miR‐195 reduces age‐related blood–brain barrier leakage caused by thrombospondin‐1‐mediated selective autophagy
Blood–brain barrier (BBB) disruption contributes to neurodegenerative diseases. Loss of tight junction (TJ) proteins in cerebral endothelial cells (ECs) is a leading cause of BBB breakdown. We recently reported that miR‐195 provides vasoprotection, which urges us to explore the role of miR‐195 in BB...
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| Published in | Aging cell Vol. 19; no. 11; pp. e13236 - n/a |
|---|---|
| Main Authors | , , , , , , , |
| Format | Journal Article |
| Language | English |
| Published |
England
John Wiley & Sons, Inc
01.11.2020
John Wiley and Sons Inc |
| Subjects | |
| Online Access | Get full text |
| ISSN | 1474-9718 1474-9726 1474-9726 |
| DOI | 10.1111/acel.13236 |
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| Abstract | Blood–brain barrier (BBB) disruption contributes to neurodegenerative diseases. Loss of tight junction (TJ) proteins in cerebral endothelial cells (ECs) is a leading cause of BBB breakdown. We recently reported that miR‐195 provides vasoprotection, which urges us to explore the role of miR‐195 in BBB integrity. Here, we found cerebral miR‐195 levels decreased with age, and BBB leakage was significantly increased in miR‐195 knockout mice. Furthermore, exosomes from miR‐195‐enriched astrocytes increased endothelial TJ proteins and improved BBB integrity. To decipher how miR‐195 promoted BBB integrity, we first demonstrated that TJ proteins were metabolized via autophagic–lysosomal pathway and the autophagic adaptor p62 was necessary to promote TJ protein degradation in cerebral ECs. Next, proteomic analysis of exosomes revealed miR‐195‐suppressed thrombospondin‐1 (TSP1) as a major contributor to BBB disruption. Moreover, TSP1 was demonstrated to activate selective autophagy of TJ proteins by increasing the formation of claudin‐5‐p62 and ZO1‐p62 complexes in cerebral ECs while TSP1 impaired general autophagy. Delivering TSP1 antibody into the circulation showed dose‐dependent reduction of BBB leakage by 20%–40% in 25‐month‐old mice. Intravenous or intracerebroventricular injection of miR‐195 rescued TSP1‐induced BBB leakage. Dementia patients with BBB damage had higher levels of serum TSP1 compared to those without BBB damage (p = 0.0015), while the normal subjects had the lowest TSP1 (p < 0.0001). Taken together, the study implies that TSP1‐regulated selective autophagy facilitates the degradation of TJ proteins and weakens BBB integrity. An adequate level of miR‐195 can suppress the autophagy–lysosome pathway via a reduction of TSP1, which may be important for maintaining BBB function.
The present study revealed that thrombospondin‐1 (TSP1) is a key factor for BBB leakage and miR‐195 protects BBB integrity. We showed that cerebral miR‐195 reduces with age and blood‐brain barrier (BBB) leakage is increased in miR‐195 knockout mice. miR‐195‐regulated thrombospondin‐1 impairs BBB via selective autophagy of tight junctions. Furthermore, circulating TSP1 was higher in BBB‐damaged patients, which implied TSP1 as a new biomarker of BBB damage. |
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| AbstractList | Blood–brain barrier (BBB) disruption contributes to neurodegenerative diseases. Loss of tight junction (TJ) proteins in cerebral endothelial cells (ECs) is a leading cause of BBB breakdown. We recently reported that miR‐195 provides vasoprotection, which urges us to explore the role of miR‐195 in BBB integrity. Here, we found cerebral miR‐195 levels decreased with age, and BBB leakage was significantly increased in miR‐195 knockout mice. Furthermore, exosomes from miR‐195‐enriched astrocytes increased endothelial TJ proteins and improved BBB integrity. To decipher how miR‐195 promoted BBB integrity, we first demonstrated that TJ proteins were metabolized via autophagic–lysosomal pathway and the autophagic adaptor p62 was necessary to promote TJ protein degradation in cerebral ECs. Next, proteomic analysis of exosomes revealed miR‐195‐suppressed thrombospondin‐1 (TSP1) as a major contributor to BBB disruption. Moreover, TSP1 was demonstrated to activate selective autophagy of TJ proteins by increasing the formation of claudin‐5‐p62 and ZO1‐p62 complexes in cerebral ECs while TSP1 impaired general autophagy. Delivering TSP1 antibody into the circulation showed dose‐dependent reduction of BBB leakage by 20%–40% in 25‐month‐old mice. Intravenous or intracerebroventricular injection of miR‐195 rescued TSP1‐induced