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Article ; Online: Corynoxine promotes TFEB/TFE3-mediated autophagy and alleviates Aβ pathology in Alzheimer's disease models.

Guan, Xin-Jie / Deng, Zhi-Qiang / Liu, Jia / Su, Cheng-Fu / Tong, Benjamin Chun-Kit / Zhu, Zhou / Sreenivasmurthy, Sravan Gopalkrishnashetty / Kan, Yu-Xuan / Lu, Ke-Jia / Chu, Carol Pui-Kei / Pi, Rong-Biao / Cheung, King-Ho / Iyaswamy, Ashok / Song, Ju-Xian / Li, Min

Acta pharmacologica Sinica

2024 Volume 45, Issue 5, Page(s) 900–913

Abstract: Autophagy impairment is a key factor in Alzheimer's disease (AD) pathogenesis. TFEB (transcription factor EB) and TFE3 (transcription factor binding to IGHM enhancer 3) are nuclear transcription factors that regulate autophagy and lysosomal biogenesis. ... ...

Abstract	Autophagy impairment is a key factor in Alzheimer's disease (AD) pathogenesis. TFEB (transcription factor EB) and TFE3 (transcription factor binding to IGHM enhancer 3) are nuclear transcription factors that regulate autophagy and lysosomal biogenesis. We previously showed that corynoxine (Cory), a Chinese medicine compound, protects neurons from Parkinson's disease (PD) by activating autophagy. In this study, we investigated the effect of Cory on AD models in vivo and in vitro. We found that Cory improved learning and memory function, increased neuronal autophagy and lysosomal biogenesis, and reduced pathogenic APP-CTFs levels in 5xFAD mice model. Cory activated TFEB/TFE3 by inhibiting AKT/mTOR signaling and stimulating lysosomal calcium release via transient receptor potential mucolipin 1 (TRPML1). Moreover, we demonstrated that TFEB/TFE3 knockdown abolished Cory-induced APP-CTFs degradation in N2aSwedAPP cells. Our findings suggest that Cory promotes TFEB/TFE3-mediated autophagy and alleviates Aβ pathology in AD models.
MeSH term(s)	Basic Helix-Loop-Helix Leucine Zipper Transcription Factors/metabolism ; Animals ; Alzheimer Disease/drug therapy ; Alzheimer Disease/metabolism ; Alzheimer Disease/pathology ; Autophagy/drug effects ; Mice ; Disease Models, Animal ; Lysosomes/metabolism ; Lysosomes/drug effects ; Humans ; Mice, Transgenic ; Amyloid beta-Peptides/metabolism ; Mice, Inbred C57BL ; TOR Serine-Threonine Kinases/metabolism ; Male ; Proto-Oncogene Proteins c-akt/metabolism ; Neurons/drug effects ; Neurons/metabolism ; Neurons/pathology ; Signal Transduction/drug effects ; Amyloid beta-Protein Precursor/metabolism ; Amyloid beta-Protein Precursor/genetics ; Transient Receptor Potential Channels
Chemical Substances	Basic Helix-Loop-Helix Leucine Zipper Transcription Factors ; Tcfeb protein, mouse ; Tcfe3 protein, mouse (136896-33-8) ; Mcoln1 protein, mouse ; Amyloid beta-Peptides ; TOR Serine-Threonine Kinases (EC 2.7.11.1) ; Proto-Oncogene Proteins c-akt (EC 2.7.11.1) ; Amyloid beta-Protein Precursor ; Transient Receptor Potential Channels
Language	English
Publishing date	2024-01-15
Publishing country	United States
Document type	Journal Article
ZDB-ID	1360774-1
ISSN	1745-7254 ; 0253-9756 ; 1671-4083
ISSN (online)	1745-7254
ISSN	0253-9756 ; 1671-4083
DOI	10.1038/s41401-023-01197-1
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Zs.A 1904: Show issues

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Article ; Online: Transcription factor EB: an emerging drug target for neurodegenerative disorders.

