Schäfer, Katrin

[["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","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.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"]]

[["dc.bibliographiccitation.firstpage","1063"],["dc.bibliographiccitation.issue","5"],["dc.bibliographiccitation.journal","Thrombosis and Haemostasis"],["dc.bibliographiccitation.lastpage","1071"],["dc.bibliographiccitation.volume","98"],["dc.contributor.author","Dellas, Claudia"],["dc.contributor.author","Schäfer, Katrin"],["dc.contributor.author","Rohm, Ilonka"],["dc.contributor.author","Lankeit, Mareike"],["dc.contributor.author","Leifheit, Maren"],["dc.contributor.author","Loskutoff, David J."],["dc.contributor.author","Hasenfuß, Gerd"],["dc.contributor.author","Konstantinides, Stavros V."],["dc.date.accessioned","2017-09-07T11:49:24Z"],["dc.date.available","2017-09-07T11:49:24Z"],["dc.date.issued","2007"],["dc.description.abstract","Leptin enhances agonist-induced platelet aggregation, and human platelets have been reported to express the leptin receptor. However, the pathways and mediators lying downstream of leptin binding to platelets remain, with few exceptions, unknown. In the present study, we sought to gain further insight into the possible role of leptin as a platelet agonist. Stimulation of platelets with leptin promoted thromboxane generation and activation of alpha(IIb)beta(3), as demonstrated by PAC-I binding. Furthermore, it increased the adhesion to immobilised fibrinogen (p < 0.001) and induced cytoskeletal rearrangement of both platelets and Meg01 cells. Leptin time- and dose-dependently phosphorylated the intracellular signalling molecules JAK2 and STAT3, although the importance of STAT3 for leptin-induced platelet activation remains to be determined. Important intracellular mediators and pathways activated by leptin downstream of JAK2 were found to include phosphaticlylinositol-3 kinase, phospholipase C gamma 2 and protein kinase C,as well as the p38 MAP kinase-phospholipase A(2) axis. Accordingly, incubation with the specific inhibitors AG490, Ly294002, U73122, and SB203580 prevented leptin-mediated platelet activation. These results help delineate biologically relevant leptin signalling pathways in platelets and may improve our understanding of the mechanisms linking hyperleptinaemia to the increased thrombosis risk in human obesity."],["dc.identifier.doi","10.1160/TH07-03-0213"],["dc.identifier.gro","3143420"],["dc.identifier.isi","000251064400021"],["dc.identifier.pmid","18000612"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/932"],["dc.notes.intern","WoS Import 2017-03-10 / Funder: NCRR NIH HHS [M01 RR00833]; NHLBI NIH HHS [HL75736]"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.issn","0340-6245"],["dc.title","Leptin signalling and leptin-mediated activation of human platelets: Importance of JAK2 and the phospholipases C gamma 2 and A(2)"],["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","31"],["dc.contributor.author","Lankeit, Mareike K."],["dc.contributor.author","Friesen, D."],["dc.contributor.author","Hasenfuß, Gerd"],["dc.contributor.author","Schaefer, K."],["dc.contributor.author","Konstantinides, Stavros V."],["dc.contributor.author","Dellas, Claudia"],["dc.date.accessioned","2018-11-07T08:39:21Z"],["dc.date.available","2018-11-07T08:39:21Z"],["dc.date.issued","2010"],["dc.format.extent","627"],["dc.identifier.isi","000281531904141"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/18974"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Oxford Univ Press"],["dc.publisher.place","Oxford"],["dc.relation.eventlocation","Stockholm, SWEDEN"],["dc.relation.issn","0195-668X"],["dc.title","Bedside testing for H-FABP is a useful tool for immediate risk stratification of normotensive patients with acute 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","224"],["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","European heart journal"],["dc.bibliographiccitation.lastpage","229"],["dc.bibliographiccitation.volume","28"],["dc.contributor.author","Puls, Miriam"],["dc.contributor.author","Dellas, Claudia"],["dc.contributor.author","Lankeit, Mareike"],["dc.contributor.author","Olschewski, Manfred"],["dc.contributor.author","Binder, Lutz"],["dc.contributor.author","Geibel, Anette"],["dc.contributor.author","Reiner, Christian"],["dc.contributor.author","Schaefer, Katrin"],["dc.contributor.author","Hasenfuß, Gerd"],["dc.contributor.author","Konstantinides, Stavros"],["dc.date.accessioned","2017-09-07T11:49:52Z"],["dc.date.available","2017-09-07T11:49:52Z"],["dc.date.issued","2007"],["dc.description.abstract","Aims We investigated the value of a novel early biomarker, heart-type fatty acid-binding protein (H-FABP), in risk stratification of patients with acute pulmonary embolism (PE). Methods and results We prospectively included 107 consecutive patients with confirmed PE. The endpoints were (i) PE-related death or major complications and (ii) overall 30-day mortality. Overall, 29 patients (27%) had abnormal (> 6 ng/mL) H-FABP levels at presentation. Of those, 12 (41%) had a complicated course, whereas all patients with normal baseline H-FABP had a favourable 30-day outcome (OR, 71.45; P < 0.0001). At multivariable analysis, H-FABP (P < 0.0001), but not cardiac troponin T (P = 0.13) or N-terminal pro-brain natriuretic peptide (P = 0.36), predicted an adverse outcome. Evaluation of a strategy combining biomarker testing with echocardiography revealed that patients with a negative H-FABP test had an excellent prognosis regardless of echocardiographic findings. In contrast, patients with a positive H-FABP test had a complication rate of 23.1% even in the presence of a normal echocardiogram, and this rose to 57.1% if echocardiography also demonstrated right ventricular dysfunction (OR vs. a negative H-FABP test, 5.6 and 81.4, respectively). Conclusion H-FABP is a promising early indicator of right ventricular injury and dysfunction in acute PE. It may help optimize risk stratification algorithms and treatment strategies."],["dc.identifier.doi","10.1093/eurheartj/ehl405"],["dc.identifier.gro","3143555"],["dc.identifier.isi","000244259600020"],["dc.identifier.pmid","17127709"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/1082"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.publisher","Oxford Univ Press"],["dc.relation.issn","0195-668X"],["dc.title","Heart-type fatty acid-binding protein permits early risk stratification of 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","1254"],["dc.bibliographiccitation.issue","6"],["dc.bibliographiccitation.journal","Arteriosclerosis, Thrombosis, and Vascular Biology"],["dc.bibliographiccitation.lastpage","1259"],["dc.bibliographiccitation.volume","26"],["dc.contributor.author","Schäfer, Katrin"],["dc.contributor.author","Schroeter, Marco R."],["dc.contributor.author","Dellas, Claudia"],["dc.contributor.author","Puls, Miriam"],["dc.contributor.author","Nitsche, Mirko"],["dc.contributor.author","Weiss, Elisabeth"],["dc.contributor.author","Hasenfuss, Gerd"],["dc.contributor.author","Konstantinides, Stavros V."],["dc.date.accessioned","2017-09-07T11:52:41Z"],["dc.date.available","2017-09-07T11:52:41Z"],["dc.date.issued","2006"],["dc.description.abstract","Objective - To investigate the ability of bone marrow ( BM) - derived cells to modulate neointimal growth after injury by expressing plasminogen activator inhibitor-1 ( PAI-1). Methods and Results - We performed BM transplantation ( BMT) in lethally irradiated wild- type ( WT) and PAI-1-/- mice. Three weeks after carotid injury with ferric chloride, analysis of Y-chromosome DNA expression in the vessel wall of female hosts revealed that 20.8 +/- 6.0% of the cells in the neointima and 37.6 +/- 5.7% of those in the media were of BM origin. Lack of PAI-1 in either the host or the donor cells did not affect recruitment of BM-derived cells into sites of vascular injury. The neointima consisted predominantly of smooth muscle cells, and a proportion of these cells expressed PAI-1. Overall, lack of PAI-1 was associated with enhanced neointimal formation. However, importantly, BMTWT -> PAI-1-/- mice exhibited reduced neointimal area ( P = 0.05) and luminal stenosis ( P = 0.04) compared with BMTPAI-1-/--> PAI-1-/- mice. Although PAI-1-expressing cells were shown to be present in BMTWT -> PAI-1-/- lesions, these mice did not exhibit detectable levels of the inhibitor in the circulation, suggesting that local production of PAI-1 by cells in the neointima and media was sufficient to reduce luminal stenosis. Conclusions - PAI-1 from BM-derived cells appears capable of suppressing neointimal growth after vascular injury."],["dc.identifier.doi","10.1161/01.ATV.0000215982.14003.b7"],["dc.identifier.gro","3143681"],["dc.identifier.isi","000237644000012"],["dc.identifier.pmid","16514083"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/1221"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.issn","1079-5642"],["dc.title","Plasminogen Activator Inhibitor-1 From Bone Marrow–Derived Cells Suppresses Neointimal Formation After Vascular Injury in Mice"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1080"],["dc.bibliographiccitation.issue","5"],["dc.bibliographiccitation.journal","Thrombosis and Haemostasis"],["dc.bibliographiccitation.lastpage","1082"],["dc.bibliographiccitation.volume","110"],["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","2017-09-07T11:47:04Z"],["dc.date.available","2017-09-07T11:47:04Z"],["dc.date.issued","2013"],["dc.identifier.doi","10.1160/TH13-05-0367"],["dc.identifier.gro","3142259"],["dc.identifier.isi","000326991900026"],["dc.identifier.pmid","23884216"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/6298"],["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","Atheroprotective Kruppel-like factor 4 is downregulated in monocyte subsets of patients with coronary artery disease"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","letter_note"],["dspace.entity.type","Publication"]]