BBB leakage. Dementia patients with BBB damage had higher levels of serum TSP1 compared to those without BBB damage (p = 0.0015), while the normal subjects had the lowest TSP1 (p < 0.0001). Taken together, the study implies that TSP1‐regulated selective autophagy facilitates the degradation of TJ proteins and weakens BBB integrity. An adequate level of miR‐195 can suppress the autophagy–lysosome pathway via a reduction of TSP1, which may be important for maintaining BBB function. Blood–brain barrier (BBB) disruption contributes to neurodegenerative diseases. Loss of tight junction (TJ) proteins in cerebral endothelial cells (ECs) is a leading cause of BBB breakdown. We recently reported that miR‐195 provides vasoprotection, which urges us to explore the role of miR‐195 in BBB integrity. Here, we found cerebral miR‐195 levels decreased with age, and BBB leakage was significantly increased in miR‐195 knockout mice. Furthermore, exosomes from miR‐195‐enriched astrocytes increased endothelial TJ proteins and improved BBB integrity. To decipher how miR‐195 promoted BBB integrity, we first demonstrated that TJ proteins were metabolized via autophagic–lysosomal pathway and the autophagic adaptor p62 was necessary to promote TJ protein degradation in cerebral ECs. Next, proteomic analysis of exosomes revealed miR‐195‐suppressed thrombospondin‐1 (TSP1) as a major contributor to BBB disruption. Moreover, TSP1 was demonstrated to activate selective autophagy of TJ proteins by increasing the formation of claudin‐5‐p62 and ZO1‐p62 complexes in cerebral ECs while TSP1 impaired general autophagy. Delivering TSP1 antibody into the circulation showed dose‐dependent reduction of BBB leakage by 20%–40% in 25‐month‐old mice. Intravenous or intracerebroventricular injection of miR‐195 rescued TSP1‐induced BBB leakage. Dementia patients with BBB damage had higher levels of serum TSP1 compared to those without BBB damage ( p = 0.0015), while the normal subjects had the lowest TSP1 ( p < 0.0001). Taken together, the study implies that TSP1‐regulated selective autophagy facilitates the degradation of TJ proteins and weakens BBB integrity. An adequate level of miR‐195 can suppress the autophagy–lysosome pathway via a reduction of TSP1, which may be important for maintaining BBB function. Blood-brain barrier (BBB) disruption contributes to neurodegenerative diseases. Loss of tight junction (TJ) proteins in cerebral endothelial cells (ECs) is a leading cause of BBB breakdown. We recently reported that miR-195 provides vasoprotection, which urges us to explore the role of miR-195 in BBB integrity. Here, we found cerebral miR-195 levels decreased with age, and BBB leakage was significantly increased in miR-195 knockout mice. Furthermore, exosomes from miR-195-enriched astrocytes increased endothelial TJ proteins and improved BBB integrity. To decipher how miR-195 promoted BBB integrity, we first demonstrated that TJ proteins were metabolized via autophagic-lysosomal pathway and the autophagic adaptor p62 was necessary to promote TJ protein degradation in cerebral ECs. Next, proteomic analysis of exosomes revealed miR-195-suppressed thrombospondin-1 (TSP1) as a major contributor to BBB disruption. Moreover, TSP1 was demonstrated to activate selective autophagy of TJ proteins by increasing the formation of claudin-5-p62 and ZO1-p62 complexes in cerebral ECs while TSP1 impaired general autophagy. Delivering TSP1 antibody into the circulation showed dose-dependent reduction of BBB leakage by 20%-40% in 25-month-old mice. Intravenous or intracerebroventricular injection of miR-195 rescued TSP1-induced BBB leakage. Dementia patients with BBB damage had higher levels of serum TSP1 compared to those without BBB damage (p = 0.0015), while the normal subjects had the lowest TSP1 (p < 0.0001). Taken together, the study implies that TSP1-regulated selective autophagy facilitates the degradation of TJ proteins and weakens BBB integrity. An adequate level of miR-195 can suppress the autophagy-lysosome pathway via a reduction of TSP1, which may be important for maintaining BBB function. Blood–brain barrier (BBB) disruption contributes to neurodegenerative diseases. Loss of tight junction (TJ) proteins in cerebral endothelial cells (ECs) is a leading cause of BBB breakdown. We recently reported that miR‐195 provides vasoprotection, which urges us to explore the role of miR‐195 in BBB integrity. Here, we found cerebral miR‐195 levels decreased with age, and BBB leakage was significantly increased in miR‐195 knockout