| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
American Journal of Pathology, Vol 108, 135-139, Copyright © 1982 by American Society for Investigative Pathology
REGULAR ARTICLES |
GG Cornwell 3d, P Westermark, W Murdoch and P Pitkanen
Department of Medicine, Dartmouth Medical School, Hanover, New Hampshire 03755.
Aortic tissues from 22 elderly patients were analyzed by Congo red staining for amyloid deposits. All samples contained amyloid, which was resistant to the potassium permanganate reaction. Tryptophan was present in all amyloid deposits. The amyloid failed to react with antiserums to amyloid fibril protein ASc1 or human prealbumin, proteins previous demonstrated in generalized senile cardiac amyloid. It also differed from age-related isolated atrial amyloid, which has been shown to lack tryptophan. Deposits did not react with antiserums specific for amyloid fibril proteins of the A lambda IV, A lambda VI, AA, or AEt types. These results indicate that senile aortic amyloid is distinct from amyloid present in primary and secondary amyloidosis and appears to represent a third form of cardiovascular amyloid associated with the aging process.
This article has been cited by other articles:
![]() |
I Kholova and H W M Niessen Amyloid in the cardiovascular system: a review J. Clin. Pathol., February 1, 2005; 58(2): 125 - 133. [Abstract] [Full Text] [PDF] |
||||
![]() |
H. T. Blumenthal Amyloidosis: A Universal Disease of Aging? J. Gerontol. A Biol. Sci. Med. Sci., April 1, 2004; 59(4): M361 - M369. [Full Text] [PDF] |
||||
![]() |
H. T. Blumenthal Guest Editorial: The Autopsy in Gerontological Research: A Retrospective J. Gerontol. A Biol. Sci. Med. Sci., July 1, 2002; 57(7): M433 - 437. [Full Text] |
||||
| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |