Journal of the American Society of Nephrology
2008 JASN IMPACT FACTOR 7.505 HOME   AUTHOR INFO   EDITORIAL BOARD   SUBSCRIBE   FEEDBACK   ALERTS   HELP 
    advanced
CURRENT ISSUE ARCHIVES JASN Express ONLINE SUBMISSION


Published ahead of print on December 17, 2008
J Am Soc Nephrol 20: 1681-1685, 2009
© 2009 American Society of Nephrology
doi: 10.1681/ASN.2008070813
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow All Versions of this Article:
ASN.2008070813v1
20/8/1681    most recent
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Picken, M. M.
Right arrow Articles by Linke, R. P.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Picken, M. M.
Right arrow Articles by Linke, R. P.

Pathophysiology of the Renal Biopsy

Nephrotic Syndrome Due to an Amyloidogenic Mutation in Fibrinogen A {alpha} Chain

Maria M. Picken* and Reinhold P. Linke{dagger}

*Department of Pathology, Loyola University Medical Center, Maywood, Illinois; and
{dagger}Reference Center of Amyloid Diseases, Martinsried, Germany

Correspondence: Dr. Maria M. Picken, Department of Pathology, Building 110, Room 2242, Loyola University Medical Center, 2160 South First Avenue, Maywood, IL 60153. Phone: 708-327-2607; Fax: 708-327-2620; E-mail: mpicken{at}lumc.edu, mmpicken{at}aol.com

We identified amyloid derived from a mutant fibrinogen A {alpha} chain associated with one of the hereditary amyloidoses by kidney biopsy. The recognition of molecular and etiologic diversity among amyloidoses has revolutionized the management of systemic amyloidosis and necessitates precision in amyloid typing. Pitfalls and recommendations for the differential diagnosis of renal amyloid and current standards of amyloid typing are briefly discussed. Diagnosis of the amyloidosis type must be based on identification of the chemical composition of the amyloid protein in deposits and not on clinical suspicion, laboratory tests, or genetic testing. A clinical correlation is required to support but not make a diagnosis of amyloid type. If a hereditary form is detected by amyloid protein typing, then molecular studies are indicated. Conversely, in cases in which DNA sequence indicates a mutant amyloid precursor protein, protein analysis of the deposits must provide the definitive evidence. Negative or inconclusive results must be investigated further by a reference laboratory with the capability of applying more sophisticated methods.






HOME CURRENT ISSUE ARCHIVES JASN Express ONLINE SUBMISSION AUTHOR INFO
EDITORIAL BOARD SUBSCRIBE FEEDBACK ALERTS HELP

Copyright © 2009 by the American Society of Nephrology. Online ISSN: 1533-3450 Print ISSN: 1046-6673