Correlation of DNA, LPS-binding-protein and CD14 of periodontal microbes and cardiac tissue-preliminary results

2014 ◽  
Vol 62 (S 01) ◽  
Author(s):  
B.C. Danner ◽  
D. Ziebolz ◽  
C. Rost ◽  
J. Schmidt ◽  
R. Waldmann-Beushausen ◽  
...  
Keyword(s):  
Cardiac Tissue ◽  
Binding Protein ◽  
Preliminary Results ◽  
Lps Binding

Periodontal Bacterial DNA and Their Link to Human Cardiac Tissue: Findings of a Pilot Study

2015 ◽  
Vol 66 (01) ◽  
pp. 083-090 ◽  
Author(s):  
Dirk Ziebolz ◽  
Christoph Rost ◽  
Julia Schmidt ◽  
Regina Waldmann-Beushausen ◽  
Friedrich Schöndube ◽  
...  
Keyword(s):  
Pilot Study ◽  
Aortic Valve ◽  
Cardiac Tissue ◽  
Binding Protein ◽  
Myocardial Revascularization ◽  
Tissue Samples ◽  
Bacterial Dna ◽  
Protocol Biopsies ◽  
Human Cardiac Tissue ◽  
Lps Binding

Background The aim of this pilot study was to detect correlations of microbiological DNA, inflammatory proteins, and infection parameters in patients with periodontal disease (PD) and valvular heart disease (VHD). Methods A perioperative comprehensive dental examination for the investigation of periodontal status, including sampling of specific subgingival bacteria, was performed in 10 patients with indication for surgery of aortic valve stenosis with or without concomitant myocardial revascularization. Standard protocol biopsies were taken from right atrium (A), left septal myocardium (M), and aortic valve (V). Eleven periodontal pathogens DNA in oral and cardiac tissue samples (A/M/V) were analyzed using polymerase chain reaction. For cardiac tissue samples, Western blot analysis of LPS-binding protein (LBP), immunohistochemical (IHC) detection of LBP-big42, LPS-binding protein receptor (CD14), and macrophages (CD68), as well as inflammation scoring measurement were performed. Results Periodontitis was present in all patients with severe intensity in 7, moderate in 2 and mild in one patient. Same bacterial DNA was detected in A, M, and V in different distribution, and detection was more often in atrium than in myocardium or valve tissue. Morphological investigation revealed increased extracellular inflammatory cell migration. In IHC markers of LBP, CD68 and CD14 showed positive findings for all patients in atrium and myocardium. Conclusion Our results demonstrate the presence of oral bacterial DNA in human cardiac tissue, as well as inflammatory markers potentially indicating connection of PD and VHD. Further investigation is necessary to confirm these preliminary data.

Kupffer cell activation by LPS is mediated via LPS binding protein and CD14

2001 ◽  
Vol 120 (5) ◽  
pp. A27-A27
Author(s):  
M FAN ◽  
S GOYERT ◽  
A AMINLARI ◽  
R KLEIN ◽  
L STEINSTRAESSER ◽  
...  
Keyword(s):  
Kupffer Cell ◽  
Cell Activation ◽  
Binding Protein ◽  
Lps Binding

Hemoglobin Enhances the Binding of Bacterial Endotoxin to Human Endothelial Cells

1996 ◽  
Vol 76 (02) ◽  
pp. 258-262 ◽  
Author(s):  
Robert I Roth
Keyword(s):  
Endothelial Cells ◽  
Binding Protein ◽  
Bacterial Endotoxin ◽  
Dependent Manner ◽  
Serum Free Medium ◽  
Free Medium ◽  
Human Endothelial Cells ◽  
Serum Factors ◽  
Serum Free ◽  
Lps Binding

