Human antimicrobial peptide LL-37 contributes to Alzheimer’s disease progression

As a prime mover in Alzheimer’s disease (AD), microglial activation requires membrane translocation, integration, and activation of the metamorphic protein chloride intracellular channel 1 (CLIC1), which is primarily cytoplasmic under physiological conditions. However, the formation and activation m...

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Published inMolecular psychiatry Vol. 27; no. 11; pp. 4790 - 4799
Main Authors Chen, Xue, Deng, Suixin, Wang, Wenchao, Castiglione, Stefania, Duan, Zilei, Luo, Lei, Cianci, Francesca, Zhang, Xiaoxue, Xu, Jianglei, Li, Hao, Zhao, Jizong, Kamau, Peter Muiruri, Zhang, Zhiye, Mwangi, James, Li, Jiali, Shu, Yousheng, Hu, Xintian, Mazzanti, Michele, Lai, Ren
Format Journal Article
LanguageEnglish
Published London Nature Publishing Group UK 01.11.2022
Nature Publishing Group
Subjects
13/1
13/2
13/21
13/51
14/19
631/378
631/80
64/110
64/60
Alzheimer Disease - metabolism
Alzheimer Disease - pathology
Alzheimer's disease
Amyloid beta-Peptides - metabolism
Animal models
Animals
Antimicrobial agents
Antimicrobial peptides
Atrophy
Behavioral Sciences
Biological Psychology
Cathelicidins - metabolism
Cathelicidins - pharmacology
Chloride Channels - metabolism
Cognition
Excitotoxicity
Humans
Inflammation
Medicine
Medicine & Public Health
Mice
Microglia - metabolism
Neurodegenerative diseases
Neurofibrillary tangles
Neurosciences
Peptides
Pharmacotherapy
Phenotypes
Psychiatry
Synaptic plasticity
Ventricle (lateral)
β-Amyloid
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Abstract As a prime mover in Alzheimer’s disease (AD), microglial activation requires membrane translocation, integration, and activation of the metamorphic protein chloride intracellular channel 1 (CLIC1), which is primarily cytoplasmic under physiological conditions. However, the formation and activation mechanisms of functional CLIC1 are unknown. Here, we found that the human antimicrobial peptide (AMP) LL-37 promoted CLIC1 membrane translocation and integration. It also activates CLIC1 to cause microglial hyperactivation, neuroinflammation, and excitotoxicity. In mouse and monkey models, LL-37 caused significant pathological phenotypes linked to AD, including elevated amyloid-β, increased neurofibrillary tangles, enhanced neuronal death and brain atrophy, enlargement of lateral ventricles, and impairment of synaptic plasticity and cognition, while Clic1 knockout and blockade of LL-37-CLIC1 interactions inhibited these phenotypes. Given AD’s association with infection and that overloading AMP may exacerbate AD, this study suggests that LL-37, which is up-regulated upon infection, may be a driving force behind AD by acting as an endogenous agonist of CLIC1.
AbstractList As a prime mover in Alzheimer’s disease (AD), microglial activation requires membrane translocation, integration, and activation of the metamorphic protein chloride intracellular channel 1 (CLIC1), which is primarily cytoplasmic under physiological conditions. However, the formation and activation mechanisms of functional CLIC1 are unknown. Here, we found that the human antimicrobial peptide (AMP) LL-37 promoted CLIC1 membrane translocation and integration. It also activates CLIC1 to cause microglial hyperactivation, neuroinflammation, and excitotoxicity. In mouse and monkey models, LL-37 caused significant pathological phenotypes linked to AD, including elevated amyloid-β, increased neurofibrillary tangles, enhanced neuronal death and brain atrophy, enlargement of lateral ventricles, and impairment of synaptic plasticity and cognition, while Clic1 knockout and blockade of LL-37-CLIC1 interactions inhibited these phenotypes. Given AD’s association with infection and that overloading AMP may exacerbate AD, this study suggests that LL-37, which is up-regulated upon infection, may be a driving force behind AD by acting as an endogenous agonist of CLIC1.
As a prime mover in Alzheimer's disease (AD), microglial activation requires membrane translocation, integration, and activation of the metamorphic protein chloride intracellular channel 1 (CLIC1), which is primarily cytoplasmic under physiological conditions. However, the formation and activation mechanisms of functional CLIC1 are unknown. Here, we found that the human antimicrobial peptide (AMP) LL-37 promoted CLIC1 membrane translocation and integration. It also activates CLIC1 to cause microglial hyperactivation, neuroinflammation, and excitotoxicity. In mouse and monkey models, LL-37 caused significant pathological phenotypes linked to AD, including elevated amyloid-β, increased neurofibrillary tangles, enhanced neuronal death and brain atrophy, enlargement of lateral ventricles, and impairment of synaptic plasticity and cognition, while Clic1 knockout and blockade of LL-37-CLIC1 interactions inhibited these phenotypes. Given AD's association with infection and that overloading AMP may exacerbate AD, this study suggests that LL-37, which is up-regulated upon infection, may be a driving force behind AD by acting as an endogenous agonist of CLIC1.
Author Mazzanti, Michele
Zhao, Jizong
Zhang, Zhiye
Deng, Suixin
Cianci, Francesca
Li, Hao
Xu, Jianglei
Lai, Ren
Castiglione, Stefania
Luo, Lei
Chen, Xue
Zhang, Xiaoxue
Mwangi, James
Li, Jiali
Wang, Wenchao
Kamau, Peter Muiruri
Duan, Zilei
Shu, Yousheng
Hu, Xintian
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Snippet As a prime mover in Alzheimer’s disease (AD), microglial activation requires membrane translocation, integration, and activation of the metamorphic protein...
As a prime mover in Alzheimer's disease (AD), microglial activation requires membrane translocation, integration, and activation of the metamorphic protein...
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SubjectTerms 13/1
13/2
13/21
13/51
14/19
631/378
631/80
64/110
64/60
Alzheimer Disease - metabolism
Alzheimer Disease - pathology
Alzheimer's disease
Amyloid beta-Peptides - metabolism
Animal models
Animals
Antimicrobial agents
Antimicrobial peptides
Atrophy
Behavioral Sciences
Biological Psychology
Cathelicidins - metabolism
Cathelicidins - pharmacology
Chloride Channels - metabolism
Cognition
Excitotoxicity
Humans
Inflammation
Medicine
Medicine & Public Health
Mice
Microglia - metabolism
Neurodegenerative diseases
Neurofibrillary tangles
Neurosciences
Peptides
Pharmacotherapy
Phenotypes
Psychiatry
Synaptic plasticity
Ventricle (lateral)
β-Amyloid
Title Human antimicrobial peptide LL-37 contributes to Alzheimer’s disease progression
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https://www.ncbi.nlm.nih.gov/pubmed/36138130
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