.bibliographiccitation.journal","Circulation"],["dc.bibliographiccitation.volume","118"],["dc.contributor.author","Dallas, Claudia"],["dc.contributor.author","Lankeit, Mareike K."],["dc.contributor.author","Puls, Miriam"],["dc.contributor.author","Schaefer, Katrin"],["dc.contributor.author","Hasenfuß, Gerd"],["dc.contributor.author","Konstantinides, Stavros V."],["dc.date.accessioned","2018-11-07T11:09:52Z"],["dc.date.available","2018-11-07T11:09:52Z"],["dc.date.issued","2008"],["dc.format.extent","S621"],["dc.identifier.isi","000262104501728"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/53094"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Lippincott Williams & Wilkins"],["dc.publisher.place","Philadelphia"],["dc.relation.conference","81st Annual Scientific Session of the American-Heart-Association"],["dc.relation.eventlocation","New Orleans, LA"],["dc.relation.issn","0009-7322"],["dc.title","Heart-Type Fatty Acid-Binding Protein Predicts Outcome In Normotensive Patients With Pulmonary Embolism"],["dc.type","conference_abstract"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","515"],["dc.bibliographiccitation.issue","5"],["dc.bibliographiccitation.journal","Circulation"],["dc.bibliographiccitation.lastpage","525"],["dc.bibliographiccitation.volume","116"],["dc.contributor.author","Knoell, Ralph"],["dc.contributor.author","Postel, Ruben"],["dc.contributor.author","Wang, Jianming"],["dc.contributor.author","Kraetzner, Ralph"],["dc.contributor.author","Hennecke, Gerrit"],["dc.contributor.author","Vacaru, Andrei M."],["dc.contributor.author","Vakeel, Padmanabhan"],["dc.contributor.author","Schubert, Cornelia"],["dc.contributor.author","Murthy, Kenton"],["dc.contributor.author","Rana, Brinda K."],["dc.contributor.author","Kube, Dieter"],["dc.contributor.author","Knoell, Gudrun"],["dc.contributor.author","Schaefer, Katrin"],["dc.contributor.author","Hayashi, Takeharu"],["dc.contributor.author","Holm, Torbjorn"],["dc.contributor.author","Kimura, Akinori"],["dc.contributor.author","Schork, Nicholas"],["dc.contributor.author","Toliat, Mohammad Reza"],["dc.contributor.author","Nürnberg, Peter"],["dc.contributor.author","Schultheiss, Heinz-Peter"],["dc.contributor.author","Schaper, Wolfgang"],["dc.contributor.author","Schaper, Jutta"],["dc.contributor.author","Bos, Erik"],["dc.contributor.author","Hertog, Jeroen den"],["dc.contributor.author","van Eeden, Fredericus J. M."],["dc.contributor.author","Peters, Peter J."],["dc.contributor.author","Hasenfuß, Gerd"],["dc.contributor.author","Chien, Kenneth R."],["dc.contributor.author","Bakkers, Jeroen"],["dc.date.accessioned","2017-09-07T11:49:27Z"],["dc.date.available","2017-09-07T11:49:27Z"],["dc.date.issued","2007"],["dc.description.abstract","Background - Extracellular matrix proteins, such as laminins, and endothelial cells are known to influence cardiomyocyte performance; however, the underlying molecular mechanisms remain poorly understood. Methods and Results - We used a forward genetic screen in zebrafish to identify novel genes required for myocardial function and were able to identify the lost-contact (loc) mutant, which encodes a nonsense mutation in the integrin-linked kinase ( ilk) gene. This loc/ilk mutant is associated with a severe defect in cardiomyocytes and endothelial cells that leads to severe myocardial dysfunction. Additional experiments revealed the epistatic regulation between laminin-alpha 4 (Lama4), integrin, and Ilk, which led us to screen for mutations in the human ILK and LAMA4 genes in patients with severe dilated cardiomyopathy. We identified 2 novel amino acid residue - altering mutations (2828C > T [Pro943Leu] and 3217C > T [Arg1073X]) in the integrin-interacting domain of the LAMA4 gene and 1 mutation (785C > T [Ala262Val]) in the ILK gene. Biacore quantitative protein/protein interaction data, which have been used to determine the equilibrium dissociation constants, point to the loss of integrin-binding capacity in case of the Pro943Leu (K-d = 5 +/- 3 mu mol/L) and Arg1073X LAMA4 (K-d=1 +/- 0.2 mu mol/L) mutants compared with the wild-type LAMA4 protein (K-d=440 +/- 20nmol/L). Additional functional data point to the loss of endothelial cells in affected patients as a direct consequence of the mutant genes, which ultimately leads to heart failure. Conclusions - This is the first report on mutations in the laminin, integrin, and ILK system in human cardiomyopathy, which has consequences for endothelial