| BCHE — Butyrylcholinesterase | |
|---|---|
| Symbol | BCHE |
| Full Name | Butyrylcholinesterase (Pseudocholinesterase) |
| Chromosome | 3q26.1-q26.2 |
| NCBI Gene | 163 |
| Ensembl | ENSG00000114200 |
| OMIM | 177400 |
| UniProt | P06276 |
| Diseases | Alzheimer's Disease, Mild Cognitive Impairment |
| Expression | Liver, Brain (cerebral cortex, hippocampus, basal forebrain), Serum |
Bche Gene Butyrylcholinesterase is an important component in the neurobiology of neurodegenerative diseases. This page provides detailed information about its structure, function, and role in disease processes.
BCHE (Butyrylcholinesterase, also known as pseudocholinesterase or BuChE) is a gene located on chromosome 3q26.1-q26.2 that encodes the enzyme butyrylcholinesterase, a member of the cholinesterase family [1]. BCHE is approximately 7.5 kilobases long and contains 4 exons. The encoded protein is a 574-amino acid glycoprotein synthesized primarily in the liver and secreted into the plasma [2].
While traditionally studied for its role in drug metabolism (particularly suxamethonium hydrolysis), BCHE has emerged as an important modulator of neurodegenerative processes, particularly in Alzheimer's Disease (AD) [3]. The BCHE enzyme hydrolyzes acetylcholine and other choline esters, serving as a secondary cholinergic system that becomes more important when acetylcholinesterase activity declines [4].
Butyrylcholinesterase (BuChE) is a serine hydrolase that catalyzes the hydrolysis of acetylcholine (ACh), butyrylcholine, and other choline esters [1]. Unlike acetylcholinesterase (AChE), which is primarily localized at neuronal synapses, BuChE is found in:
In the brain, BuChE activity is localized to:
BuChE contributes to cholinergic signaling by hydrolyzing acetylcholine, thereby terminating synaptic transmission and regulating cholinergic tone [4]. Under normal conditions, AChE is the primary acetylcholine-terminating enzyme. However, in aging and AD, BuChE activity increases while AChE activity decreases, suggesting that BuChE may partially compensate for lost AChE function [5].
Emerging evidence suggests BCHE may interact with amyloid precursor protein (APP) processing and amyloid-beta (Aβ) metabolism [6]. The enzyme has been shown to:
BCHE is most strongly associated with Alzheimer's Disease through multiple mechanisms [3][5]:
The BCHE-K variant (Atypical butyrylcholinesterase, codon 70 mutation) has been linked to:
AD is characterized by profound loss of basal forebrain cholinergic neurons and decreased acetylcholine levels in the hippocampus and cortex [3]. BCHE activity increases in AD brain tissue and cerebrospinal fluid, potentially reflecting:
Interaction
BCHE colocalizes with amyloid deposits in AD brain and cerebral amyloid angiopathy (CAA), suggesting a role in vascular amyloid clearance and Aβ metabolism [6].
Elevated BCHE activity has been detected in individuals with Mild Cognitive Impairment (MCI), particularly those who progress to AD [8]. BCHE is being investigated as a:
| Variant | Effect | Clinical Relevance |
|---|---|---|
| BCHE-K (Atypical) | Asp70Ala (D70A) | Altered drug sensitivity, potential AD modifier |
| BCHE-A | Various | Butyrylcholinesterase deficiency |
| -116A>G | Promoter variant | Altered expression levels |
Like acetylcholinesterase inhibitors (donepezil, rivastigmine, galantamine), BCHE inhibitors are being explored as AD therapeutics [10]:
BCHE expression in the brain is primarily in non-neuronal cells:
Expression data is available from the Allen Human Brain Atlas.
The study of Bche Gene Butyrylcholinesterase has evolved significantly over the past decades. Research in this area has revealed important insights into the underlying mechanisms of neurodegeneration and continues to drive therapeutic development.
Historical context and key discoveries in this field have shaped our current understanding and will continue to guide future research directions.