SummaryHuman endothelial cells, when incubated with bacterial endotoxin (lipopolysaccharide, LPS), modify their surface in association with prominent production of procoagulant tissue factor (TF) activity. This deleterious biological effect of LPS has been shown previously to be enhanced approximately 10-fold by the presence of hemoglobin (Hb), a recently recognized LPS binding protein that causes disaggregation of LPS and increases the biological activity of LPS in a number of in vitro assays. The present study was performed to test the hypothesis that Hb enhances the LPS-induced procoagulant activity of human umbilical vein endothelial cells (HUVEC) by increasing LPS binding to the cells. The binding of 3H-LPS to HUVEC was determined in the absence or presence of Hb or two other known LPS-binding proteins, human serum albumin (HSA) and IgG. LPS binding was substantially increased in the presence of Hb, in a Hb concentration-dependent manner, but was not increased by HSA or IgG. Hb enhancement of LPS binding was observed in serum-free medium, indicating that there was no additional requirement for any of the serum factors known to participate in the interaction of LPS with cells (e.g., lipopolysaccharide (LPS)-binding protein (LBP) and soluble CD14 (sCD14)). Hb enhancement of LPS binding also was observed in the more physiologic condition of 100% plasma. LPS-induced TF activity was stimulated by Hb, but not by HSA or IgG. In serum-free medium, TF activity was not stimulated under any of the conditions tested. Ultrafiltration of LPS was dramatically increased after incubation with Hb but not with HSA or IgG, suggesting that LPS disaggregation by Hb was responsible for the enhanced binding of LPS to HUVEC and the subsequent stimulation of TF activity.

Kupffer cell activation by LPS is mediated via LPS binding protein and CD14

2001 ◽  
Vol 120 (5) ◽  
pp. A27
Author(s):  
Ming Hui Fan ◽  
Sanna M. Goyert ◽  
Alireza Aminlari ◽  
Richard D. Klein ◽  
Lars Steinstraesser ◽  
...  
Keyword(s):  
Kupffer Cell ◽  
Cell Activation ◽  
Binding Protein ◽  
Lps Binding

scholarly journals Interaction of SP-A (surfactant protein A) with bacterial rough lipopolysaccharide (Re-LPS), and effects of SP-A on the binding of Re-LPS to CD14 and LPS-binding protein

2005 ◽  
Vol 391 (1) ◽  
pp. 115-124 ◽  
Author(s):  
Ignacio García-Verdugo ◽  
Fernando Sánchez-Barbero ◽  
Katrin Soldau ◽  
Peter S. Tobias ◽  
Cristina Casals
Keyword(s):  
Binding Protein ◽  
Protein A ◽  
Fluorescence Analysis ◽  
Surfactant Protein ◽  
Lipid Binding ◽  
Coli Strain ◽  
Surfactant Protein A ◽  
Human Macrophage ◽  
Independent Manner ◽  
Lps Binding

SP-A (surfactant protein A) is a lipid-binding collectin primarily involved in innate lung immunity. SP-A interacts with the bacterial rough LPS (lipopolysaccharide) Re-LPS (Re595 mutant of LPS from Salmonella minnesota), but not with smooth LPS. In the present study, we first examined the characteristics of the interaction of human SP-A with Re-LPS. Fluorescence intensity and anisotropy measurements of FITC-labelled Re-LPS in the presence and absence of SP-A indicated that SP-A bound to Re-LPS in solution in a Ca2+-independent manner, with a dissociation constant of 2.8×10−8 M. In the presence of calcium, a high-mobility complex of SP-A and [3H]Rb-LPS (Rb mutant of LPS from Escherichia coli strain LCD 25) micelles was formed, as detected by sucrose density gradients. Re-LPS aggregation induced by SP-A was further characterized by light scattering. On the other hand, human SP-A inhibited TNF-α (tumour necrosis factor-α) secretion by human macrophage-like U937 cells stimulated with either Re-LPS or smooth LPS. We further examined the effects of human SP-A on the binding of Re-LPS to LBP (LPS-binding protein) and CD14. SP-A decreased the binding of Re-LPS to CD14, but not to LBP, as detected by cross-linking experiments with 125I-ASD-Re-LPS [125I-labelled sulphosuccinimidyl-2-(p-azidosalicylamido)-1,3-dithiopropionate derivative of Re-LPS] and fluorescence analysis with FITC-Re-LPS. When SP-A, LBP and CD14 were incubated together, SP-A reduced the ability of LBP to transfer 125I-ASD-Re-LPS to CD14. These SP-A effects were not due to the ability of SP-A to aggregate Re-LPS in the presence of calcium, since they were observed in both the absence and the presence of calcium. These studies suggest that SP-A could contribute to modulate Re-LPS responses by altering the competence of the LBP–CD14 receptor complex.

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