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.
Full text
PDF



















Images in this article
Selected References
These references are in PubMed. This may not be the complete list of references from this article.
- Aronson N. N., Jr, De Duve C. Digestive activity of lysosomes. II. The digestion of macromolecular carbohydrates by extracts of rat liver lysosomes. J Biol Chem. 1968 Sep 10;243(17):4564–4573. [PubMed] [Google Scholar]
- Axelrad M., Kisilevsky R., Beswetherick S. Acceleration of amyloidosis by syngeneic spleen cells from normal donors. Am J Pathol. 1975 Feb;78(2):277–284. [PMC free article] [PubMed] [Google Scholar]
- Baumstark J. S. Studies on the elastase-serum protein interaction. I. Molecular identity of the inhibitors in human serum and direct demonstration of inhibitor-elastase complexes by zone and immunoelectrophoresis. Arch Biochem Biophys. 1967 Mar 20;118(3):619–630. doi: 10.1016/0003-9861(67)90397-9. [DOI] [PubMed] [Google Scholar]
- Benditt E. P., Eriksen N. Chemical characteristics of the substance of typical amyloidosis in monkeys. Acta Pathol Microbiol Scand Suppl. 1972;233:103–108. [PubMed] [Google Scholar]
- Benditt E. P., Eriksen N. Chemical classes of amyloid substance. Am J Pathol. 1971 Oct;65(1):231–252. [PMC free article] [PubMed] [Google Scholar]
- Benson M. D., Aldo-Benson M. A., Shirahama T., Borel Y., Cohen A. S. Suppression of in vitro antibody response by a serum factor (SAA) in experimentally induced amyloidosis. J Exp Med. 1975 Jul 1;142(1):236–241. doi: 10.1084/jem.142.1.236. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Benson M. D., Skinner M., Lian J., Cohen A. S. "A" protein of amyloidosis. Isolation of a cross-reacting component from serum by affinity chromatography. Arthritis Rheum. 1975 Jul-Aug;18(4):315–322. doi: 10.1002/art.1780180404. [DOI] [PubMed] [Google Scholar]
- COHEN S., HOLLOWAY R. C., MATTHEWS C., MCFARLANE A. S. Distribution and elimination of 131 I- and 14C-labelled plasma proteins in the rabbit. Biochem J. 1956 Jan;62(1):143–154. doi: 10.1042/bj0620143. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Cohen A. S., Cathcart E. S. Amyloidosis and immunoglobulins. Adv Intern Med. 1974;19:41–55. [PubMed] [Google Scholar]
- Debanne M. T., Regoeczi E., Dolovich J. Serum protease inhibitors in the blood clearance of subtilisin A. Br J Exp Pathol. 1973 Oct;54(5):571–582. [PMC free article] [PubMed] [Google Scholar]
- Ein D., Kimura S., Terry W. D., Magnotta J., Glenner G. G. Amino acid sequence of an amyloid fibril protein of unknown origin. J Biol Chem. 1972 Sep 10;247(17):5653–5655. [PubMed] [Google Scholar]
- GITLIN D., JANEWAY C. A. Some isotopic studies on the distribution and metabolism of plasma proteins. Adv Biol Med Phys. 1960;7:249–293. doi: 10.1016/b978-1-4832-3113-6.50009-9. [DOI] [PubMed] [Google Scholar]
- Glenner G. G., Terry W., Harada M., Isersky C., Page D. Amyloid fibril proteins: proof of homology with immunoglobulin light chains by sequence analyses. Science. 1971 Jun 11;172(3988):1150–1151. doi: 10.1126/science.172.3988.1150. [DOI] [PubMed] [Google Scholar]
- HAVERBACK B. J., DYCE B., BUNDY H. F., WIRTSCHAFTER S. K., EDMONDSON H. A. Protein binding of pancreatic proteolytic enzymes. J Clin Invest. 1962 May;41:972–980. doi: 10.1172/JCI104576. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Harpel P. C. Human plasma alpha 2-macroglobulin. An inhibitor of plasma kallikrein. J Exp Med. 1970 Aug 1;132(2):329–352. doi: 10.1084/jem.132.2.329. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Hermodson M. A., Kuhn R. W., Walsh K. A., Neurath H., Eriksen N., Benditt E. P. Amino acid sequence of monkey amyloid protein A. Biochemistry. 1972 Aug 1;11(16):2934–2938. doi: 10.1021/bi00766a002. [DOI] [PubMed] [Google Scholar]