mice. Furthermore, exosomes from miR‐195‐enriched astrocytes increased endothelial TJ proteins and improved BBB integrity. To decipher how miR‐195 promoted BBB integrity, we first demonstrated that TJ proteins were metabolized via autophagic–lysosomal pathway and the autophagic adaptor p62 was necessary to promote TJ protein degradation in cerebral ECs. Next, proteomic analysis of exosomes revealed miR‐195‐suppressed thrombospondin‐1 (TSP1) as a major contributor to BBB disruption. Moreover, TSP1 was demonstrated to activate selective autophagy of TJ proteins by increasing the formation of claudin‐5‐p62 and ZO1‐p62 complexes in cerebral ECs while TSP1 impaired general autophagy. Delivering TSP1 antibody into the circulation showed dose‐dependent reduction of BBB leakage by 20%–40% in 25‐month‐old mice. Intravenous or intracerebroventricular injection of miR‐195 rescued TSP1‐induced BBB leakage. Dementia patients with BBB damage had higher levels of serum TSP1 compared to those without BBB damage ( p = 0.0015), while the normal subjects had the lowest TSP1 ( p < 0.0001). Taken together, the study implies that TSP1‐regulated selective autophagy facilitates the degradation of TJ proteins and weakens BBB integrity. An adequate level of miR‐195 can suppress the autophagy–lysosome pathway via a reduction of TSP1, which may be important for maintaining BBB function. The present study revealed that thrombospondin‐1 (TSP1) is a key factor for BBB leakage and miR‐195 protects BBB integrity. We showed that cerebral miR‐195 reduces with age and blood‐brain barrier (BBB) leakage is increased in miR‐195 knockout mice. miR‐195‐regulated thrombospondin‐1 impairs BBB via selective autophagy of tight junctions. Furthermore, circulating TSP1 was higher in BBB‐damaged patients, which implied TSP1 as a new biomarker of BBB damage. Blood–brain barrier (BBB) disruption contributes to neurodegenerative diseases. Loss of tight junction (TJ) proteins in cerebral endothelial cells (ECs) is a leading cause of BBB breakdown. We recently reported that miR‐195 provides vasoprotection, which urges us to explore the role of miR‐195 in BBB integrity. Here, we found cerebral miR‐195 levels decreased with age, and BBB leakage was significantly increased in miR‐195 knockout mice. Furthermore, exosomes from miR‐195‐enriched astrocytes increased endothelial TJ proteins and improved BBB integrity. To decipher how miR‐195 promoted BBB integrity, we first demonstrated that TJ proteins were metabolized via autophagic–lysosomal pathway and the autophagic adaptor p62 was necessary to promote TJ protein degradation in cerebral ECs. Next, proteomic analysis of exosomes revealed miR‐195‐suppressed thrombospondin‐1 (TSP1) as a major contributor to BBB disruption. Moreover, TSP1 was demonstrated to activate selective autophagy of TJ proteins by increasing the formation of claudin‐5‐p62 and ZO1‐p62 complexes in cerebral ECs while TSP1 impaired general autophagy. Delivering TSP1 antibody into the circulation showed dose‐dependent reduction of BBB leakage by 20%–40% in 25‐month‐old mice. Intravenous or intracerebroventricular injection of miR‐195 rescued TSP1‐induced BBB leakage. Dementia patients with BBB damage had higher levels of serum TSP1 compared to those without BBB damage (p = 0.0015), while the normal subjects had the lowest TSP1 (p < 0.0001). Taken together, the study implies that TSP1‐regulated selective autophagy facilitates the degradation of TJ proteins and weakens BBB integrity. An adequate level of miR‐195 can suppress the autophagy–lysosome pathway via a reduction of TSP1, which may be important for maintaining BBB function. The present study revealed that thrombospondin‐1 (TSP1) is a key factor for BBB leakage and miR‐195 protects BBB integrity. We showed that cerebral miR‐195 reduces with age and blood‐brain barrier (BBB) leakage is increased in miR‐195 knockout mice. miR‐195‐regulated thrombospondin‐1 impairs BBB via selective autophagy of tight junctions. Furthermore, circulating TSP1 was higher in BBB‐damaged patients, which implied TSP1 as a new biomarker of BBB damage. Blood-brain barrier (BBB) disruption contributes to neurodegenerative diseases. Loss of tight junction (TJ) proteins in cerebral endothelial cells (ECs) is a leading cause of BBB breakdown. We recently reported that miR-195 provides vasoprotection, which urges us to explore the role of miR-195 in BBB integrity. Here, we found cerebral miR-195 levels decreased with age, and BBB leakage was significantly increased in miR-195 knockout mice. Furthermore, exosomes