This Article Order Full text via Infotrieve Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Cochran, E. Articles by Autilio-Gambetti, L. Search for Related Content PubMed PubMed Citation Articles by Cochran, E. Articles by Autilio-Gambetti, L.

American Journal of Pathology, Vol 139, 485-489, Copyright © 1991 by American Society for Investigative Pathology

REGULAR ARTICLES

Amyloid precursor protein and ubiquitin immunoreactivity in dystrophic axons is not unique to Alzheimer's disease

E Cochran, B Bacci, Y Chen, A Patton, P Gambetti and L Autilio-Gambetti
Division of Neuropathology, Case Western Reserve University, Cleveland, Ohio 44106.

A distinctive feature of Alzheimer's disease (AD) is the presence of dystrophic neurites that immunoreact with antibodies to amyloid precursor protein (APP) and ubiquitin (Ub). The authors examined dystrophic axons (DA) present in other chronic conditions such as familial infantile neuroaxonal dystrophy (INAD), aging, cystic fibrosis, and biliary obstruction as well as in conditions of shorter duration such as human immunodeficiency virus (HIV) leucoencephalopathy, infarction and radiation therapy to determine whether APP and Ub immunoreactivity was unique to the DA of AD. A large number of DA immunoreacted with antibodies to the A4, C- and N-terminal regions of APP as well as to Ub. Ub and APP immunoreactivities often, but not always, colocalized. "Acute" DA generally reacted more intensely and in larger number with antibodies to APP than to Ub, whereas the reverse was true for "chronic" DA. Structureless DA immunostained diffusely. In DA with cores or granules, the Ub immunoreaction was occasionally limited to these structures, whereas reaction with antibodies to APP was more diffuse. In view of the contention that impairment of proteolysis is the common pathogenetic step in the formation of DA, Ub immunoreactivity in all DA may indicate a vicarious attempt to degrade accumulated components through an activation of the Ub system. The role of APP in the formation of DA remains to be determined.

This article has been cited by other articles:

				M. J. Craner, B. C. Hains, A. C. Lo, J. A. Black, and S. G. Waxman Co-localization of sodium channel Nav1.6 and the sodium-calcium exchanger at sites of axonal injury in the spinal cord in EAE Brain, February 1, 2004; 127(2): 294 - 303. [Abstract] [Full Text] [PDF]

				Y.-H. Suh and F. Checler Amyloid Precursor Protein, Presenilins, and alpha -Synuclein: Molecular Pathogenesis and Pharmacological Applications in Alzheimer's Disease Pharmacol. Rev., September 1, 2002; 54(3): 469 - 525. [Abstract] [Full Text] [PDF]

				A. Popa-Wagner, E. Schroder, L.C. Walker, C. Kessler, and N. Futrell ß-Amyloid Precursor Protein and ß-Amyloid Peptide Immunoreactivity in the Rat Brain After Middle Cerebral Artery Occlusion : Effect of Age • Editorial Comment: Effect of Age Stroke, October 1, 1998; 29(10): 2196 - 2202. [Abstract] [Full Text] [PDF]

				B. D. Trapp, J. Peterson, R. M. Ransohoff, R. Rudick, S. Mork, and L. Bo Axonal Transection in the Lesions of Multiple Sclerosis N. Engl. J. Med., January 29, 1998; 338(5): 278 - 285. [Abstract] [Full Text] [PDF]