Potential Roles of α-amylase in Alzheimer’s Disease: Biomarker and Drug Target

Abstract

: Alzheimer’s disease (AD), the most common form of dementia, is pathologically characterized by the deposition of amyloid-β plaques and the formation of neurofibrillary tangles. In a neurodegenerative brain, glucose metabolism is also impaired and considered as one of the key features in AD patients. The impairment causes a reduction in glucose transporters and the uptake of glucose as well as alterations in the specific activity of glycolytic enzymes. Recently, it has been reported that α-amylase, a polysaccharide-degrading enzyme, is present in the human brain. The enzyme is known to be associated with various diseases such as type 2 diabetes mellitus and hyperamylasaemia. With this information at hand, we hypothesize that α-amylase could have a vital role in the demented brains of AD patients. This review aims to shed insight into the possible link between the expression levels of α-amylase and AD. Lastly, we also cover the diverse role of amylase inhibitors and how they could serve as a therapeutic agent to manage or stop AD progression.

Ecological and toxicological features of the effect of stable cesium on striated muscle tissue (myocardium and skeletal muscles) of mammals

“…The detected α-amylase hyperfermentation (on day 4, an increase in α-amylase by 39.7% was observed, and on day 24, an increase in α-amylase activity by 93.4% was shown compared to intact animals) may indicate two possible mechanisms of its formation. The first is due to the cytotoxic effect of cesium, since α-amylase is found in many types of cells and tissues, and the second is due to the nephrotoxicity of cesium and reduced clearance of the enzyme in the development of renal failure (Chen et al, 2022).…”

Characterization of an α-Amylase from the Honeybee Chalk Brood Pathogen Ascosphaera apis

“…Amylases have been extensively sought after for use in a wide range of clinical and pharmaceutical applications, as well as in the food, detergent, textile, brewing, and distilling industries, because of their nontoxic characteristics [14,16,17]. Amylases have been characterized from almost every group of organisms, including from a wide range of eukaryotes, e.g., animals (including humans), plants, protists, and fungi, as well as from any prokaryotes and Archaea [33][34][35][36]. Fungi, in particular, have been rich sources of amylases with various desirable properties, e.g., thermal, pH, and salt stability, and have been widely used to meet current commercial needs [35,37].…”

“…Amylases have been characterized from almost every group of organisms, including from a wide range of eukaryotes, e.g., animals (including humans), plants, protists, and fungi, as well as from any prokaryotes and Archaea [33][34][35][36]. Fungi, in particular, have been rich sources of amylases with various desirable properties, e.g., thermal, pH, and salt stability, and have been widely used to meet current commercial needs [35,37]. The insect pathogenic fungus A. apis is an important and potentially dangerous pest of bees that has been plagued with population declines in various parts of the world.…”

Genetic factors associated with serum amylase in a Japanese population: combined analysis of copy-number and single-nucleotide variants

“…Elevated amylase levels are used as conventional biomarkers for acute pancreatitis [ 2 ] and indicators of psychological stress [ 3 ]. In recent years, individual differences in amylase levels, even within the normal range have attracted attention as they are significantly associated with food perception and preference [ 3 ], gut microbial patterns [ 4 ], metabolic syndrome, diabetes [ 5 ], obesity, cardiovascular diseases [ 6 ], and neurological diseases [ 7 , 8 ]. However, the important determinants of individual differences in amylase levels and their pathophysiological role remain unclear.…”