from miR-195-enriched astrocytes increased endothelial TJ proteins and improved BBB integrity. To decipher how miR-195 promoted BBB integrity, we first demonstrated that TJ proteins were metabolized via autophagic-lysosomal pathway and the autophagic adaptor p62 was necessary to promote TJ protein degradation in cerebral ECs. Next, proteomic analysis of exosomes revealed miR-195-suppressed thrombospondin-1 (TSP1) as a major contributor to BBB disruption. Moreover, TSP1 was demonstrated to activate selective autophagy of TJ proteins by increasing the formation of claudin-5-p62 and ZO1-p62 complexes in cerebral ECs while TSP1 impaired general autophagy. Delivering TSP1 antibody into the circulation showed dose-dependent reduction of BBB leakage by 20%-40% in 25-month-old mice. Intravenous or intracerebroventricular injection of miR-195 rescued TSP1-induced BBB leakage. Dementia patients with BBB damage had higher levels of serum TSP1 compared to those without BBB damage (p = 0.0015), while the normal subjects had the lowest TSP1 (p < 0.0001). Taken together, the study implies that TSP1-regulated selective autophagy facilitates the degradation of TJ proteins and weakens BBB integrity. An adequate level of miR-195 can suppress the autophagy-lysosome pathway via a reduction of TSP1, which may be important for maintaining BBB function.Blood-brain barrier (BBB) disruption contributes to neurodegenerative diseases. Loss of tight junction (TJ) proteins in cerebral endothelial cells (ECs) is a leading cause of BBB breakdown. We recently reported that miR-195 provides vasoprotection, which urges us to explore the role of miR-195 in BBB integrity. Here, we found cerebral miR-195 levels decreased with age, and BBB leakage was significantly increased in miR-195 knockout mice. Furthermore, exosomes from miR-195-enriched astrocytes increased endothelial TJ proteins and improved BBB integrity. To decipher how miR-195 promoted BBB integrity, we first demonstrated that TJ proteins were metabolized via autophagic-lysosomal pathway and the autophagic adaptor p62 was necessary to promote TJ protein degradation in cerebral ECs. Next, proteomic analysis of exosomes revealed miR-195-suppressed thrombospondin-1 (TSP1) as a major contributor to BBB disruption. Moreover, TSP1 was demonstrated to activate selective autophagy of TJ proteins by increasing the formation of claudin-5-p62 and ZO1-p62 complexes in cerebral ECs while TSP1 impaired general autophagy. Delivering TSP1 antibody into the circulation showed dose-dependent reduction of BBB leakage by 20%-40% in 25-month-old mice. Intravenous or intracerebroventricular injection of miR-195 rescued TSP1-induced BBB leakage. Dementia patients with BBB damage had higher levels of serum TSP1 compared to those without BBB damage (p = 0.0015), while the normal subjects had the lowest TSP1 (p < 0.0001). Taken together, the study implies that TSP1-regulated selective autophagy facilitates the degradation of TJ proteins and weakens BBB integrity. An adequate level of miR-195 can suppress the autophagy-lysosome pathway via a reduction of TSP1, which may be important for maintaining BBB function. |
| Audience | Academic |
| Author | Yang, Jenq‐Lin Chen, Cheng‐Sheng Chen, Chao‐Jung Chan, Julie Y. H. Lin, Hsiu‐Fen Chen, Chien‐Yuan Chao, Yung‐Mei Juo, Suh‐Hang H. |
| AuthorAffiliation | 9 Department of Medical Research China Medical University Hospital Taichung Taiwan 7 Department of Psychiatry Kaohsiung Medical University Hospital Kaohsiung Taiwan 2 Institute for Translational Research in Biomedicine Chang Gung Memorial Hospital Kaohsiung Taiwan 11 Institute of New Drug Development China Medical University Taichung Taiwan 4 Department of Neurology College of Medicine, Kaohsiung Medical University Kaohsiung Taiwan 6 Graduate Institute of Integrated Medicine China Medical University Taichung Taiwan 3 Department of Neurology Kaohsiung Medical University Hospital Kaohsiung Taiwan 1 Graduate Institute of Medicine College of Medicine, Kaohsiung Medical University Kaohsiung Taiwan 5 Proteomics Core Laboratory Department of Medical Research, China Medical University Hospital Taichung Taiwan 8 Department of Psychiatry College of Medicine, Kaohsiung Medical University Kaohsiung Taiwan 10 Graduate Institute of Biomedical Sciences China Medical University Taichung Taiwan 12 Drug Developmen |