cells as well as for cardiomyocytes, thus providing a new genetic basis for dilated cardiomyopathy in humans."],["dc.identifier.doi","10.1161/CIRCULATIONAHA.107.689984"],["dc.identifier.gro","3143464"],["dc.identifier.isi","000248456000009"],["dc.identifier.pmid","17646580"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/981"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.issn","0009-7322"],["dc.title","Laminin-alpha 4 and integrin-linked kinase mutations cause human cardiomyopathy via simultaneous defects in cardiomyocytes and endothelial cells"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","144"],["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","Journal of Internal Medicine"],["dc.bibliographiccitation.lastpage","154"],["dc.bibliographiccitation.volume","275"],["dc.contributor.author","Czepluch, Frauke S."],["dc.contributor.author","Kuschicke, Hendrik"],["dc.contributor.author","Dellas, Claudia"],["dc.contributor.author","Riggert, Joachim"],["dc.contributor.author","Hasenfuß, Gerd"],["dc.contributor.author","Schaefer, Katrin"],["dc.date.accessioned","2017-09-07T11:46:53Z"],["dc.date.available","2017-09-07T11:46:53Z"],["dc.date.issued","2014"],["dc.description.abstract","BackgroundMonocytes and platelets are important cellular mediators of atherosclerosis. Human monocytes can be divided into CD14(++)CD16(-), CD14(++)CD16(+) and CD14(+)CD16(++) cells, which differ in their functional properties. The aim of this study was to examine monocyte subset distribution, monocyte-platelet aggregate (MPA) formation and expression of CCR5, the receptor of the platelet-derived chemokine CCL5, and to determine whether these parameters are altered in individuals with coronary atherosclerosis. MethodsPeripheral blood cells from 64 healthy blood donors (HBDs) and 60 patients with stable coronary artery disease (CAD) were stained with antibodies against CD14, CD16, CD42b and CCR5 and analysed by flow cytometry. Circulating CCL5 levels were determined using an enzyme-linked immunosorbent assay. ResultsIn patients with CAD, the relative proportion of the CD14(++)CD16(-) monocyte subset was elevated (P<0.05) and of the CD14(+)CD16(++) subset was reduced (P<0.001) compared with the HBD group. Furthermore, MPA formation significantly increased in patients with CAD in all three monocyte subsets. In both study groups, the majority of CCR5(+) cells was detected in CD14(++)CD16(+) monocytes (P<0.001 versus CD14(++)CD16(-) and CD14(+)CD16(++)), although the CCR5(+) monocyte number was reduced in patients with CAD (CD14(++)CD16(-)/CD14(+)CD16(++), P<0.001; CD14(++)CD16(+), P<0.05) compared with the HBD group, particularly in those who were not taking statins. Ex vivo incubation of monocytes from HBDs with plasma from patients with CAD also decreased CCR5(+) expression (P<0.05 versus plasma from HBDs). Serum CCL5 levels were similar in both groups. ConclusionsThe increased monocyte-platelet cross-talk in patients with CAD might have contributed to atherosclerosis progression. The decreased CCR5(+) monocyte numbers in patients with CAD could have resulted from CCR5(+) cell recruitment into atherosclerotic lesions or CCR5 downregulation in response to circulating factors."],["dc.identifier.doi","10.1111/joim.12145"],["dc.identifier.gro","3142194"],["dc.identifier.isi","000329764500006"],["dc.identifier.pmid","24118494"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/5577"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10 / Funder: University Medical Center Gottingen"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.eissn","1365-2796"],["dc.relation.issn","0954-6820"],["dc.title","Increased proatherogenic monocyte-platelet cross-talk in monocyte subpopulations of patients with stable coronary artery disease"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","857"],["dc.bibliographiccitation.issue","5"],["dc.bibliographiccitation.journal","Thrombosis and Haemostasis"],["dc.bibliographiccitation.lastpage","864"],["dc.bibliographiccitation.volume","95"],["dc.contributor.author","Hecke, A."],["dc.contributor.author","Brooks, H"],["dc.contributor.author","Meryet-Figuiere, M"],["dc.contributor.author","Minne, S."],["dc.contributor.author","Konstantinides, Stavros"],["dc.contributor.author","Hasenfuß, Gerd"],["dc.contributor.author","Lebleu, B."],["dc.contributor.author","Schäfer, Katrin"],["dc.date.accessioned","2017-09-07T11:53:05Z"],["dc.date.available","2017-09-07T11:53:05Z"],["dc.date.issued","2006"],["dc.description.abstract","Clinical