title: Effects of amyloid induction on plasma protein turnover, and its implication.
abstract: Using polyacrylamide gel electrophoresis and radioiodinated plasma proteins, data on the rate constant for synthesis and fractional degradation rates for albumin, alpha1-, alpha2-, beta-, and gamma-globulins were obtained during accelerated amyloid induction in a murine model. The results indicate that during amyloid induction there is an increased rate of synthesis of alpha2-, beta-, and gamma-globulins but only the alpha2-globulin degradation rate is accelerated. In this experimental system, should amyloid protein be a degradation product of a plasma fraction, the alpha2-globulin appears as the most likely precursor. The implications of our findings are discussed, and a new general mechanism of amyloid production is proposed.
mesh_terms: D000510:Alpha-Globulins / Q000378:metabolism; D000682:Amyloid / Q000032:analysis / Q000096:biosynthesis*; D000686:Amyloidosis / Q000139:chemically induced / Q000209:etiology; D000818:Animals; D001609:Beta-Globulins / Q000378:metabolism; D001797:Blood Protein Electrophoresis; D001798:Blood Proteins / Q000378:metabolism*; D002364:Caseins; D004591:Electrophoresis, Polyacrylamide Gel; D005260:Female; D006023:Glycoproteins / Q000378:metabolism; D006207:Half-Life; D007700:Kinetics; D051379:Mice; D013997:Time Factors; D005719:gamma-Globulins / Q000378:metabolism
chemical_list: D000510:Alpha-Globulins; D000682:Amyloid; D001609:Beta-Globulins; D001798:Blood Proteins; D002364:Caseins; D006023:Glycoproteins; D005719:gamma-Globulins