Escherichia coli in menstrual blood: An association with bacterial endotoxin and toll-like receptor 4 (TLR4)-mediated growth of endometriosis

2006 ◽  
Vol 71 (2) ◽  
pp. 152-153 ◽  
Author(s):  
K.N. Khan ◽  
M. Kitajima ◽  
K. Hiraki ◽  
A. Fujishita ◽  
T. Ishimaru ◽  
...  
2020 ◽  
Vol 41 (33) ◽  
pp. 3156-3165 ◽  
Author(s):  
Roberto Carnevale ◽  
Sebastiano Sciarretta ◽  
Valentina Valenti ◽  
Flavio di Nonno ◽  
Camilla Calvieri ◽  
...  

Abstract Aims Low-grade endotoxaemia is detectable in human circulation but its role in thrombosis is still unclear. Methods and results We measured serum lipopolysaccharide (LPS) concentration, soluble P-selectin (sP-selectin), a marker of platelet activation, and zonulin, a marker of gut permeability, in peripheral circulation, coronary thrombi, and intracoronary blood of patients with ST-elevation myocardial infarction (STEMI, n = 50) and stable angina (SA) (n = 50), respectively, and in controls (n = 50). Experimental study was carried out in mice to assess if Escherichia coli-LPS (E. coli-LPS) possess thrombotic property. Coronary thrombi from STEMI showed higher concentrations of LPS, sP-selectin vs. intracoronary blood of SA and peripheral blood of controls (P < 0.001). Zonulin was higher in STEMI compared to the other two groups [4.57 (3.34–5.22); 2.56 (0.41–4.36); 1.95 (1.22–2.65) ng/mL; P < 0.001] and correlated with LPS (Rs = 0.585; P < 0.001). Escherichia coli DNA was positive in 34% of STEMI vs. 12% of SA and 4% of controls (P < 0.001). In a subgroup of 12 STEMI, immunohistochemical analysis of coronary thrombi showed positivity for leucocyte Toll-like receptor 4 (TLR4), cathepsin G, and LPS from E. coli in 100%, 80%, and 25% of samples, respectively. E. coli-LPS injected in mice to reach LPS concentrations like those detected in coronary thrombi was associated with enhanced artery thrombosis and platelet activation, an effect blunted by TLR4 inhibitor co-administration. In vitro study demonstrated that LPS from E. coli enhanced platelet aggregation via TLR4-mediated leucocyte cathepsin G activation. Conclusion ST-elevation myocardial infarction patients disclose an enhanced gut permeability that results in LPS translocation in human circulation and eventually thrombus growth at site of artery lesion via leucocyte–platelet interaction.


2009 ◽  
Vol 68 (1) ◽  
pp. 40-52 ◽  
Author(s):  
Khaleque Newaz Khan ◽  
Michio Kitajima ◽  
Koichi Hiraki ◽  
Akira Fujishita ◽  
Ichiro Sekine ◽  
...  

2004 ◽  
Vol 279 (19) ◽  
pp. 20044-20048 ◽  
Author(s):  
Kiyoshi Kawasaki ◽  
Robert K. Ernst ◽  
Samuel I. Miller

Toll-like receptor 4 (TLR4)-mediated responses, which are induced by the lipid A portion of lipopolysaccharide, are important for host defense against Salmonellae infection. A variety of different data indicate that the acylation state of lipid A can alter TLR4-mediated responses. TheS. typhimuriumvirulence gene product PhoP/PhoQ signals the presence of host microenvironments to regulate the expression of a lipid A 3-O-deacylase, PagL, and a lipid A palmitoyltransferase, PagP. We now demonstrate that 3-O-deacylation and palmitoylation of lipid A decreases its ability to induce TLR4-mediated signaling. Deacylated lipid A, deacylated and palmitoylated lipid A, palmitoylated lipid A, and unmodified lipid A species were purified fromEscherichia coliheterologously expressing PagL and/or PagP. The purified lipid A preparations showed spectra of a single lipid A species on mass spectrometry and gave a single band on thin layer chromatography. The activity of purified lipid A species was examined using human and mouse cell lines that express recombinant human TLR4. Compared with unmodified lipid A, the modified lipid A species are 30–100-fold less active in the ability to induce NF-κB-dependent reporter activation. These results suggest that the lipid A modifications reduce TLR4-signaling as part of Salmonellae adaptation to host environments.


2004 ◽  
Vol 32 (Supplement) ◽  
pp. A15
Author(s):  
Masayuki Ii ◽  
Mie Sunamoto ◽  
Naoko Matsunaga ◽  
Kazuyo Nakamura ◽  
Katsunori Takashima ◽  
...  

2011 ◽  
Vol 138-139 ◽  
pp. 1168-1173
Author(s):  
Quan Xin Gao ◽  
Li Li Qi ◽  
Jin Bo Wang ◽  
Qing Cha Zhuang ◽  
Shi Jian Chen ◽  
...  

The aim of this study was to determine whether theEscherichia coli(EPEC) attached to cells by the TLR4. A fusion between gene encoding fluoresce-enhanced green fluorescent protein (EGFP) and Toll like receptor 4 (TLR4) was constructed and expressed inEscherichia coli. Then the pEGFP-N1-TLR4 fusion expression vector was transfected into HT-29 cells. The green fluoresce was observed at the plasma membrane of HT-29 cells under inverted fluorescent microscopes. In addition, the FITC stained EPEC was also observed adherence to the TLR4 of HT-29 cells.The results indicated that the EPEC adhered to cells by bonding to TLR4 protein. It is the first time that the TLR4 has been explained as an adhesion receptor.


2002 ◽  
Vol 283 (4) ◽  
pp. H1645-H1655 ◽  
Author(s):  
James A. Thomas ◽  
May F. Tsen ◽  
D. Jean White ◽  
Jureta W. Horton

Both large burns and severe gram-negative sepsis are associated with acute myocardial contractile dysfunction. Because others have reported that burn injury may be followed by transient endotoxemia, we hypothesized that bacterial endotoxin induces contractile impairment after burn trauma. We tested this hypothesis in two rodent models. In each model, postburn myocardial contractility was assessed using Langendorff preparations of excised hearts. In the first model, mice expressing either a mutant form of or no Toll-like receptor 4 (TLR4), a critical element of the mammalian endotoxin receptor, were resistant to postburn myocardial contractile dysfunction. In the second model, starting 30 min or 4 h after burn injury, rats were infused with recombinant bactericidal/permeability-increasing protein (rBPI21), a protein that binds and neutralizes endotoxin. Hearts from rBPI21-treated animals were completely protected from postburn contractile impairment. Because burn-induced contractile dysfunction can be prevented either by blocking signaling through the endotoxin receptor or by neutralizing circulating LPS, bacterial endotoxin may contribute to impaired myocardial contractility after burn injury.


Sign in / Sign up

Export Citation Format

Share Document