This Article Order Full text via Infotrieve Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Gallo, G. Articles by Frangione, B. Search for Related Content PubMed PubMed Citation Articles by Gallo, G. Articles by Frangione, B.

American Journal of Pathology, Vol 145, 526-530, Copyright © 1994 by American Society for Investigative Pathology

REGULAR ARTICLES

Potential role of apolipoprotein-E in fibrillogenesis

G Gallo, T Wisniewski, NH Choi-Miura, J Ghiso and B Frangione
Department of Pathology, New York University Medical Center, NY 10016.

Immunohistochemical and biochemical studies have demonstrated several different proteins in amyloid deposits that are not intrinsic components of the fibril itself but may play a role in their deposition and fibril formation. We compared the distribution of several amyloid- associated proteins, ie, amyloid P component, apolipoprotein-E, apolipoprotein-J, and vitronectin, in the deposits of several different amyloids, in particular light chain amyloid, with those in the deposits of nonamyloid monoclonal immunoglobulin, which may be considered a form of preamyloid disease. Although 100% of amyloid specimens (7 amyloid A, 15 immunoglobulin light chain, and 1 transthyretin) had amyloid P component and 100% had apolipoprotein-E (2 amyloid A, 10 immunoglobulin light chain, and 1 transthyretin) co-localized with the primary amyloid protein, none of the monoclonal nonamyloid cases (14 light chain deposition disease and 6 light and heavy chain deposition disease) had amyloid P component and only 1 of 11 had apolipoprotein-E. On the other hand, staining for apolipoprotein-J and vitronectin was positive in 100% of cases of amyloid and nonamyloid monoclonal deposits. The association between the presence of apolipoprotein-E and amyloid P component in the fibrillar form of monoclonal light chain deposits and their absence in the nonfibrillar form of deposits suggest a role for these proteins in the process of fibrillogenesis. This lends support for the previously proposed concept that apolipoprotein-E functions as a pathological chaperone by altering the conformation of amyloidogenic proteins.

This article has been cited by other articles:

				S. M. Korbet and M. M. Schwartz Multiple Myeloma J. Am. Soc. Nephrol., September 1, 2006; 17(9): 2533 - 2545. [Full Text] [PDF]

				J. N. Buxbaum Treatment and prevention of the amyloidoses: Can the lessons learned be applied to sporadic inclusion-body myositis? Neurology, January 24, 2006; 66(1_suppl_1): S110 - S113. [Abstract] [Full Text] [PDF]

				C. A. MacRaild, C. R. Stewart, Y.-F. Mok, M. J. Gunzburg, M. A. Perugini, L. J. Lawrence, V. Tirtaatmadja, J. J. Cooper-White, and G. J. Howlett Non-fibrillar Components of Amyloid Deposits Mediate the Self-association and Tangling of Amyloid Fibrils J. Biol. Chem., May 14, 2004; 279(20): 21038 - 21045. [Abstract] [Full Text] [PDF]

				G. Merlini and V. Bellotti Molecular Mechanisms of Amyloidosis N. Engl. J. Med., August 7, 2003; 349(6): 583 - 596. [Full Text] [PDF]

				T. Oweity, A. B. West, and M. B. Stokes Necrotizing Angiitis of the Small Intestine Related to AA-Amyloidosis: A Novel Association International Journal of Surgical Pathology, April 1, 2001; 9(2): 149 - 154. [Abstract] [PDF]

				R. Vidal, F. Goni, F. Stevens, P. Aucouturier, A. Kumar, B. Frangione, J. Ghiso, and G. Gallo Somatic Mutations of the L12a Gene in V-{kappa}1 Light Chain Deposition Disease : Potential Effects on Aberrant Protein Conformation andDeposition Am. J. Pathol., December 1, 1999; 155(6): 2009 - 2017. [Abstract] [Full Text] [PDF]

				R. L. Comenzo, E. Vosburgh, R. H. Falk, V. Sanchorawala, J. Reisinger, S. Dubrey, L. M. Dember, J. L. Berk, G. Akpek, M. LaValley, et al. Dose-Intensive Melphalan With Blood Stem-Cell Support for the Treatment of AL (Amyloid Light-Chain) Amyloidosis: Survival and Responses in 25 Patients Blood, May 15, 1998; 91(10): 3662 - 3670. [Abstract] [Full Text] [PDF]

				S. S. Kushwaha, J. T. Fallon, and V. Fuster Restrictive Cardiomyopathy N. Engl. J. Med., January 23, 1997; 336(4): 267 - 276. [Full Text] [PDF]

				T. Arendt, C. Schindler, M. K. Bruckner, K. Eschrich, V. Bigl, D. Zedlick, and L. Marcova Plastic Neuronal Remodeling Is Impaired in Patients with Alzheimer's Disease Carrying Apolipoprotein epsilon 4 Allele J. Neurosci., January 15, 1997; 17(2): 516 - 529. [Abstract] [Full Text] [PDF]

				S. Janciauskiene, P. G.ía de Frutos, E. Carlemalm, B.ör. Dahlbäck, and S. Eriksson Inhibition of Alzheimer beta-Peptide Fibril Formation by Serum Amyloid P Component J. Biol. Chem., November 3, 1995; 270(44): 26041 - 26044. [Abstract] [Full Text] [PDF]

				E. M. Castao, F. Prelli, M. Pras, and B. Frangione Apolipoprotein E Carboxyl-terminal Fragments Are Complexed to Amyloids A and L J. Biol. Chem., July 21, 1995; 270(29): 17610 - 17615. [Abstract] [Full Text] [PDF]

				E. Matsubara, B. Frangione, and J. Ghiso Characterization of Apolipoprotein J-Alzheimer's Abeta Interaction J. Biol. Chem., March 31, 1995; 270(13): 7563 - 7567. [Abstract] [Full Text] [PDF]