title: Proteoglycans from pig aorta. Comparative study of their interactions with lipoproteins.
abstract: Different proteoglycans (PGs) were isolated from pig aorta for aggregation studies with hyaluronic acid and human low-density lipoproteins (LDL). Extraction of the intima-media with 4M-guanidinium chloride and digestion of the residue with collagenase solubilized 91% of aortic hexuronic acid content. From the guanidinium chloride extract two PGs were isolated by ion-exchange and gel-permeation chromatography: proteochondroitin sulphate (PGI) with a protein-core apparent Mr of 250 000 and proteodermatan-chondroitin sulphate (PGII) with a protein-core apparent Mr of 55 000. Only PGI forms high-Mr aggregates with hyaluronic acid. From the collagenase digest two other PGs were isolated: proteoheparan sulphate and proteochondroitin sulphate (PGIII and PGIV respectively). PGIV had a smaller hydrodynamic size than PGI. PGI and PGII formed insoluble complexes with human LDL in the presence of Ca2+. PGIII or PGIV did not form precipitates with the LDL. PGI and PGII, but neither PGIII nor PGIV, were bound to LDL-Sepharose. The main peaks of PGI and PGII were eluted from LDL-Sepharose with 60 mM- and 90 mM-NaCl respectively. The results indicate that aortic PGs have different interacting potentials with lipoproteins, depending on their Mr and their glycosaminoglycan composition.
mesh_terms: D000818:Animals; D001011:Aorta / Q000378:metabolism*; D002845:Chromatography; D002850:Chromatography, Gel; D006025:Glycosaminoglycans / Q000032:analysis; D006820:Hyaluronic Acid / Q000378:metabolism; D008077:Lipoproteins, LDL / Q000378:metabolism*; D046911:Macromolecular Substances; D011485:Protein Binding; D011509:Proteoglycans / Q000302:isolation & purification / Q000378:metabolism*; D013552:Swine
chemical_list: D006025:Glycosaminoglycans; D008077:Lipoproteins, LDL; D046911:Macromolecular Substances; D011509:Proteoglycans; D006820:Hyaluronic Acid