MICB0106 gene polymorphism is associated with ulcerative colitis in central China

Background: The highly polymorphic nonclassical MHC class I chain-related genes A and B (MICA and MICB) encode stress-inducible glycoproteins expressed on various epithelial cells including intestinal epithelial cells. MICA and MICB gene polymorphisms and expressions are associated with autoimmune diseases but not known in ulcerative colitis (UC). Aims: To investigate the association of MICB exon 2-4 polymorphisms and soluble MICA (sMICA) expression with the susceptibility of UC in central China. Materials and methods: Genomic DNA was isolated from peripheral blood. The allele frequencies of MICB exon 2-4 were genotyped in 105 UC patients and 213 healthy controls by PCR single-stranded conformation polymorphism method. Thirty-two patients and 32 controls were selected for determining serum sMICA expression by ELISA. Results: Allele frequency of MICB0106 was significantly higher in UC patients than in healthy controls (19.0% vs. 8.9%, corrected P (Pc)=0.0006), especially in patients with extensive colitis (24.4% vs. 8.9%, Pc=0.0006), moderate and severe disease (24.1% vs. 8.9%, Pc=0.0006), extraintestinal manifestations (20.5% vs. 8.9%, Pc=0.012), male patients (22.1% vs. 8.0%, Pc=0.006), and patients over the age of 40 years (28.8% vs. 8.3%, Pc=0.0006). The sMICA level was significantly higher in UC than in healthy controls (604.41±480.43 pg/ml vs. 175.37±28.31 pg/ml, P=0.0001) but not associated with the MICB0106 genotypes. Conclusions: Overall, MICB0106 allele was positively associated with UC in the Han Chinese in central China. sMICA was highly expressed in UC but not associated with the MICB0106 genotype

Evidence for conserved fuzzy complexes involving a preorganized Unique domain in the Src family of kinases. Structure, 2017

File description: pkl_* = Peak lists exported from CCPN Analysis 2.4.2 CSP_* = Chemical Shift Perturbation values between the constructs referenced in thee name and at the specified temperature. Calculated with Farseer version alpha (Joao MC Teixeira et al., manuscript in preparation) according to the following formula: CSP = (0.5*((∆δH**2)+ ((0.2*∆δ N)**2)))**0.5 PRE_* = Calculated PRE (Ipara/Ida) for th specified constructs. DeltaPRE_* = Calculated DeltaPRE and random coil simulation (Flexible Meccano v1.1, Ozenne et al.)Flexible Meccano (see paper for further details and references) SAXS_*fit = Experimental SAXS curves and theoretical values for random coil (rc) or optimized (eom) ensemble. SAXS_*_rghist = Histogram of the Rg values of the conformers inthe random coil (rc) or optimized (eom) ensemble

The Unique Domain Forms a Fuzzy Intramolecular Complex in Src Family Kinases. Structure, 2017

File description: pkl_* = Peak lists exported from CCPN Analysis 2.4.2 CSP_* = Chemical Shift Perturbation values between the constructs referenced in thee name and at the specified temperature. Calculated with Farseer version alpha (Joao MC Teixeira et al., manuscript in preparation) according to the following formula: CSP = (0.5*((∆δH**2)+ ((0.2*∆δ N)**2)))**0.5 PRE_* = Calculated PRE (Ipara/Ida) for th specified constructs. DeltaPRE_* = Calculated DeltaPRE and random coil simulation (Flexible Meccano v1.1, Ozenne et al.)Flexible Meccano (see paper for further details and references) SAXS_*fit = Experimental SAXS curves and theoretical values for random coil (rc) or optimized (eom) ensemble. SAXS_*_rghist = Histogram of the Rg values of the conformers inthe random coil (rc) or optimized (eom) ensemble

Journal of Thrombosis and Haemostasis / Platelet-borne complement proteins and their role in platelet-bacteria interactions

Background: The role of platelets in immune defense is increasingly being recognized. Platelets bind complement proteins from plasma, initiate complement activation, and interact with bacteria. However, the contribution of platelets to complement-mediated defense against bacterial infections is not known in detail. Objectives: To assess platelet interactions with Escherichia coli strains, and evaluate the contributions of platelet complement proteins to host defense. Methods: We studied the cell-cell interactions of a pathogenic and a non-pathogenic E. coli strain with platelet concentrates, washed platelets and manually isolated platelets by flow cytometry and ELISA. The presence of complement proteins and complement RNA in megakaryocytes and platelets was analyzed by PCR, RT-PCR, confocal microscopy, and western blotting. Results: Incubation with E. coli leads to platelet activation, as indicated by the expression of CD62P and CD63 on the platelet surface. RNA and protein analyses show that megakaryocytes and platelets contain complement C3, and that platelet C3 migrates differently on polyacrylamide gels than plasmatic C3. Activation of platelets by bacteria leads to translocation of C3 to the cell surface. This translocation is not induced by thrombin receptor activating peptide or lipopolysaccharide. Interaction of platelets with E. coli occurs even in the absence of plasma proteins, and is independent of platelet toll-like receptor 4 and alpha(2b)beta(3) (glycoprotein IIbIIIa). Conclusion: Platelets contain a specific form of C3. Importantly, they can modulate immune defense against bacteria by enhancing plasmatic complement activation.W 1205-B09(VLID)311220