Neuroprotective mechanisms of S-allyl-L-cysteine in neurological disease.

Publication date: Feb 01, 2020

S-allyl-L-cysteine (SAC) is a sulfur-containing amino acid present in garlic and exhibits a wide range of biological activities such as antioxidant, anti-inflammatory, and anticancer agent. An earlier study demonstrated that SAC ameliorates oxidative damage in a model of experimental stroke. However, the antioxidant property of SAC does not suffice to explain its beneficial effects in terms of the underlying mechanisms. Endoplasmic reticulum (ER) stress and ER stress-induced cell death have been shown to be involved in various neurological diseases such as brain ischemia, Alzheimer’s disease, Parkinson’s disease, amyotrophic lateral sclerosis and Huntington’s disease. We have previously demonstrated that SAC exerts significant protective effects against ER stress-induced neurotoxicity in cultured rat hippocampal neurons and organotypic hippocampal slice cultures. Recently, we demonstrated that these results are due to the direct suppression of calpain activity via the binding of SAC to this enzyme’s Ca-binding domain. We also found that the protective effects of the side-chain-modified SAC derivatives, S-ethyl-L-cysteine (SEC) and S-propyl-L-cysteine (SPC), against ER stress-induced neurotoxicity were more potent than those of SAC in cultured rat hippocampal neurons. In addition, SAC, SEC and SPC have been shown to decrease the production of amyloid-? peptide in the brains of mice with D-galactose-induced aging. These three hydrophilic cysteine-containing compounds have also been shown to exert neuroprotective effects against dopaminergic neuron injury in a murine model of Parkinson’s disease induced by 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP). In this review, we aim to provide a current overview of the protective actions of SAC and the SAC-related compounds, SEC and SPC, in neurodegenerative disease and discuss the promise of SAC as a prototype for developing novel therapeutic drugs for neurological diseases.

Open Access PDF

Kosuge, Y. Neuroprotective mechanisms of S-allyl-L-cysteine in neurological disease. 06915. 2020 Exp Ther Med (19):2.

Concepts Keywords
Aging Antioxidant
Allyl Neuron
Alzheimer Neurodegeneration
Amino Acid Cysteine
Amyloid Calpain
Amyotrophic Lateral Sclerosis Neuroprotection
Antioxidant Thiols
Brain Ischemia Peptidase
Calpain Chemical substances
Cysteine Neurology
Endoplasmic Reticulum Organ systems
Enzyme Branches of biology
ER Stress Involved neurological diseases
Ethyl
Galactose
Garlic
Hippocampal
Huntington
Hydrophilic
Methyl
MPTP
Murine
Neurodegenerative
Neurological
Neurological Diseases
Neurons
Neuroprotective
Neurotoxicity
Oxidative Damage
Parkinson
Peptide
Phenyl
Propyl
SEC
Side Chain
Stress
Stroke
Sulfur

Semantics

Type Source Name
pathway KEGG Autophagy
drug DRUGBANK Diethylstilbestrol
disease MESH renal
drug DRUGBANK Ribostamycin
drug DRUGBANK Amino acids
disease MESH inflammation
disease MESH cancer
disease MESH Diabetes Complications
drug DRUGBANK Coenzyme M
drug DRUGBANK Calcium
disease MESH hypertension
drug DRUGBANK Activated charcoal
disease MESH neurological disorders
disease MESH pathology
drug DRUGBANK Tunicamycin
drug DRUGBANK Dextrose unspecified form
disease MESH endoplasmic reticulum stress
drug DRUGBANK Ethanol
drug DRUGBANK Trestolone
drug DRUGBANK Streptozocin
disease MESH oxidative stress
disease MESH dissociation
drug DRUGBANK PD150606
drug DRUGBANK Serine
drug DRUGBANK Nerve Growth Factor
disease MESH middle cerebral artery occlusion
drug DRUGBANK Inositol
disease MESH growth
pathway KEGG Apoptosis
drug DRUGBANK (S)-Des-Me-Ampa
drug DRUGBANK Cholesterol
disease MESH death
disease MESH neurodegenerative disease
drug DRUGBANK L-Cysteine
disease MESH stroke
disease MESH brain ischemia
disease MESH amyotrophic lateral sclerosis
drug DRUGBANK Galactose
disease MESH aging
drug DRUGBANK Water

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