Inefficient degradation of oxidized regions of protein molecules.
We have previously shown that the intracellular half-life of endocytosed oxidized albumin is much longer than that of native albumin. We now report that the regions of oxidized albumin which contain oxidation products (carbonyls and fluorophores), are less readily released as small degradation products by cell-free proteolysis than is the molecule overall. We deduce that oxidized moieties in the polypeptide chain can confer localized resistance to enzymatic proteolysis. Such resistance to proteolysis may account for the intracellular accumulation of some endocytosed oxidized protein which we have previously observed.
Grant
A J
AJ
Heart Research Institute, Camperdown, Sydney, Australia.
Jessup
W
W
Dean
R T
RT
D010450:Endopeptidases / Q000378:metabolism*; D006207:Half-Life; D006868:Hydrolysis; D008264:Macrophages / Q000378:metabolism; D010084:Oxidation-Reduction; D010446:Peptide Fragments / Q000378:metabolism; D010659:Phenylhydrazines; D012710:Serum Albumin, Bovine / Q000378:metabolism*; D013050:Spectrometry, Fluorescence; D014357:Trypsin / Q000378:metabolism
D010446:Peptide Fragments; D010659:Phenylhydrazines; C004787:2,4-dinitrophenylhydrazine; D012710:Serum Albumin, Bovine; D010450:Endopeptidases; D014357:Trypsin