Effects of amyloid induction on plasma protein turnover, and its implication.
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.
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
D000510:Alpha-Globulins; D000682:Amyloid; D001609:Beta-Globulins; D001798:Blood Proteins; D002364:Caseins; D006023:Glycoproteins; D005719:gamma-Globulins