help button home button Am J Pathol R & D Systems
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS

This Article
Right arrow Order Full text via Infotrieve
Services
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 Melvin, T.
Right arrow Articles by Michael, A. F.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Melvin, T.
Right arrow Articles by Michael, A. F.

American Journal of Pathology, Vol 125, 460-464, Copyright © 1986 by American Society for Investigative Pathology


REGULAR ARTICLES

Amyloid P component is not present in the glomerular basement membrane in Alport-type hereditary nephritis

T Melvin, Y Kim and AF Michael

Serum amyloid P component (SAP) is a normal plasma glycoprotein immunochemically indistinguishable from amyloid P, a glycoprotein found in all tissue amyloid deposits. SAP has also been shown to be a constituent of normal glomerular basement membrane (GBM). In this study the authors discovered a unique association between SAP and Goodpasture (GP) antigen. In those patients whose GBM lack GP antigen (those with Alport-type hereditary nephritis) SAP is also uniformly absent. Although the relationship between these two components is unknown, this association may provide clues to the abnormality of GBM in Alport-type hereditary nephritis.


This article has been cited by other articles:


Home page
J. Leukoc. Biol.Home page
D. D. Shao, R. Suresh, V. Vakil, R. H. Gomer, and D. Pilling
Pivotal Advance: Th-1 cytokines inhibit, and Th-2 cytokines promote fibrocyte differentiation
J. Leukoc. Biol., June 1, 2008; 83(6): 1323 - 1333.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
K. Zahedi and K. Zahedi
Characterization of the Binding of Serum Amyloid P to Laminin
J. Biol. Chem., January 24, 1997; 272(4): 2143 - 2148.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
K. Zahedi and K. Zahedi
Characterization of the Binding of Serum Amyloid P to Type IV Collagen
J. Biol. Chem., June 21, 1996; 271(25): 14897 - 14902.
[Abstract] [Full Text] [PDF]




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Copyright © 1986 by the American Society for Investigative Pathology.