Song, Ju-Xian / Liu, Jia / Jiang, Yimin / Wang, Zi-Ying / Li, Min

Drug discovery today

2020 Volume 26, Issue 1, Page(s) 164–172

Abstract: The discovery of transcription factor EB (TFEB) as a master regulator of the autophagy-lysosomal pathway (ALP) has triggered increasing numbers of studies that aim to explore the therapeutic potential of targeting TFEB to treat neurodegenerative ... ...

Abstract	The discovery of transcription factor EB (TFEB) as a master regulator of the autophagy-lysosomal pathway (ALP) has triggered increasing numbers of studies that aim to explore the therapeutic potential of targeting TFEB to treat neurodegenerative disorders (NDs) such as Alzheimer's disease and Parkinson's disease. So far, the findings are exciting and promising. Here, we delineate the dysfunction of the TFEB-mediated ALP in NDs, and we summarize small molecules that have been identified as TFEB activators, along with their protective effects in NDs. We discuss the molecular mechanisms and targets, and the pros and cons of these TFEB activators from the perspective of drug development. Specific and potent small-molecule TFEB activators with ideal brain bioavailability could provide a method for treating NDs.
MeSH term(s)	Autophagy-Related Proteins/metabolism ; Basic Helix-Loop-Helix Leucine Zipper Transcription Factors/agonists ; Basic Helix-Loop-Helix Leucine Zipper Transcription Factors/metabolism ; Brain/drug effects ; Brain/metabolism ; Drug Discovery ; Humans ; Molecular Targeted Therapy ; Neurodegenerative Diseases/drug therapy ; Neurodegenerative Diseases/metabolism ; Proteins/metabolism ; Signal Transduction/drug effects
Chemical Substances	Autophagy-Related Proteins ; Basic Helix-Loop-Helix Leucine Zipper Transcription Factors ; Proteins ; TFEB protein, human ; lysosomal proteins
Language	English
Publishing date	2020-10-22
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	1324988-5
ISSN	1878-5832 ; 1359-6446
ISSN (online)	1878-5832
ISSN	1359-6446
DOI	10.1016/j.drudis.2020.10.013
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Article ; Online: TNEA therapy promotes the autophagic degradation of NLRP3 inflammasome in a transgenic mouse model of Alzheimer's disease via TFEB/TFE3 activation.

Lin, Wenjia / Li, Zhao / Liang, Guangfeng / Zhou, Runjin / Zheng, Xiaoyan / Tao, Rongrong / Huo, Qingwei / Su, Chengfu / Li, Min / Xu, Nenggui / Tang, Chunzhi / Song, Ju-Xian

Journal of neuroinflammation

2023 Volume 20, Issue 1, Page(s) 21

Abstract: Background: The impairment in the autophagy-lysosomal pathway (ALP) and the activation of NLR family pyrin domain containing 3 (NLRP3) inflammasome represent two molecular events leading to neurodegeneration and neuroinflammation in Alzheimer's disease ( ...