- Ho J., Jeejeebhoy K. N., Painter R. H. A plasma protein fractionation procedure for use in studies of protein metabolism. Biochem J. 1974 Sep;141(3):655–665. doi: 10.1042/bj1410655. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Janigan D. T., Druet R. L. Experimental amyloidosis. Role of antigenicity and rapid induction. Am J Pathol. 1966 Jun;48(6):1013–1025. [PMC free article] [PubMed] [Google Scholar]
- Kueppers F., Bearn A. G. A possible experimental approach to the association of hereditary alpha-1-antitrypsin deficiency and pulmonary emphysema. Proc Soc Exp Biol Med. 1966 Apr;121(4):1207–1209. doi: 10.3181/00379727-121-31006. [DOI] [PubMed] [Google Scholar]
- LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
- Levin M., Franklin E. C., Frangione B., Pras M. The amino acid sequence of a major nonimmunoglobulin component of some amyloid fibrils. J Clin Invest. 1972 Oct;51(10):2773–2776. doi: 10.1172/JCI107098. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Levin M., Pras M., Franklin E. C. Immunologic studies of the major nonimmunoglobulin protein of amyloid. I. Identification and partial characterization of a related serum component. J Exp Med. 1973 Aug 1;138(2):373–380. doi: 10.1084/jem.138.2.373. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Linke R. P., Sipe J. D., Pollock P. S., Ignaczak T. F., Glenner G. G. Isolation of a low-molecular-weight serum component antigenically related to an amyloid fibril protein of unknown origin. Proc Natl Acad Sci U S A. 1975 Apr;72(4):1473–1476. doi: 10.1073/pnas.72.4.1473. [DOI] [PMC free article] [PubMed] [Google Scholar]
- McFARLANE A. S. The behavior of I 131-labeled plasma proteins in vivo. Ann N Y Acad Sci. 1957 Aug 30;70(1):19–25. doi: 10.1111/j.1749-6632.1957.tb35374.x. [DOI] [PubMed] [Google Scholar]
- Pruzanski W., Katz A., Nyburg S. C., Freedman M. H. In vitro production of an amyloid-like substance from gamma 3 heavy chain disease protein. Immunol Commun. 1974;3(5):469–476. doi: 10.3109/08820137409061126. [DOI] [PubMed] [Google Scholar]
- Rosenthal C. J., Franklin E. C. Age-associated changes of an amyloid related serum component. Trans Assoc Am Physicians. 1974;87:159–168. [PubMed] [Google Scholar]
- Shirahama T., Cohen A. S. Intralysosomal formation of amyloid fibrils. Am J Pathol. 1975 Oct;81(1):101–116. [PMC free article] [PubMed] [Google Scholar]
- Skinner M., Cathcart E. S., Cohen A. S., Benson M. D. Isolation and identification by sequence analysis of experimentally induced guinea pig amyloid fibrils. J Exp Med. 1974 Sep 1;140(3):871–876. doi: 10.1084/jem.140.3.871. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Sletten K., Husby G. The complete amino-acid sequence of non-immunoglobulin amyloid fibril protein AS in rheumatoid arthritis. Eur J Biochem. 1974 Jan 3;41(1):117–125. doi: 10.1111/j.1432-1033.1974.tb03251.x. [DOI] [PubMed] [Google Scholar]
- Stephen J. M., Waterlow J. C. Use of carbon-14-labelled arginine to measure the catabolic rate of serum and liver proteins and the extent of amino-acid recycling. Nature. 1966 Aug 27;211(5052):978–980. doi: 10.1038/211978a0. [DOI] [PubMed] [Google Scholar]
- Waterlow J. C., Stephen J. M. The effect of low protein diets on the turn-over rates of serums, liver and muscle proteins in the rat, measured by continuous infusion of L-[14C]lysine. Clin Sci. 1968 Oct;35(2):287–305. [PubMed] [Google Scholar]



