The binding of dsDNA and ssDNA to human types I, II and IV collagens.
Our study was undertaken to determine if dsDNA and ssDNA, which are known to bind to bovine collagen and to glomerular basement membrane, also bind to purified human types I, II and IV collagens. Four human sera with antibodies to dsDNA and 4 human sera with antibodies to ssDNA, when employed in an enzyme linked immunosorbent assay, detected DNA binding to the solid phase only when the solid phase had been precoated with collagen. Mean optical densities (OD) of .978, 1.062 and 1.033 for dsDNA binding to types I, II and IV collagens, respectively, were substantially higher than the mean OD value of .177 obtained when dsDNA was applied to the noncollagen coated solid phase. Similarly, mean OD values of .664, .526 and .902 for ssDNA binding to types I, II and IV collagens, respectively, were higher than the mean OD value of .147 obtained when ssDNA was applied to the noncollagen coated solid phase. The affinity of DNA for collagen could be an important factor contributing to the localization of DNA-anti-DNA complexes in target tissues.
D000818:Animals; D003094:Collagen / Q000145:classification / Q000378:metabolism*; D003166:Complement Activating Enzymes / Q000378:metabolism; D015922:Complement C1q; D004247:DNA / Q000378:metabolism*; D004277:DNA, Single-Stranded / Q000378:metabolism*; D006801:Humans; D007114:Immunization; D011817:Rabbits
D004277:DNA, Single-Stranded; D015922:Complement C1q; D003094:Collagen; D004247:DNA; D003166:Complement Activating Enzymes