Abstract	Background: The impairment in the autophagy-lysosomal pathway (ALP) and the activation of NLR family pyrin domain containing 3 (NLRP3) inflammasome represent two molecular events leading to neurodegeneration and neuroinflammation in Alzheimer's disease (AD), a devastating neurodegenerative disorder without a cure. Previously we demonstrated the cognitive-enhancing effect of a combined electroacupuncture (EA) therapy termed TNEA in a transgenic mouse model of AD, involving activation of transcription factor EB (TFEB), a master regulator of ALP. However, whether and how TNEA inhibits NLRP3 inflammasome via TFEB-mediated ALP in AD remains to be investigated. Methods: 5xFAD mice overexpressing amyloid-β (Aβ) were treated with TNEA or EA on its composing acupoints (GB13 and GV24). The changes in the signaling pathways regulating NLRP3 inflammasome, the association of NLRP3 inflammasome with ALP, and the roles of TFEB/TFE3 in mice brains were determined by immunoblots, immunohistochemistry and AAV-mediated knockdown assays. Results: TNEA inhibits the activation of NLRP3 inflammasome and the release of active interleukin 1β (IL1B) in the hippocampi of 5xFAD mice. Mechanistically, TNEA promoted the autophagic degradation of inflammasome components via activating both TFEB and TFE3 by modulating kinases including AMPK and AKT. The composing acupoints in TNEA showed synergistic effects on regulating these molecular events and memory improvement. Conclusion: Our findings suggest that TNEA attenuates AD-associated memory impairment via promoting TFEB/TFE3-mediated autophagic clearance of Aβ and NLRP3 inflammasome, and partially reveal the molecular basis of combined acupoints therapy originated from ancient wisdom.
MeSH term(s)	Mice ; Animals ; Inflammasomes/metabolism ; Alzheimer Disease/genetics ; Alzheimer Disease/therapy ; Alzheimer Disease/metabolism ; Mice, Transgenic ; NLR Family, Pyrin Domain-Containing 3 Protein/genetics ; NLR Family, Pyrin Domain-Containing 3 Protein/metabolism ; Autophagy ; Amyloid beta-Peptides/metabolism ; Basic Helix-Loop-Helix Leucine Zipper Transcription Factors/genetics
Chemical Substances	Inflammasomes ; NLR Family, Pyrin Domain-Containing 3 Protein ; Amyloid beta-Peptides ; Basic Helix-Loop-Helix Leucine Zipper Transcription Factors ; Nlrp3 protein, mouse
Language	English
Publishing date	2023-02-02
Publishing country	England
Document type	Journal Article
ZDB-ID	2156455-3
ISSN	1742-2094 ; 1742-2094
ISSN (online)	1742-2094
ISSN	1742-2094
DOI	10.1186/s12974-023-02698-w
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Article ; Online: Corrigendum to "Traditional Chinese medicine compounds regulate autophagy for treating neurodegenerative disease: A mechanism review" [ Biomed. Pharamacother. 133, (2021) 110968].

Wang, Zi-Ying / Liu, Jia / Zhu, Zhou / Su, Cheng-Fu / Sreenivasmurthy, Sravan Gopalkrishnashetty / Iyaswamy, Ashok / Lu, Jia-Hong / Chen, Gang / Song, Ju-Xian / Li, Min

Biomedicine & pharmacotherapy = Biomedecine & pharmacotherapie

2023 Volume 164, Page(s) 114979

Language	English
Publishing date	2023-06-05
Publishing country	France
Document type	Published Erratum
ZDB-ID	392415-4
ISSN	1950-6007 ; 0753-3322 ; 0300-0893
ISSN (online)	1950-6007
ISSN	0753-3322 ; 0300-0893
DOI	10.1016/j.biopha.2023.114979
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Article ; Online: Strategies for brain-targeting liposomal delivery of small hydrophobic molecules in the treatment of neurodegenerative diseases.

Wang, Zi-Ying / Sreenivasmurthy, Sravan Gopalkrishnashetty / Song, Ju-Xian / Liu, Jing-Yi / Li, Min

Drug discovery today

2018 Volume 24, Issue 2, Page(s) 595–605

Abstract: Neurodegenerative diseases (NDs), including Alzheimer's disease (AD) and Parkinson's disease (PD), threaten the health of an ever-growing number of older people worldwide; so far, there are no effective cures. Significant efforts have been devoted to ... ...

Abstract	Neurodegenerative diseases (NDs), including Alzheimer's disease (AD) and Parkinson's disease (PD), threaten the health of an ever-growing number of older people worldwide; so far, there are no effective cures. Significant efforts have been devoted to developing new drugs for NDs in recent years, and some small molecules have been shown to be promising in preclinical studies. However, the major challenge for brain-targeting drugs is how to efficiently deliver the drugs across the blood-brain barrier (BBB) to desired targets. To address this issue, liposomal delivery systems have proved to be ideal carriers for neuroprotective small molecules. Here, we summarize recent advances in the brain-targeting liposomal delivery of small hydrophobic molecules (SHMs) and propose strategies for developing liposomal SHMs as disease-modifying neurotherapeutics for NDs.
MeSH term(s)	Animals ; Brain/metabolism ; Humans ; Hydrophobic and Hydrophilic Interactions ; Liposomes ; Neurodegenerative Diseases/drug therapy ; Neurodegenerative Diseases/metabolism ; Neuroprotective Agents/administration & dosage ; Neuroprotective Agents/chemistry
Chemical Substances	Liposomes ; Neuroprotective Agents
Language	English
Publishing date	2018-11-08
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	1324988-5
ISSN	1878-5832 ; 1359-6446
ISSN (online)	1878-5832
ISSN	1359-6446
DOI	10.1016/j.drudis.2018.11.001
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Zs.A 4725: Show issues

