This Article Full Text Full Text (PDF) Data Supplement Submit a response Alert me when this article is cited Alert me when eLetters are posted Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Request Permissions Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Röcken, C. Articles by Bürger, T. Search for Related Content PubMed PubMed Citation Articles by Röcken, C. Articles by Bürger, T.

(Arteriosclerosis, Thrombosis, and Vascular Biology. 2006;26:676.)
© 2006 American Heart Association, Inc.

Letters to the Editor

Prevalence and Pathology of Amyloid in Atherosclerotic Arteries

Christoph Röcken; Jörg Tautenhahn; Frank Bühling; Daniela Sachwitz; Steffi Vöckler; Andreas Goette; Thomas Bürger

From the Departments of Pathology (C.R., D.S., S.V.), General Surgery (J.T.), and Immunology (F.B.), Otto-von-Guericke-University Magdeburg, Germany; the Department of Clinical and Laboratory Medicine (F.B.), Cottbus, Germany; the Division of Cardiology (A.G.), of the Otto-von-Guericke-University Magdeburg, Germany; and the Diakonissen Krankenhaus (T.B.), Kassel, Germany.

Correspondence to Prof Dr med Christoph Röcken, Department of Pathology, Charité University Hospital, Schumannstr. 20/21, D-10117 Berlin, Germany. E-mail rockenc@gmx.de

An extract of the first 250 words of the full text is provided, because this article has no abstract.

To the Editor:

Apolipoprotein AI (AApoAI)–associated amyloidosis is characterized by the deposition of apolipoprotein AI (apoAI) and occurs as a hereditary and a nonhereditary form. Hereditary AApoAI amyloidosis is a systemic disease leading to the deposition of amyloid in various organs and tissues and is caused by germline mutations in the APOA1 gene. Nonhereditary AApoAI amyloid is far more prevalent and characterized by deposits of nonvariant protein in atherosclerotic arteries.^1–3 Despite being linked to the most common cause of morbidity and mortality in Western societies, nonhereditary AApoAI amyloid has achieved only little attention.^1–4 It shares several striking similarities with secondary or reactive AA amyloidosis. Nonhereditary AApoAI amyloid occurs in the background of a local chronic inflammatory reaction, it originates from an apolipoprotein that largely associates with high-density lipoproteins (HDLs), and apoAI-containing HDL is endocytosed and retroendocytosed by macrophages, which, in themselves, are able to form amyloid in vitro. Finally, AApoAI amyloidosis is characterized by the deposition of proteolytic fragments of the precursor protein, leading us to speculate that proteolysis is involved in the pathogenesis of AApoAI amyloid.^1,3 The aim of this study was to gain further insights into the pathology of nonhereditary AApoAI amyloid.

See cover

The prevalence and spatial distribution of amyloid, macrophages, cathepsin B (CathB), cathepsin K (CathK), cathepsin L (CathL), and carboxy methyl lysine (CML) was studied using carotid artery specimens obtained from a consecutive series of all 225 patients undergoing carotid endarterectomy with polyester patch angioplasty (Table I, available online at http://atvb.ahajournals.org) during the period from . . . [Full Text of this Article]

This article has been cited by other articles:

				N. Altaf, P. S. Morgan, A. Moody, S. T. MacSweeney, J. R. Gladman, and D. P. Auer Brain White Matter Hyperintensities Are Associated with Carotid Intraplaque Hemorrhage Radiology, July 1, 2008; 248(1): 202 - 209. [Abstract] [Full Text] [PDF]

				E. Herczenik and M. F. B. G. Gebbink Molecular and cellular aspects of protein misfolding and disease FASEB J, July 1, 2008; 22(7): 2115 - 2133. [Abstract] [Full Text] [PDF]

				J. Herrmann, S. M. Soares, L. O. Lerman, and A. Lerman Potential Role of the Ubiquitin-Proteasome System in Atherosclerosis: Aspects of a Protein Quality Disease J. Am. Coll. Cardiol., May 27, 2008; 51(21): 2003 - 2010. [Abstract] [Full Text] [PDF]

				M. J. Gunzburg, M. A. Perugini, and G. J. Howlett Structural Basis for the Recognition and Cross-linking of Amyloid Fibrils by Human Apolipoprotein E J. Biol. Chem., December 7, 2007; 282(49): 35831 - 35841. [Abstract] [Full Text] [PDF]

				C. R. Stewart, A. Haw III, R. Lopez, T. O. McDonald, J. M. Callaghan, M. J. McConville, K. J. Moore, G. J. Howlett, and K. D. O'Brien Serum amyloid P colocalizes with apolipoproteins in human atheroma: functional implications J. Lipid Res., October 1, 2007; 48(10): 2162 - 2171. [Abstract] [Full Text] [PDF]