Ethanol-Induced Activation of Myosin Light Chain Kinase Leads to Dysfunction of Tight Junctions and Blood-Brain Barrier Compromise
Background: Brain endothelial cells form the blood‐brain barrier (BBB) that regulates solute and macromolecule flux in and out of the brain, leukocyte migration, and maintains the homeostasis of the central nervous system. BBB dysfunction is associated with disruption of tight junctions (TJ) in the...
Gespeichert in:
| Veröffentlicht in: | Alcoholism, clinical and experimental research clinical and experimental research, 2005-06, Vol.29 (6), p.999-1009 |
|---|---|
| Hauptverfasser: | , , , , , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 1009 |
|---|---|
| container_issue | 6 |
| container_start_page | 999 |
| container_title | Alcoholism, clinical and experimental research |
| container_volume | 29 |
| creator | Haorah, James Heilman, David Knipe, Bryan Chrastil, Jesse Leibhart, Jessica Ghorpade, Anuja Miller, Donald W. Persidsky, Yuri |
| description | Background:
Brain endothelial cells form the blood‐brain barrier (BBB) that regulates solute and macromolecule flux in and out of the brain, leukocyte migration, and maintains the homeostasis of the central nervous system. BBB dysfunction is associated with disruption of tight junctions (TJ) in the brain endothelium. We propose that alcohol abuse may impair BBB permeability through TJ modification.
Methods:
Primary cultured bovine brain microvascular endothelial cells (BBMEC) were treated with 50 mM ethanol (EtOH), and monolayer tightness was assessed by measurement of transendothelial electrical resistance (TEER). Changes in TEER were correlated with alterations in TJ protein distribution occludin, zonula occludens‐1 (ZO‐1), claudin‐5 using immunofluorescence (IF). Expression of myosin light chain (MLC) kinase (MLCK), ZO‐1, claudin‐5, and phosphorylated MLC, occludin and claudin‐5 were determined by immunoprecipitation and Western blot. EtOH‐induced changes in monocyte migration across in vitro BBB constructs were also examined.
Results:
EtOH induced a decrease in TEER of BBMEC monolayers that was reversed by EtOH withdrawal. Treatment of BBMEC with EtOH or its metabolite, acetaldehyde, prior to monocyte application resulted in a 2‐fold increase in monocyte migration across the BBB. IF demonstrated decrease in claudin‐5 staining, occludin translocation from cell borders to cytoplasm and gap formation in EtOH‐treated BBMEC monolayer. These changes paralleled significant increase in phosphorylation of MLC, occludin and claudin‐5. EtOH‐treated BBMEC showed reduction of total occludin and claudin‐5 without changes in ZO‐1 or MLC. TEER decrease, changes in occludin/claudin staining, increase in MLC, occludin and claudin‐5 phosphorylation and enhanced monocyte migration across the BBB were all reversed by inhibition of MLCK. Inhibition of EtOH metabolism in BBMEC also reversed these events.
Conclusion:
These results suggest that EtOH activates MLCK leading to phosphorylation of MLC, occludin and claudin‐5. Cytoskeletal alterations (MLC) and TJ changes (occludin and claudin‐5 phosphorylation) result in BBB impairment (decrease in TEER). TJ compromise is associated with increased monocyte migration across the BBB. |
| doi_str_mv | 10.1097/01.ALC.0000166944.79914.0A |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_67963998</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>67963998</sourcerecordid><originalsourceid>FETCH-LOGICAL-c4419-98f60576fbc1f2e236582c23c9aadcd52cb8c3b3ce8757d4fecc167ba234dd033</originalsourceid><addsrcrecordid>eNqVkUGP1CAcxRujccfVr2CIid5aoVAoXkynOzvu2tVkXbOJF0KBOridskKrztVPLrtTnbNcIOT33vvDS5IXCGYIcvYaoqxq6gzGhSjlhGSMc0QyWD1IFqjAMIU5Yw-TBUSkSCmE5VHyJIRvkSclpY-TI1RwRoucLpLfq3EjB9enZ4OelNGgUqP9IUfrBuA6cLFzwQ6gsV83I6g3Mp7f20EGAxojdQCjAye70E2D-qu4ukfP55sA5KDBsndOp0t_J19K763xoHbbW--2NpinyaNO9sE8m_fj5PPp6qp-lzYf12d11aSKEMRTXnYUFox2rUJdbnJMizJXOVZcSq10kau2VLjFypSsYJp0RilEWStzTLSGGB8nr_a-Mff7ZMIoYroyfS8H46YgKOMUc15G8M0eVN6F4E0nbr3dSr8TCIq7BgREIjYgDg2I-wYErKL4-ZwytVujD9L5yyPwcgZkULLvvByUDQeORo5iErm3e-6n7c3uP0YQVb265JxHh3TvYMNofv1zkP4mvhWzQlx_WIuL80_ry5Mv1-IU_wHXm7JT</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>67963998</pqid></control><display><type>article</type><title>Ethanol-Induced Activation of Myosin Light Chain Kinase Leads to Dysfunction of Tight Junctions and Blood-Brain Barrier Compromise</title><source>MEDLINE</source><source>Wiley Online Library Journals Frontfile Complete</source><source>Journals@Ovid Complete</source><creator>Haorah, James ; Heilman, David ; Knipe, Bryan ; Chrastil, Jesse ; Leibhart, Jessica ; Ghorpade, Anuja ; Miller, Donald W. ; Persidsky, Yuri</creator><creatorcontrib>Haorah, James ; Heilman, David ; Knipe, Bryan ; Chrastil, Jesse ; Leibhart, Jessica ; Ghorpade, Anuja ; Miller, Donald W. ; Persidsky, Yuri</creatorcontrib><description>Background:
Brain endothelial cells form the blood‐brain barrier (BBB) that regulates solute and macromolecule flux in and out of the brain, leukocyte migration, and maintains the homeostasis of the central nervous system. BBB dysfunction is associated with disruption of tight junctions (TJ) in the brain endothelium. We propose that alcohol abuse may impair BBB permeability through TJ modification.