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Article ; Online: Theranostic F-SLOH mitigates Alzheimer's disease pathology involving TFEB and ameliorates cognitive functions in Alzheimer's disease models.

Iyaswamy, Ashok / Wang, Xueli / Krishnamoorthi, Senthilkumar / Kaliamoorthy, Venkatapathy / Sreenivasmurthy, Sravan G / Kumar Durairajan, Siva Sundara / Song, Ju-Xian / Tong, Benjamin Chun-Kit / Zhu, Zhou / Su, Cheng-Fu / Liu, Jia / Cheung, King-Ho / Lu, Jia-Hong / Tan, Jie-Qiong / Li, Hung Wing / Wong, Man Shing / Li, Min

Redox biology

2022 Volume 51, Page(s) 102280

Abstract: Accumulation of amyloid-β (Aβ) oligomers and phosphorylated Tau aggregates are crucial pathological events or factors that cause progressive neuronal loss, and cognitive impairments in Alzheimer's disease (AD). Current medications for AD have failed to ... ...

Abstract	Accumulation of amyloid-β (Aβ) oligomers and phosphorylated Tau aggregates are crucial pathological events or factors that cause progressive neuronal loss, and cognitive impairments in Alzheimer's disease (AD). Current medications for AD have failed to halt, much less reverse this neurodegenerative disorder; therefore, there is an urgent need for the development of effective and safe drugs for AD therapy. In the present study, the in vivo therapeutic efficacy of an Aβ-oligomer-targeted fluorescent probe, F-SLOH, was extensively investigated in 5XFAD and 3XTg-AD mouse models. We have shown that F-SLOH exhibits an efficient inhibitory activity against Aβ aggregation in vivo, and acts as an effective theranostic agent for the treatment of multiple neuropathological changes in AD mouse models. F-SLOH has been found to significantly reduce not only the levels of Aβ oligomers, Tau aggregates and plaques but also the levels of amyloid precursor protein (APP) and its metabolites via autophagy lysosomal degradation pathway (ALP) in the brains of 5XFAD and 3XTg-AD mice. It also reduces astrocyte activation and microgliosis ultimately alleviating neuro-inflammation. Furthermore, F-SLOH mitigates hyperphosphorylated Tau aggregates, synaptic deficits and ameliorates synaptic memory function, and cognitive impairment in AD mouse models. The mechanistic studies have shown that F-SLOH promotes the clearance of C-terminal fragment 15 (CTF15) of APP and Paired helical filaments of Tau (PHF1) in stable cell models via the activation of transcription factor EB (TFEB). Moreover, F-SLOH promotes ALP and lysosomal biogenesis for the clearance of soluble, insoluble Aβ, and phospho Tau. Our results unambiguously reveal effective etiological capabilities of theranostic F-SLOH to target and intervene multiple neuropathological changes in AD mouse models. Therefore, F-SLOH demonstrates tremendous therapeutic potential for treating AD in its early stage.
MeSH term(s)	Alzheimer Disease/metabolism ; Amyloid beta-Peptides/metabolism ; Amyloid beta-Protein Precursor/genetics ; Amyloid beta-Protein Precursor/metabolism ; Animals ; Cognition ; Disease Models, Animal ; Mice ; Mice, Transgenic ; Theranostic Nanomedicine ; tau Proteins/metabolism
Chemical Substances	Amyloid beta-Peptides ; Amyloid beta-Protein Precursor ; tau Proteins
Language	English
Publishing date	2022-03-08
Publishing country	Netherlands
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2701011-9
ISSN	2213-2317 ; 2213-2317
ISSN (online)	2213-2317
ISSN	2213-2317
DOI	10.1016/j.redox.2022.102280
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Article ; Online: Electroacupuncture ameliorates beta-amyloid pathology and cognitive impairment in Alzheimer disease via a novel mechanism involving activation of TFEB (transcription factor EB).

