7 research outputs found
Localization in <i>SERPINC1</i> gene of potential vitamin D response elements (VDRE) identified by using <i>in silico</i> predictions with JASPAR software.
<p>The localization in <i>SERPINC1</i> of the genetic variations evaluated in this study is shown. The predictive score of interaction with RXRα/VDR of wild type and mutated sequences obtained by using JASPAR software are also indicated.</p
Demographic, clinical, analytical and genetic features of patients with antithrombin deficiency and mutations affecting potential regulatory sequences in <i>SERPINC1</i>.
<p>Demographic, clinical, analytical and genetic features of patients with antithrombin deficiency and mutations affecting potential regulatory sequences in <i>SERPINC1</i>.</p
<i>LARGE</i> haplotypes identified in the validation study and their correlation with anti-FXa activity.
<p><i>LARGE</i> haplotypes identified in the validation study and their correlation with anti-FXa activity.</p
Manhattan plot GWAS with antithrombin phenotype.
<p>The thresholdof significance to select candidate SNPs for validation is also shown.</p
Genotype-phenotype analysis in the validation study.
<p>Genotype-phenotype analysis in the validation study.</p
Consequences of <i>LARGE</i> gene silencing in HepG2 and HEK-EBNA cell lines.
<p>A) Secreted proteins to the conditioned medium evaluated by immunoblotting. B) Effect on intracellular antithrombin from HepG2 cells analyzed by immunofluorescence and immunoblotting. C) Effect on the levels of <i>SERPINC1</i> expression in HEK-EBNA and HepG2 cell lines. Immunoblots and immunofluorescence figures are representative of at least 3 independent experiments. Control represents cells transfected with scramble siRNA, although similar results were observed in cells transfected without siRNA.</p
Glycomic and proteomic analysis of α-antithrombin purified from plasma of healthy subjects with the highest (blue) and lowest (red) <i>LARGE</i> expression.
<p>As controls we also used antithrombin glycoforms α (black), and β (green) purified from a pool of 100 healthy blood donors. The β glycoform has 3 <i>N</i>-glycans since it lacks N-glycosylation at N-135. A) MALDI TOF mass spectrometric analysis of: 1) Intact glycoproteins; 2) 2AB-labeled N-glycans. B) HPLC data. 1) Distribution of the glycan structures of antithrombin specimens. Values are represented as % of total glycan pool. Between brackets are the absolute fluorescence units. 2) HILIC HPLC profiles of antithrombin specimens.</p