Interaction of intact type VI collagen with hyaluronan.
The capacity of non-pepsinyzed type VI collagen to bind to hyaluronan was investigated. Type VI collagen was extracted from bovine meniscal cartilage with 6 M GuHCl and purified by extraction of PEG precipitates and dissociative Sephacryl S-500 HR chromatography. Type VI collagen, detected with a monoclonal antibody, bound in 0.5 M NaCl to hyaluronan-coated micro-wells, the degree of binding being higher at 37 degrees C than 23 degrees C and 4 degrees C. Incubation of type VI collagen in competitive inhibition assays with testicular hyaluronidase digests of hyaluronan in liquid phase, reduced binding of the protein to hyaluronan-coated microwells to background levels. Thus, non-pepsinyzed type VI collagen binds to hyaluronan in vitro.
McDevitt
C A
CA
Department of Musculoskeletal Research, Cleveland Clinic Foundation Research Institute, OH 44195.
Marcelino
J
J
Tucker
L
L
D000818:Animals; D001667:Binding, Competitive; D015153:Blotting, Western; D002356:Cartilage / Q000737:chemistry; D002417:Cattle; D011232:Chemical Precipitation; D003094:Collagen / Q000302:isolation & purification / Q000378:metabolism*; D004797:Enzyme-Linked Immunosorbent Assay; D006801:Humans; D006820:Hyaluronic Acid / Q000378:metabolism*; D006821:Hyaluronoglucosaminidase / Q000378:metabolism; D008297:Male; D011092:Polyethylene Glycols; D013737:Testis / Q000201:enzymology
D011092:Polyethylene Glycols; D006820:Hyaluronic Acid; D003094:Collagen; D006821:Hyaluronoglucosaminidase