Zheng, Xiaoyan / Lin, Wenjia / Jiang, Yimin / Lu, Kejia / Wei, Wenjing / Huo, Qingwei / Cui, Shaoyang / Yang, Xifei / Li, Min / Xu, Nenggui / Tang, Chunzhi / Song, Ju-Xian

Autophagy

2021 Volume 17, Issue 11, Page(s) 3833–3847

Abstract: Alzheimer disease (AD) is the most prevalent neurodegenerative disorder leading to dementia in the elderly. Unfortunately, no cure for AD is available to date. Increasing evidence has proved the roles of misfolded protein aggregation due to impairment of ...

Abstract	Alzheimer disease (AD) is the most prevalent neurodegenerative disorder leading to dementia in the elderly. Unfortunately, no cure for AD is available to date. Increasing evidence has proved the roles of misfolded protein aggregation due to impairment of the macroautophagy/autophagy-lysosomal pathway (ALP) in the pathogenesis of AD, and thus making TFEB (transcription factor EB), which orchestrates ALP, as a promising target for treating AD. As a complementary therapy, acupuncture or electroacupuncture (EA) has been commonly used for treating human diseases. Although the beneficial effects of acupuncture for AD have been primarily studied both pre-clinically and clinically, the real efficacy of acupuncture on AD remains inconclusive and the underlying mechanisms are largely unexplored. In this study, we demonstrated the cognitive-enhancing effect of three-needle EA (TNEA) in an animal model of AD with beta-amyloid (Aβ) pathology (5xFAD). TNEA reduced APP (amyloid beta (A4) precursor protein), C-terminal fragments (CTFs) of APP and Aβ load, and inhibited glial cell activation in the prefrontal cortex and hippocampus of 5xFAD. Mechanistically, TNEA activated TFEB via inhibiting the AKT-MAPK1-MTORC1 pathway, thus promoting ALP in the brains. Therefore, TNEA represents a promising acupuncture therapy for AD, via a novel mechanism involving TFEB activation.
MeSH term(s)	Alzheimer Disease/metabolism ; Alzheimer Disease/pathology ; Alzheimer Disease/therapy ; Amyloid beta-Peptides/metabolism ; Animals ; Basic Helix-Loop-Helix Leucine Zipper Transcription Factors/metabolism ; Brain/metabolism ; Brain/pathology ; Cognitive Dysfunction/metabolism ; Cognitive Dysfunction/pathology ; Cognitive Dysfunction/therapy ; Disease Models, Animal ; Electroacupuncture/methods ; Female ; Lysosomes/metabolism ; Male ; Mice ; Mice, Inbred C57BL ; Microglia/metabolism ; Microglia/pathology ; Morris Water Maze Test
Chemical Substances	Amyloid beta-Peptides ; Basic Helix-Loop-Helix Leucine Zipper Transcription Factors ; Tcfeb protein, mouse
Language	English
Publishing date	2021-02-23
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2454135-7
ISSN	1554-8635 ; 1554-8627
ISSN (online)	1554-8635
ISSN	1554-8627
DOI	10.1080/15548627.2021.1886720
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Zs.A 6741: Show issues

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Article ; Online: Qingyangshen mitigates amyloid-β and Tau aggregate defects involving PPARα-TFEB activation in transgenic mice of Alzheimer's disease.