as well as experimental evidence suggests that vascular overexpression of plasminogen activator inhibitor (PAI)-1, the primary physiological inhibitor of both urokinase and tissue-type plasminogen activator, may be involved in the pathophysiology of atherosclerosis and cardiovascular disease. We investigated the feasibility, efficacy and functional effects of PAI-1 gene silencing in human vascular endothelial cells using small interfering RNA. Double-stranded 21 bp-RNA molecules targeted at sequences within the human PAI-1 gene were constructed. Successful siRNA transfection of HUVEC was confirmed using fluorescence microscopy and flow cytometry. One of five candidate siRNA sequences reduced PAI-1 mRNA and protein in a concentration- and time-dependent manner. Suppression of PAI-1 mRNA was detected up to 72 hours after transfection. Moreover, siRNA treatment reduced the activity of PAI-1 released from HUVEC,and prevented the oxLDL- or LPS-induced upregulation of PAI-1 secretion. Importantly, siRNA treatment did not affect the expression of other endothelial-cell markers. Moreover, downregulation of PAI-1 significantly enhanced the ability of endothelial cells to adhere to vitronectin,and this effect could be reversed upon addition of recombinant PAI-1. SiRNA-mediated reduction of PAI-1 expression may be a promising strategy for dissecting the effects of PAI-1 on vascular homeostasis."],["dc.identifier.doi","10.1160/TH05-08-0569"],["dc.identifier.gro","3143701"],["dc.identifier.isi","000237718100018"],["dc.identifier.pmid","16676078"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/1244"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.issn","0340-6245"],["dc.title","Successful silencing of plasminogen activator inhibitor-I in human vascular enclothelial cells using small interfering RNA"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","996"],["dc.bibliographiccitation.issue","5"],["dc.bibliographiccitation.journal","Thrombosis and Haemostasis"],["dc.bibliographiccitation.lastpage","1003"],["dc.bibliographiccitation.volume","111"],["dc.contributor.author","Dellas, Claudia"],["dc.contributor.author","Tschepe, Merle"],["dc.contributor.author","Seeber, Valerie"],["dc.contributor.author","Zwiener, Isabella"],["dc.contributor.author","Kuhnert, Katherina"],["dc.contributor.author","Schaefer, Katrin"],["dc.contributor.author","Hasenfuß, Gerd"],["dc.contributor.author","Konstantinides, Stavros"],["dc.contributor.author","Lankeit, Mareike"],["dc.date.accessioned","2017-09-07T11:46:17Z"],["dc.date.available","2017-09-07T11:46:17Z"],["dc.date.issued","2014"],["dc.description.abstract","We tested whether heart-type fatty acid binding protein (H-FABP) measured by a fully-automated immunoturbidimetric assay in comparison to ELISA provides additive prognostic value in patients with pulmonary embolism (PE), and validated a fast prognostic score in comparison to the ESC risk prediction model and the simplified Pulmonary Embolism Severity Index (sPESI). We prospectively examined 271 normotensive patients with PE; of those, 20 (7%) had an adverse 30-day outcome. H-FABP levels determined by immunoturbidimetry were higher (median, 5.2 [IQR; 2.7-9.8] ng/ml) than those by ELISA (2.9 [1.1-5.4] ng/ml), but Bland-Altman plot demonstrated a good agreement of both assays. The area under the curve for H-FABP was greater for immunoturbidimetry than for ELISA (0.82 [0.74-0.91] vs 0.78 [0.68-0.89]; P=0.039). H-FABP measured by immunoturbidimetry (but not by ELISA) provided additive prognostic information to other predictors of 30-day outcome (OR, 12.4 [95% CI, 1.6-97.6]; P=0.017).When H-FABP determined by immunoturbidimetry was integrated into a novel prognostic score (H-FABP, Syncope, and Tachycardia; FAST score), the score provided additive prognostic information by multivariable analysis (OR, 14.2 [3.9-51.4]; p<0.001; c-index, 0.86) which were superior to information obtained by the ESC model(c-index, 0.62; net reclassification improvement (NRI), 0.39 [0.21-0.56]; P<0.001) or the sPESI (c-index, 0.68; NRI, 0.24 [0.05-0.43]; P=0.012). In conclusion, determination of H-FABP by immunoturbidimetry provides prognostic information superior to that of ELISA and, if integrated in the FAST score, appears more suitable to identify patients with an adverse 30-day outcome compared to the ESC model and