ABSTRACT
INTRODUCTION: Congenital heart malformations are risk factors that make children susceptible to infections resulting in inflammation. MATERIAL AND METHODS: The concentration of histamine as a modulator of inflammation was quantified in pericardial fluid and expression of histamine H(4) receptor (H(4)R) and histamine-releasing factor (HRF) was determined at mRNA and protein levels. Samples of pericardium and pericardial fluid were obtained during cardiac reconstruction surgery in children. RESULTS: In children with pericarditis, increased levels of histamine were found and expression of H(4)R was localized on mast cells. Expression of HRF was independent of presence or absence of inflammation in pericardium and was localized within stationary epithelial cells. CONCLUSION: Results indicate that involvement of H4R in pericardial inflammation depends on penetration of mast cells into inflamed tissue, but HRF may not be directly involved in inflammatory reaction of the pericardium.
Subject(s)
Heart Defects, Congenital/complications , Heart Defects, Congenital/metabolism , Histamine/blood , Pericarditis/etiology , Pericarditis/metabolism , Pericardium/metabolism , Biomarkers, Tumor/biosynthesis , Biomarkers, Tumor/genetics , Child, Preschool , Heart Defects, Congenital/pathology , Humans , Immunohistochemistry , Infant , Pericardial Effusion/metabolism , Pericarditis/pathology , Pericardium/pathology , RNA, Messenger/biosynthesis , RNA, Messenger/genetics , Receptors, G-Protein-Coupled/biosynthesis , Receptors, G-Protein-Coupled/genetics , Receptors, Histamine/biosynthesis , Receptors, Histamine/genetics , Receptors, Histamine H4 , Reverse Transcriptase Polymerase Chain Reaction , Tumor Protein, Translationally-Controlled 1ABSTRACT
Human factor VIII was purified from cryoprecipitate and incubated for up to 24 hours with four neutral proteases of human blood leukocytes, namely, with elastase-like protease (ELP), chymotrypsin-like protease (CLP), collagenase and gelatinase. Electrophoretic patterns showed a reproducible sequence of degradation of factor VIII and of its 230,000 molecular weight subunit by ELP and CLP. Intermediate products were similar but those resulting from exhaustive proteolysis by ELP and CLP differed distinctly from each other. Procoagulant activity of factor VIII was rapidly and completely destroyed by ELP and CLP before visible electrophoretic changes would be detected. No increase in this activity was observed prior to its destruction. Von Willebrand factor (ristocetin cofactor) activity was considerably more resistant to ELP and CLP and declined in rough relation to degradation of highly aggregated forms of factor VIII. ELP and CLP produced a pronounced progressive increase in the Laurell reaction antigen. Normal human plasma showed a high potency to inhibit ELP and CLP. Large doses of these enzymes (300 microgram per ml) produced in the plasma medium only a moderate fall in factor VIII procoagulant activity. Collagenase and gelatinase did neither degrade factor VIII nor change its biological properties.