Iyaswamy, Ashok / Krishnamoorthi, Senthil Kumar / Zhang, Huan / Sreenivasmurthy, Sravan G / Zhu, Zhou / Liu, Jia / Su, Cheng-Fu / Guan, Xin-Jie / Wang, Zi-Ying / Cheung, King-Ho / Song, Ju-Xian / Durairajan, Siva Sundara Kumar / Li, Min

Phytomedicine : international journal of phytotherapy and phytopharmacology

2021 Volume 91, Page(s) 153648

Abstract: Background: Alzheimer's disease (AD) is the most common neurodegenerative disease. Deposition of amyloid β plaques (Aβ) and neurofibrillary tangles (NFTs) is the key pathological hallmark of AD. Accumulating evidence suggest that impairment of autophagy- ...

Abstract	Background: Alzheimer's disease (AD) is the most common neurodegenerative disease. Deposition of amyloid β plaques (Aβ) and neurofibrillary tangles (NFTs) is the key pathological hallmark of AD. Accumulating evidence suggest that impairment of autophagy-lysosomal pathway (ALP) plays key roles in AD pathology. Purpose: The present study aims to assess the neuroprotective effects of Qingyangshen (QYS), a Chinese herbal medicine, in AD cellular and animal models and to determine its underlying mechanisms involving ALP regulation. Methods: QYS extract was prepared and its chemical components were characterized by LC/MS. Then the pharmacokinetics and acute toxicity of QYS extract were evaluated. The neuroprotective effects of QYS extract were determined in 3XTg AD mice, by using a series of behavioral tests and biochemical assays, and the mechanisms were examined in vitro. Results: Oral administration of QYS extract improved learning and spatial memory, reduced carboxy-terminal fragments (CTFs), amyloid precursor protein (APP), Aβ and Tau aggregates, and inhibited microgliosis and astrocytosis in the brains of 3XTg mice. Mechanistically, QYS extract increased the expression of PPARα and TFEB, and promoted ALP both in vivo and in vitro. Conclusion: QYS attenuates AD pathology, and improves cognitive function in 3XTg mice, which may be mediated by activation of PPARα-TFEB pathway and the subsequent ALP enhancement. Therefore, QYS may be a promising herbal material for further anti-AD drug discovery.
MeSH term(s)	Alzheimer Disease/drug therapy ; Amyloid beta-Peptides ; Amyloid beta-Protein Precursor/genetics ; Animals ; Basic Helix-Loop-Helix Leucine Zipper Transcription Factors/metabolism ; Disease Models, Animal ; Drugs, Chinese Herbal/pharmacology ; Mice ; Mice, Transgenic ; PPAR alpha/metabolism ; tau Proteins
Chemical Substances	Amyloid beta-Peptides ; Amyloid beta-Protein Precursor ; Basic Helix-Loop-Helix Leucine Zipper Transcription Factors ; Drugs, Chinese Herbal ; PPAR alpha ; Tcfeb protein, mouse ; tau Proteins
Language	English
Publishing date	2021-07-12
Publishing country	Germany
Document type	Journal Article
ZDB-ID	1205240-1
ISSN	1618-095X ; 0944-7113
ISSN (online)	1618-095X
ISSN	0944-7113
DOI	10.1016/j.phymed.2021.153648
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Zs.A 4115: Show issues

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Article ; Online: PPARɑ Ligand Caudatin Improves Cognitive Functions and Mitigates Alzheimer's Disease Defects By Inducing Autophagy in Mice Models.

Journal of neuroimmune pharmacology : the official journal of the Society on NeuroImmune Pharmacology

2023 Volume 18, Issue 3, Page(s) 509–528

Abstract: The autophagy-lysosomal pathway (ALP) is a major cellular machinery involved in the clearance of aggregated proteins in Alzheimer disease (AD). However, ALP is dramatically impaired during AD pathogenesis via accumulation of toxic amyloid beta (Aβ) and ... ...

