[Frontiers in Bioscience 3, a27-31, May 11, 1998]

	[Frontiers in Bioscience 3, a27-31, May 11, 1998] Reprints PubMed CAVEAT LECTOR
	THE ALZHEIMER'S PLAQUES, TANGLES AND MEMORY DEFICITS MAY HAVE A COMMON ORIGIN; PART I; A CALCIUM DEFICIT HYPOTHESIS Ming Chen Department of Pharmacology and Therapeutics, University of South Florida, College of Medicine, Tampa, Florida 3361 and Medical Research Service (151), Bay Pines VA Medical Center, St. Petersburg, Florida 33744 Received 4/27/98 Accepted 5/1/98 2. INTRODUCTION Alzheimer's disease (AD) is a cognitive disorder with unknown pathological origin. However, the invariable presence of amyloid plaques and neurofibrillary tangles in most AD patients (1-4) would suggest that the biological processes underlying the cognitive impairments and the formation of the histological lesions may be related. Amyloid plaques are mainly comprised of ß-amyloid protein (Aß), which is derived from ß-amyloid precursor protein (APP). Processing of APP normally occurs within the Aß region by a putative a -secretase thus precluding the formation of Aß. For unknown reasons, APP in AD is excessively cleaved by two other proteases, ß-/g -secretases, resulting in an overproduction of Aß (1,2).

[Frontiers in Bioscience 3, a27-31, May 11, 1998]
Reprints
PubMed
CAVEAT LECTOR

THE ALZHEIMER'S PLAQUES, TANGLES AND MEMORY DEFICITS MAY HAVE A COMMON ORIGIN; PART I; A CALCIUM DEFICIT HYPOTHESIS

Ming Chen

Department of Pharmacology and Therapeutics, University of South Florida, College of Medicine, Tampa, Florida 3361 and Medical Research Service (151), Bay Pines VA Medical Center, St. Petersburg, Florida 33744

Received 4/27/98 Accepted 5/1/98

2. INTRODUCTION

Alzheimer's disease (AD) is a cognitive disorder with unknown pathological origin. However, the invariable presence of amyloid plaques and neurofibrillary tangles in most AD patients (1-4) would suggest that the biological processes underlying the cognitive impairments and the formation of the histological lesions may be related. Amyloid plaques are mainly comprised of ß-amyloid protein (Aß), which is derived from ß-amyloid precursor protein (APP). Processing of APP normally occurs within the Aß region by a putative a -secretase thus precluding the formation of Aß. For unknown reasons, APP in AD is excessively cleaved by two other proteases, ß-/g -secretases, resulting in an overproduction of Aß (1,2).