Recongnition by guinea-pig peritoneal exudate cells of conformationally different states of the collagen molecule.
Guinea-pig peritoneal exudate cells were tested in vitro in the presence or absence of specific antiserum to native collagen for their capacity to discriminate between native and denatured collagens of various species. Adherent exudate cells bound denatured collagens, regardless of the origin of the collagen or the presence of serum. The binding was reduced if the cells were pretreated with trypsin. Recovery of binding was mediated by a normal serum component resembling an IgM antibody to denatured collagen. In the presence of normal serum, native collagen was only marginally bound, apparently in a non-specific manner. Uptake of native heterologous collagens was greatly increased in the presence of specific antiserum to native collagen with specificity of binding reflecting the type of collagen. Binding of denatured and native collagen occur via independent mechanisms.
D000818:Animals; D000917:Antibody Formation; D000918:Antibody Specificity; D001202:Ascitic Fluid / Q000166:cytology*; D003094:Collagen / Q000276:immunology*; D005260:Female; D006168:Guinea Pigs; D007104:Immune Adherence Reaction; D007106:Immune Sera; D066298:In Vitro Techniques; D008297:Male; D009439:Neuraminidase / Q000494:pharmacology; D010587:Phagocytosis; D011485:Protein Binding; D011487:Protein Conformation; D011489:Protein Denaturation; D013045:Species Specificity; D013997:Time Factors; D014357:Trypsin / Q000494:pharmacology
D007106:Immune Sera; D003094:Collagen; D009439:Neuraminidase; D014357:Trypsin