sPESI."],["dc.identifier.doi","10.1160/TH13-08-0663"],["dc.identifier.gro","3142135"],["dc.identifier.isi","000335541500025"],["dc.identifier.pmid","24477222"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/4933"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.publisher","Schattauer Gmbh-verlag Medizin Naturwissenschaften"],["dc.relation.issn","0340-6245"],["dc.title","A novel H-FABP assay and a fast prognostic score for risk assessment of normotensive pulmonary embolism"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","220"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Thrombosis and Haemostasis"],["dc.bibliographiccitation.lastpage","227"],["dc.bibliographiccitation.volume","98"],["dc.contributor.author","Dellas, Claudia"],["dc.contributor.author","Schremmer, Carmen"],["dc.contributor.author","Hasenfuß, Gerd"],["dc.contributor.author","Konstantinides, Stavros V."],["dc.contributor.author","Schaefer, Katrin"],["dc.date.accessioned","2017-09-07T11:49:27Z"],["dc.date.available","2017-09-07T11:49:27Z"],["dc.date.issued","2007"],["dc.description.abstract","Urokinase plasminogen activator (uPA) is strongly expressed in atherosclerotic lesions, but the overall effect of the protease on plaque composition and growth remains controversial. In the present study, apolipoprotein E-deficient (apoE(-/-)) mice were intercrossed with mice which were lacking the uPA gene (double-knockout; DKO). In ferric chloride-induced carotid artery lesions in chow-fed mice, uPA deficiency increased neointimal size (P=0.015) and luminal stenosis (P=0.014), while reducing media thickness (P=0.002). A lack of uPA also increased the size of and the luminal obstruction from atherosclerotic plaques at the coronary and brachiocephalic arteries of apoE(-/-) mice. Plaques were characterised by a higher fibrinogen/fibrin content and a decrease in cellularity and collagen content. When apoE(-/-) and DKO mice were analysed as a single group, a significant-correlation was found between the (x-actin (smooth muscle cell) and collagen content of atherosclerotic lesions (r = 0.554; P < 0.05), and a negative correlation existed between the a-actin and fibrin/fibrinogen immunopositive area (r = -0.79 1; P < 0.001). Further analysis of brachiocephalic atherosclerosis, a predilection site for plaque rupture in the apoE(-/-) mouse, revealed signs of plaque vulnerability, including a reduced cap-to-intima ratio (0.21 +/- 0.04 vs. 0.37 +/- 0.05; P=0.03) and more frequent detection of intraplaque haemorrhage (56% vs. 13%; P < 0.01) and buried fibrous caps (1.8 +/- 0.5 vs. 0.5 +/- 0.2; P=0.02) in DKO compared to apoE(-/-) mice. These results indicate that, at least at (patho) physiologic concentrations, uPA is essential for maintaining the cellularity and collagen content and, possibly, the stability of lesions, both by preventing excessive intramural fibrin accumulation and by facilitating cell migration and invasion."],["dc.identifier.doi","10.1160/TH06-09-0508"],["dc.identifier.gro","3143478"],["dc.identifier.isi","000248180700037"],["dc.identifier.pmid","17598016"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/996"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.issn","0340-6245"],["dc.title","Lack of urokinase plasminogen activator promotes progression and instability of atherosclerotic lesions in apolipoprotein E-knockout mice"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.issue","18"],["dc.bibliographiccitation.journal","Circulation"],["dc.bibliographiccitation.volume","120"],["dc.contributor.author","Leifheit, Maren"],["dc.contributor.author","Conrad, Gaby"],["dc.contributor.author","Heide, Nana-Maria"],["dc.contributor.author","Schroeter, Marco"],["dc.contributor.author","Hasenfuß, Gerd"],["dc.contributor.author","Konstantinides, Stavros V."],["dc.contributor.author","Schaefer, Katrin"],["dc.date.accessioned","2018-11-07T11:22:15Z"],["dc.date.available","2018-11-07T11:22:15Z"],["dc.date.issued","2009"],["dc.format.extent","S1151"],["dc.identifier.isi","000271831504246"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/55953"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Lippincott Williams & Wilkins"],["dc.publisher.place","Philadelphia"],["dc.relation.conference","82nd Scientific Session of the American-Heart-Association"],["dc.relation.eventlocation","Orlando, FL"],["dc.relation.issn","0009-7322"],["dc.title","Overexpression of Integrin Beta5 Enhances the Paracrine Angiogenic Properties of Early Outgrowth Endothelial Progenitor Cells via Sire Kinase-Mediated