title: Endothelial chylomicron binding is altered by interaction with high-density lipoprotein in Heymann's nephritis.
abstract: Very-low-density lipoprotein (VLDL) catabolism is impaired in the nephrotic syndrome, partly as a result of structural changes that impair endothelial binding in the presence of lipoprotein lipase. Previous results suggested that postsynthetic modification of VLDL by high-density lipoprotein (HDL) in nephrotic syndrome rats causes their failure to bind endothelia normally. It is unknown (1) whether the structure of secreted lipoproteins is normal before exposure to nephrotic syndrome serum and (2) whether the same structural or functional defects are imparted to chylomicrons (CMs) through their interaction with HDL from nephrotic syndrome rats. CMs were isolated from thoracic duct lymph from rats with passive Heymann's nephritis (HN) and normal controls. CMs from control rats were incubated with HDL from either HN or control rats and reisolated, and apolipoprotein E (apo E) content and endothelial binding were determined. We found that CMs secreted by HN and control rats had similar apo E/B-48 ratios. HDL from HN rats had significantly lower apo E/A-I ratios than controls. Incubation of nascent control CMs with control HDL resulted in a 4-fold increase in CM apo E content, but binding was unaffected. Incubation with HDL from HN resulted in only a 50% increase in CM apo E content but reduced binding of these treated CMs by 50% compared either with nascent control CMs or with CMs incubated with control HDL. HDL from rats with HN alters CM binding to lipoprotein lipase by a mechanism that does not involve reducing the content of apo E already present on CMs at the time of secretion.
authors.affiliation: Department of Veterans Affairs Northern California Health Care System, Mather, CA, USA.
authors.forename: G C
authors.initials: GC
authors.lastname: Shearer
authors.forename: W G
authors.initials: WG
authors.lastname: Couser
authors.forename: G A
authors.initials: GA
authors.lastname: Kaysen
mesh_terms: D000818:Animals; D001057:Apolipoproteins E / Q000378:metabolism; D002914:Chylomicrons / Q000378:metabolism*; D004730:Endothelium, Vascular / Q000378:metabolism*; D005921:Glomerulonephritis / Q000139:chemically induced / Q000378:metabolism*; D026541:Heymann Nephritis Antigenic Complex; D008075:Lipoproteins, HDL / Q000378:metabolism*; D008297:Male; D051381:Rats; D017207:Rats, Sprague-Dawley; D012709:Serum Albumin / Q000378:metabolism
chemical_list: D001057:Apolipoproteins E; D002914:Chylomicrons; D026541:Heymann Nephritis Antigenic Complex; D008075:Lipoproteins, HDL; D012709:Serum Albumin