Amyloidosis

Edward C. Franklin1, E. C. Franklin1
1Irvington House Institute Rheumatic Diseases Study Group and the Department of Medicine, New York University School of Medicine, USA

Tóm tắt

Recenti ricerche hanno fornito i seguenti dati sull’amiloide: 1) esso ha natura proteica fibrillare, con catatteristico aspetto al microscopio elettronico e alla diffrazione ai raggi X; 2) esistono due tipi immunochimici principali delle proteine dell’amiloide: il primo è correlate con le catene leggere delle immunoglobuline, il secondo è una proteina finora non identificata. Il primo si riscontra nella forma primaria ed in quella associata al mieloma, mentre il secondo è la componente principale della forma secondaria ed in certi tipi di amiloidosi familiare; 3) le proteine correlate a queste forme sono presenti nel siero e possono essere utilizzate come precursori.

Tài liệu tham khảo

Andrade C., Araki S., Block W. D., Cohen A. S., Jackson C. E., Kuroiwa Y., McKusick V. A., Nissim J., Sohar E., van Allen M. W.: Hereditary Amyloidosis - Arthr. and Rheum.13, 902, 1970. Benditt E. P., Eriksen N.: Chemical Classes of Amyloid Substance - Amer. J. Path.65, 231, 1971. Benditt E. P., Eriksen N., Hermodson M. A., Ericsson L. H.: The Major Proteins of Human and Monkey Amyloid Substance: Common Properties Including Unusual N-Terminal Amino Acid Sequences - Febs Letters19, 169, 1971. Bladen H. A., Nylen M. U., Glenner G. G.: The Ultrastructure of Human Amyloid as Revealed by the Negative Staining Technique - J. Ultrastruct. Res.14, 449, 1966. Brandt K., Cathcart E. S., Cohen A. S.: A Clinical Analysis of the Course and Prognosis of 42 Patients with Amyloidosis - Amer J. Med.44, 955, 1968. Cohen A. S.: Amyloidosis - New Engl. J. Med.277, 522, 1967. Cohen A. S., Calkins E.: Electron Microscopic Observations on a Fibrous Component in Amyloid of Diverse Origins- Nature (Lond.)183, 1202, 1959. Ein D., Kemura S., Terry W. D., Magnotta J., Glenner G. G.: Amino Acid Sequence of an Amyloid Protein of Unknown Origin - J. biol. Chem.247, 5653, 1972. Franklin E. C., Pras M.: Immunologie Studies of Water-Soluble Human Amyloid Fibrils. Comparative Studies of 8 Amyloid Preparations - J. exp. Med.130, 797, 1969. Franklin E. C., Zucker-Franklin D.: Current Concepts of Amyloidosis - Advanc. Immunol.15, 249, 1972. Franklin E. C., Zucker-Franklin D.: Antisera Specific for Human Amyloid Reactive with Conformational Antigens- Proc. Soc. exp. Biol. (N.Y.)140, 565, 1972. Glenner G. G., Ein D., Eanes E. D., Bladen H. A., Terry W. D., Page D. L.: Creation of ‘Amyloid’ Fibrils from Bence Jones Proteins in Vitro - Science174, 712, 1971. Glenner G. G., Terry W. D., Harada M., Isersky C., Page D. L.: Amyloid Fibrils Proteins: Proof of Homology with Immunoglobulin Light Chains by Sequence Analysis - Science172, 1150, 1971. Glenner G. G., Terry W. D., Isersky C.: Amyloidosis, Its Nature and Pathogenesis - Sem. Hemat.10, 65, 1973. Husby G., Natvig J. B., Michaelson T. E.: Amyloid Subunit as a Unique Protein Common to Different Types of Amyloid Fibrils - Nature (Lond.)244, 362, 1973. Husby G., Sletten K., Michaelson T. E., Natvig J. B.: Antigenic and Chemical Characterization of Non-Immunoglobulin Amyloid Proteins - Scand. J. Immunol.1, 393, 1972. Isersky C., Ein D., Page D. L., Harada M., Glenner G. G.: Immunochemical Cross Reactions of Human Amyloid Proteins with Immunoglobulin Light Chains - J. Immunol.108, 486, 1972. Levin M., Franklin E. C., Frangione B., Pras M.: The Amino Acid Sequence of the Major Non-Immunoglobulin Components of Some Amyloid Fibrils - J. clin. Invest.51, 2773, 1972. Levin M., Pras M., Franklin E. C.: Immunologic Studies of the Major Non-Immunoglobulin Components of Amyloid. I. Identification and Characterization of a Related Serum Component - J. exp. Med.138, 373, 1973. Linke R., Zucker-Franklin D., Franklin E. C.: Morphologic, Chemical, and Immunologic Studies of Amyloid-Like Fibrils Formed from Bence Jones Proteins by Proteolysis - J. Immunol.111, 10, 1973. Mellors R. C., Ortega L. G.: Analytical Pathology. III. New Observations on Pathogenesis of Glomerulonephritis, Lipid Nephrosis, Periarteritis Nodosa and Secondary Amyloidosis in Man - Amer. J. Path.32, 455, 1956. Pras M., Reshef T.: The Acid-Soluble Fraction of Amyloid: A Fibril-Forming Protein - Biochem. biophys. Acta271, 193, 1972. Pras M., Schubert M., Zucker-Franklin D., Rimon A., Franklin E. C.: The Characterization of Soluble Amyloid Prepared in Water - J. clin. Invest.47, 924, 1968. Pras M., Zucker-Franklin D., Rimon A., Franklin E. C.: Physical, Chemical and Ultrastructural Studies of Water-Soluble Human Amyloid Fibrils. Comparative Analyses of 9 Amyloid Preparations - J. exp. Med.130, 777, 1969. Ranløv P., Wanstrup J.: Ultrastructural Investigations on the Cellular Morphogenesis of Experimental Mouse Amyloidosis - Acta path. microbiol. scand.71, 575, 1967. Reimann H. A., Koucky R. F., Eklund C. M.: Primary Amyloidosis Limited to Tissue of Mesodermal Origin - Amer. J. Path.11, 977, 1935. Shirahama T., Cohen A. S.: High Resolution Electron Microscopic Analysis of the Amyloid Fibrils - J. Cell Biol.33, 679, 1967. Teilum G.: Origin of Amyloidosis from PAS Positive Reticuloendothelial Cells in Situ and Basic Factors in Pathogenesis - In:Mandema E., Ruinen L., Schulten J. H., Cohen A. S. (Eds): Amyloidosis. Excerpta Medica Foundation, Amsterdam, 1968; p. 37. Terry W. D., Page D. L., Kemura S., Isobe T.Osserman E. F., Glenner G. G.: Structural Identity of Bence Jones and Amyloid Fibril Proteins in a Patient with Plasma Cell Dyscrasia and Amyloidosis - J. clin. Invest.52, 1276, 1973. Vazquez J. J., Dixon F. J.: Immunohistochemical Analysis of Amyloid by the Fluorescence Technique - J. exp. Med.104, 727, 1956. Zucker-Franklin D.: Immunophagocytosis of Human Amyloid Fibrils by Leukocytes - J. Ultrastruct. Res.32, 247, 1970. Zucker-Franklin D., Franklin E. C.: Intracellular Localization of Human Amyloid by Fluorescence and Electron Microscopy - Amer. J. Path.59, 23, 1970.