Activation of STAT3"],["dc.type","conference_abstract"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","204"],["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","International Journal of Obesity"],["dc.bibliographiccitation.lastpage","210"],["dc.bibliographiccitation.volume","37"],["dc.contributor.author","Dellas, Claudia"],["dc.contributor.author","Lankeit, Mareike"],["dc.contributor.author","Reiner, Christian"],["dc.contributor.author","Schaefer, Katrin"],["dc.contributor.author","Hasenfuß, Gerd"],["dc.contributor.author","Konstantinides, Stavros"],["dc.date.accessioned","2017-09-07T11:48:18Z"],["dc.date.available","2017-09-07T11:48:18Z"],["dc.date.issued","2013"],["dc.description.abstract","OBJECTIVE: The adipocytokine leptin is an independent cardiovascular risk factor and exerts prothrombotic effects, both in arterial and venous thrombosis. We therefore investigated the relationship between leptin levels and clinical outcome in patients with acute pulmonary embolism (PE). DESIGN: We prospectively studied consecutive patients with confirmed acute PE admitted at the University Hospital of Goettingen (Germany) between 2003 and 2009. SUBJECTS: The study subjects were a total of 264 patients with PE (median age, 68 years; interquartile range, 53-75; 60% women; body mass index (BMI) 27 kgm(-2) (24.1-31.2)). Leptin levels were determined by a commercially available enzyme-linked immunosorbent assay. Patients were followed for an adverse 30-day outcome, that is, death, circulatory collapse with need for catecholamines, intubation or resuscitation, and for long-term survival. RESULTS: The median leptin level was 10.1 ng ml(-1) (3.7-25.2). Patients (n = 49; 18.6%) with a complicated 30-day course had significantly lower leptin levels (5.3 ng ml(-1) (1.8-19.7) compared with patients without complications (10.4 ng ml(-1) (4.7-25.5), P = 0.02). When leptin was analyzed as a continuous variable, there was a significant 36% increase in the relative risk for early complications for every decrease in the natural logarithm of leptin by one s.d. (odds ratio (OR) 1.36 (1.06-1.76), P = 0.017), independently of BMI (BMI-adjusted OR, 1.52 (1.13-2.05), P = 0.006). In addition, patients within the lowest leptin tertile had a 2.8- and 2.3-fold increased risk for 30-day-complications, compared with those in the middle (P = 0.011) and high tertile (P = 0.030), and a worse probability of long-term survival (log-rank; P = 0.018). CONCLUSION: Low plasma leptin concentration is a predictor for a complicated course and high mortality in patients with acute PE. This association is independent of known factors affecting leptin levels, including gender and obesity. International Journal of Obesity (2013) 37, 204-210; doi:10.1038/ijo.2012.36; published online 20 March 2012"],["dc.identifier.doi","10.1038/ijo.2012.36"],["dc.identifier.gro","3142393"],["dc.identifier.isi","000316932100008"],["dc.identifier.pmid","22430305"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/7786"],["dc.notes.intern","WoS Import 2017-03-10 / Funder: University of Goettingen (Heidenreich von Siebold-Programm)"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.publisher","Nature Publishing Group"],["dc.relation.issn","0307-0565"],["dc.title","BMI-independent inverse relationship of plasma leptin levels with outcome in patients with acute pulmonary embolism"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.journal","European Heart Journal"],["dc.bibliographiccitation.volume","33"],["dc.contributor.author","Lankeit, Mareike K."],["dc.contributor.author","Kuhnert, K."],["dc.contributor.author","Stuebing, M."],["dc.contributor.author","Schaefer, K."],["dc.contributor.author","Hasenfuß, Gerd"],["dc.contributor.author","Konstantinides, Stavros V."],["dc.contributor.author","Dellas, Claudia"],["dc.date.accessioned","2018-11-07T09:07:23Z"],["dc.date.available","2018-11-07T09:07:23Z"],["dc.date.issued","2012"],["dc.format.extent","412"],["dc.identifier.isi","000308012403272"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/25785"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Oxford Univ Press"],["dc.publisher.place","Oxford"],["dc.relation.eventlocation","Munchen, GERMANY"],["dc.relation.issn","0195-668X"],["dc.title","Risk stratification of non-high-risk pulmonary embolism by the use of a novel rapid immunoturbidimetric H-FABP assay"],["dc.type","conference_abstract"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]