Abstract	The autophagy-lysosomal pathway (ALP) is a major cellular machinery involved in the clearance of aggregated proteins in Alzheimer disease (AD). However, ALP is dramatically impaired during AD pathogenesis via accumulation of toxic amyloid beta (Aβ) and phosphorylated-Tau (phospho-Tau) proteins in the brain. Therefore, activation of ALP may prevent the increased production of Aβ and phospho-Tau in AD. Peroxisome proliferator-activated receptor alpha (PPARα), a transcription factor that can activate autophagy, and transcriptionally regulate transcription factor EB (TFEB) which is a key regulator of ALP. This suggests that targeting PPARα, to reduce ALP impairment, could be a viable strategy for AD therapy. In this study, we investigated the anti-AD activity of Caudatin, an active constituent of Cynanchum otophyllum (a traditional Chinese medicinal herb, Qing Yang Shen; QYS). We found that Caudatin can bind to PPARα as a ligand and augment the expression of ALP in microglial cells and in the brain of 3XTg-AD mice model. Moreover, Caudatin could activate PPARα and transcriptionally regulates TFEB-augmented lysosomal degradation of Aβ and phosphor-Tau aggregates in AD cell models. Oral administration of Caudatin decreased AD pathogenesis and ameliorated the cognitive dysfunction in 3XTg-AD mouse model. Conclusively, Caudatin can be a potential AD therapeutic agent via activation of PPARα-dependent ALP.
Language	English
Publishing date	2023-09-08
Publishing country	United States
Document type	Journal Article
ZDB-ID	2227405-4
ISSN	1557-1904 ; 1557-1890
ISSN (online)	1557-1904
ISSN	1557-1890
DOI	10.1007/s11481-023-10083-w
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Article ; Online: Hypoxia induces actin cytoskeleton remodeling by regulating the binding of CAPZA1 to F-actin via PIP2 to drive EMT in hepatocellular carcinoma.

Huang, Deng / Cao, Li / Xiao, Le / Song, Ju-Xian / Zhang, Yu-Jun / Zheng, Ping / Zheng, Shu-Guo

Cancer letters

2019 Volume 448, Page(s) 117–127

Abstract: Studies have shown that hypoxia can induce cytoskeletal injury and remodeling through the activation of the RhoA/ROCK signaling pathway by hypoxia-inducible factor-1α (HIF-1α). Our previous study confirmed that CAPZA1 can modulate EMT by regulating actin ...

Abstract	Studies have shown that hypoxia can induce cytoskeletal injury and remodeling through the activation of the RhoA/ROCK signaling pathway by hypoxia-inducible factor-1α (HIF-1α). Our previous study confirmed that CAPZA1 can modulate EMT by regulating actin cytoskeleton remodeling. However, the relationship between HIF-1α and CAPZA1 has not been illustrated. Therefore, this study aimed to investigate the mechanism by which hypoxia induces the remodeling of the actin cytoskeleton by regulating CAPZA1 in hepatocellular carcinoma (HCC) cells. In the present study, we showed that the low expression of CAPZA1 promotes HCC cell invasion and migration in vitro and in vivo by regulating actin cytoskeleton remodeling to drive EMT. Furthermore, we found that the combination of PIP2 and CAPZA1 enables CAPZA1 to be released from the barbed end of F-actin, which in turn drives the remodeling of the actin cytoskeleton. Finally, we confirmed that hypoxia increases PIP2 levels and its binding to CAPZA1 in HCC cells via the HIF-1α/RhoA/ROCK1 pathway. Thus, CAPZA1 and PIP2 could be therapeutic targets to inhibit the invasion and migration promoted by hypoxia in HCC cells.
MeSH term(s)	Actin Cytoskeleton/metabolism ; Actins/metabolism ; CapZ Actin Capping Protein/metabolism ; Carcinoma, Hepatocellular/metabolism ; Epithelial-Mesenchymal Transition/physiology ; Humans ; Hypoxia/physiopathology ; Liver Neoplasms/metabolism ; Phospholipids/metabolism ; Tumor Cells, Cultured
Chemical Substances	Actins ; CAPZA1 protein, human ; CapZ Actin Capping Protein ; Phospholipids
Language	English
Publishing date	2019-02-08
Publishing country	Ireland
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	195674-7
ISSN	1872-7980 ; 0304-3835
ISSN (online)	1872-7980
ISSN	0304-3835
DOI	10.1016/j.canlet.2019.01.042
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