[Interacting between amyloid P and connective tissue proteins ].
In order to look for the position of amyloid P in the macromolecular connective tissue and extracellular matrix system, we performed binding studies involving affinity chromatography. Binding studies revealed the strong binding of fibronectin to amyloid P (S-AP). The fibronectin-amyloid P linkage was dissociated after elution with 2 M urea. Heparan sulfate, a major glycosaminoglycan of the extracellular matrix, showed strong binding to S-AP, which was dissociated at 3 M urea. Laminin, collagen type I and type IV, reduced and alkylated glomerular basement membranes as well as the glycosamino-glycans hyaluronic acid and chondroitin-4-sulfate failed to bind to S-AP. Our binding studies show that amyloid P can react strongly with extra cellular matrix proteins and can help to explain the presence of amyloid P in normal connective tissue.
D000682:Amyloid / Q000378:metabolism*; D001669:Biochemical Phenomena; D001671:Biochemistry; D002809:Chondroitin Sulfates / Q000378:metabolism; D002846:Chromatography, Affinity; D003094:Collagen / Q000378:metabolism; D005353:Fibronectins / Q000378:metabolism*; D006023:Glycoproteins / Q000378:metabolism; D006497:Heparan Sulfate / Q000378:metabolism; D006801:Humans; D006820:Hyaluronic Acid / Q000378:metabolism; D007797:Laminin; D009363:Neoplasm Proteins / Q000378:metabolism; D000683:Serum Amyloid P-Component
D000682:Amyloid; D002809:Chondroitin Sulfates; D003094:Collagen; D005353:Fibronectins; D006023:Glycoproteins; D006497:Heparan Sulfate; D006820:Hyaluronic Acid; D007797:Laminin; D009363:Neoplasm Proteins; D000683:Serum Amyloid P-Component
Wechselwirkungen zwischen Amyloid P und Bindegewebsproteinen.