| AuthorAffiliation_xml | – name: 4 Department of Neurology College of Medicine, Kaohsiung Medical University Kaohsiung Taiwan – name: 12 Drug Development Center China Medical University Taichung Taiwan – name: 9 Department of Medical Research China Medical University Hospital Taichung Taiwan – name: 8 Department of Psychiatry College of Medicine, Kaohsiung Medical University Kaohsiung Taiwan – name: 1 Graduate Institute of Medicine College of Medicine, Kaohsiung Medical University Kaohsiung Taiwan – name: 5 Proteomics Core Laboratory Department of Medical Research, China Medical University Hospital Taichung Taiwan – name: 6 Graduate Institute of Integrated Medicine China Medical University Taichung Taiwan – name: 7 Department of Psychiatry Kaohsiung Medical University Hospital Kaohsiung Taiwan – name: 10 Graduate Institute of Biomedical Sciences China Medical University Taichung Taiwan – name: 11 Institute of New Drug Development China Medical University Taichung Taiwan – name: 2 Institute for Translational Research in Biomedicine Chang Gung Memorial Hospital Kaohsiung Taiwan – name: 3 Department of Neurology Kaohsiung Medical University Hospital Kaohsiung Taiwan |
| Author_xml | – sequence: 1 givenname: Chien‐Yuan orcidid: 0000-0003-4811-0682 surname: Chen fullname: Chen, Chien‐Yuan organization: College of Medicine, Kaohsiung Medical University – sequence: 2 givenname: Yung‐Mei surname: Chao fullname: Chao, Yung‐Mei organization: Chang Gung Memorial Hospital – sequence: 3 givenname: Hsiu‐Fen surname: Lin fullname: Lin, Hsiu‐Fen organization: College of Medicine, Kaohsiung Medical University – sequence: 4 givenname: Chao‐Jung surname: Chen fullname: Chen, Chao‐Jung organization: China Medical University – sequence: 5 givenname: Cheng‐Sheng surname: Chen fullname: Chen, Cheng‐Sheng organization: College of Medicine, Kaohsiung Medical University – sequence: 6 givenname: Jenq‐Lin surname: Yang fullname: Yang, Jenq‐Lin organization: Chang Gung Memorial Hospital – sequence: 7 givenname: Julie Y. H. surname: Chan fullname: Chan, Julie Y. H. organization: Chang Gung Memorial Hospital – sequence: 8 givenname: Suh‐Hang H. orcidid: 0000-0001-5445-740X surname: Juo fullname: Juo, Suh‐Hang H. email: hjuo@mail.cmu.edu.tw organization: China Medical University |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/33029941$$D View this record in MEDLINE/PubMed |
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| Copyright | 2020 The Authors. Aging Cell published by Anatomical Society and John Wiley & Sons Ltd 2020 The Authors. Aging Cell published by Anatomical Society and John Wiley & Sons Ltd. COPYRIGHT 2020 John Wiley & Sons, Inc. 2020. This work is published under http://creativecommons.org/licenses/by/4.0/ (the “License”). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License. |
| Copyright_xml | – notice: 2020 The Authors. Aging Cell published by Anatomical Society and John Wiley & Sons Ltd – notice: 2020 The Authors. Aging Cell published by Anatomical Society and John Wiley & Sons Ltd. – notice: COPYRIGHT 2020 John Wiley & Sons, Inc. – notice: 2020. This work is published under http://creativecommons.org/licenses/by/4.0/ (the “License”). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License. |
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| Keywords | blood-brain barrier miR-195 thrombospondin-1 tight junction selective autophagy |
| Language | English |
| License | Attribution 2020 The Authors. Aging Cell published by Anatomical Society and John Wiley & Sons Ltd. This is an open access article under the terms of the http://creativecommons.org/licenses/by/4.0/ License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited. |
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| Snippet | Blood–brain barrier (BBB) disruption contributes to neurodegenerative diseases. Loss of tight junction (TJ) proteins in cerebral endothelial cells (ECs) is a... Blood-brain barrier (BBB) disruption contributes to neurodegenerative diseases. Loss of tight junction (TJ) proteins in cerebral endothelial cells (ECs) is a... |
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| SubjectTerms | Age Analysis Astrocytes Autophagy Blood-brain barrier Brain Dementia disorders Endothelial cells Exosomes Experiments Intravenous administration Leakage Metabolism miR‐195 Nervous system diseases Neurodegenerative diseases Original Permeability Phagocytosis Proteins Proteolysis Rodents selective autophagy Thrombospondin thrombospondin‐1 tight junction |
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| Title | miR‐195 reduces age‐related blood–brain barrier leakage caused by thrombospondin‐1‐mediated selective autophagy |
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