Accelerated endocytosis and incomplete catabolism of radical-damaged protein.
Native bovine serum albumin (BSA) was endocytosed and degraded at a steady rate by resident peritoneal murine macrophages with barely detectable amounts remaining within the cells. Radical-damaged BSA was endocytosed and degraded up to 2.5-fold more rapidly than native BSA, but some radical-damaged BSA accumulated within the cells in a time-dependent manner. The extent of accumulation increased in parallel with that of radical damage. Thus, some radical-damaged BSA was processed less efficiently than native BSA. Such inefficient catabolism of radical-damaged proteins may contribute to certain diseases such as atherosclerosis.
Grant
A J
AJ
Heart Research Institute, Camperdown, Sydney, Australia.
Jessup
W
W
Dean
R T
RT
D000818:Animals; D002478:Cells, Cultured; D004586:Electrophoresis; D004705:Endocytosis / Q000502:physiology*; D005609:Free Radicals / Q000378:metabolism; D006207:Half-Life; D006868:Hydrolysis; D008264:Macrophages / Q000502:physiology*; D051379:Mice; D012710:Serum Albumin, Bovine / Q000737:chemistry / Q000378:metabolism*
D005609:Free Radicals; D012710:Serum Albumin, Bovine