Clinical Chemistry AACC Online Job Center
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

Clinical Chemistry 36: 88-91, 1990;
This Article
Right arrow Full Text (PDF)
Right arrow Submit an electronic Letter to
the Editor about this paper
Right arrow Alert me when this article is cited
Right arrow Alert me when eLetters are posted
Right arrow Alert me if a correction is posted
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 HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Ohishi, H.
Right arrow Articles by Schmid, K.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Ohishi, H.
Right arrow Articles by Schmid, K.

Clinical Chemistry, Vol 36, 88-91, Copyright © 1990 by American Association for Clinical Chemistry

Glycosaminoglycans of the hemodialysis-associated carpal synovial amyloid and of amyloid-rich tissues and fibrils of heart, liver, and spleen

H Ohishi, M Skinner, N Sato-Araki, T Okuyama, F Gejyo, A Kimura, AS Cohen and K Schmid
Department of Biochemistry, Boston University School of Medicine, MA 02118.

Significant amounts of glycosaminoglycans (GAGs) were found in amyloid fibril preparations. Using two-dimensional electrophoresis to fractionate GAG mixtures, we quantified and identified for the first time the GAGs of the fibrils from carpal synovium of patients with amyloid associated with chronic hemodialysis. The total GAG content was small, but the GAG distribution (high relative content of chondroitin sulfate and hyaluronic acid and lack of the other GAGs) was unique, unlike that for the other amyloid fibril preparations. The amyloid-rich heart, liver, and spleen tissues, as well as the fibrils isolated from these tissues of patients with systemic forms (primary amyloid and secondary amyloid) of amyloid disease, were also analyzed for GAGs. Fibrils from heart tissue of a patient with primary amyloidosis, now examined for the first time, contained four major GAGs (chondroitin sulfate, dermatan sulfate, hyaluronic acid, and heparan sulfate).


The following articles in journals at HighWire Press have cited this article:


Home page
 Protein Sci.Home page
R. W. Mclaughlin, J. K. De Stigter, L. A. Sikkink, E. M. Baden, and M. Ramirez-Alvarado
The effects of sodium sulfate, glycosaminoglycans, and Congo red on the structure, stability, and amyloid formation of an immunoglobulin light-chain protein
Protein Sci., July 1, 2006; 15(7): 1710 - 1722.
[Abstract] [Full Text] [PDF]

Home page
 Am. J. Pathol.Home page
V. Trinkaus-Randall, M. T. Walsh, S. Steeves, G. Monis, L. H. Connors, and M. Skinner
Cellular Response of Cardiac Fibroblasts to Amyloidogenic Light Chains
Am. J. Pathol., January 1, 2005; 166(1): 197 - 208.
[Abstract] [Full Text] [PDF]

Home page
 J. Am. Soc. Nephrol.Home page
S. Yamamoto, I. Yamaguchi, K. Hasegawa, S. Tsutsumi, Y. Goto, F. Gejyo, and H. Naiki
Glycosaminoglycans Enhance the Trifluoroethanol-Induced Extension of {beta}2-Microglobulin-Related Amyloid Fibrils at a Neutral pH
J. Am. Soc. Nephrol., January 1, 2004; 15(1): 126 - 133.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Copyright © 1990 by the American Association for Clinical Chemistry.