title: Hyaluronic acid-complement interactions--II. Role of divalent cations and gelatin.
abstract: Native hyaluronic acid (HA) is reported to be a weak anticomplementary agent. However, the normal buffer systems used for complement tests incorporate gelatin, Ca2+ and Mg2+, which may bind to HA, influence its conformation and interfere with its anticomplementary reactions with complement components such as Cl. In this study, metal ions (Ca2+ and Mg2+), gelatin and fibronectin appeared to react with native HA preparations and block their anticomplementary effects on Cl. In previous studies, we obtained evidence for a relationship between reversible heat-induced HA conformational changes and a subsequent reversible increase in anticomplementary activity. The anticomplementary activity of heat-treated HA preparations was also reduced by gelatin.
mesh_terms: D001665:Binding Sites; D002021:Buffers; D002118:Calcium / Q000494:pharmacology; D002413:Cations, Divalent / Q000494:pharmacology*; D003172:Complement C1 / Q000378:metabolism; D003169:Complement Inactivator Proteins / Q000037:antagonists & inhibitors*; D005353:Fibronectins / Q000494:pharmacology; D005780:Gelatin / Q000494:pharmacology*; D006461:Hemolysis / Q000187:drug effects; D006358:Hot Temperature; D006801:Humans; D006820:Hyaluronic Acid / Q000037:antagonists & inhibitors* / Q000494:pharmacology; D008274:Magnesium / Q000494:pharmacology; D011487:Protein Conformation
chemical_list: D002021:Buffers; D002413:Cations, Divalent; D003172:Complement C1; D003169:Complement Inactivator Proteins; D005353:Fibronectins; D005780:Gelatin; D006820:Hyaluronic Acid; D008274:Magnesium; D002118:Calcium