Methods:
Primary cultured bovine brain microvascular endothelial cells (BBMEC) were treated with 50 mM ethanol (EtOH), and monolayer tightness was assessed by measurement of transendothelial electrical resistance (TEER). Changes in TEER were correlated with alterations in TJ protein distribution occludin, zonula occludens‐1 (ZO‐1), claudin‐5 using immunofluorescence (IF). Expression of myosin light chain (MLC) kinase (MLCK), ZO‐1, claudin‐5, and phosphorylated MLC, occludin and claudin‐5 were determined by immunoprecipitation and Western blot. EtOH‐induced changes in monocyte migration across in vitro BBB constructs were also examined.
Results:
EtOH induced a decrease in TEER of BBMEC monolayers that was reversed by EtOH withdrawal. Treatment of BBMEC with EtOH or its metabolite, acetaldehyde, prior to monocyte application resulted in a 2‐fold increase in monocyte migration across the BBB. IF demonstrated decrease in claudin‐5 staining, occludin translocation from cell borders to cytoplasm and gap formation in EtOH‐treated BBMEC monolayer. These changes paralleled significant increase in phosphorylation of MLC, occludin and claudin‐5. EtOH‐treated BBMEC showed reduction of total occludin and claudin‐5 without changes in ZO‐1 or MLC. TEER decrease, changes in occludin/claudin staining, increase in MLC, occludin and claudin‐5 phosphorylation and enhanced monocyte migration across the BBB were all reversed by inhibition of MLCK. Inhibition of EtOH metabolism in BBMEC also reversed these events.
Conclusion:
These results suggest that EtOH activates MLCK leading to phosphorylation of MLC, occludin and claudin‐5. Cytoskeletal alterations (MLC) and TJ changes (occludin and claudin‐5 phosphorylation) result in BBB impairment (decrease in TEER). TJ compromise is associated with increased monocyte migration across the BBB.</description><identifier>ISSN: 0145-6008</identifier><identifier>EISSN: 1530-0277</identifier><identifier>DOI: 10.1097/01.ALC.0000166944.79914.0A</identifier><identifier>PMID: 15976526</identifier><identifier>CODEN: ACRSDM</identifier><language>eng</language><publisher>Oxford, UK: Blackwell Publishing Ltd</publisher><subject>Alcoholism and acute alcohol poisoning ; Animals ; Biological and medical sciences ; Blood-Brain Barrier - drug effects ; Blood-Brain Barrier - enzymology ; Blood-Brain Barrier - physiopathology ; Capillary Permeability - drug effects ; Capillary Permeability - physiology ; Cattle ; Cell Movement - drug effects ; Cell Movement - physiology ; Cells, Cultured ; Electric Impedance ; Endothelial Cells - drug effects ; Endothelial Cells - enzymology ; Endothelial Cells - metabolism ; Enzyme Activation - drug effects ; Ethanol - pharmacokinetics ; Ethanol - pharmacology ; In Vitro Techniques ; Medical sciences ; Membrane Proteins - drug effects ; Membrane Proteins - metabolism ; Microscopy, Fluorescence ; Monocytes - drug effects ; Monocytes - metabolism ; Myosin-Light-Chain Kinase - drug effects ; Myosin-Light-Chain Kinase - metabolism ; Tight Junctions - enzymology ; Tight Junctions - metabolism ; Toxicology</subject><ispartof>Alcoholism, clinical and experimental research, 2005-06, Vol.29 (6), p.999-1009</ispartof><rights>2005 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4419-98f60576fbc1f2e236582c23c9aadcd52cb8c3b3ce8757d4fecc167ba234dd033</citedby><cites>FETCH-LOGICAL-c4419-98f60576fbc1f2e236582c23c9aadcd52cb8c3b3ce8757d4fecc167ba234dd033</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1097%2F01.ALC.0000166944.79914.0A$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1097%2F01.ALC.0000166944.79914.0A$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,777,781,1412,27905,27906,45555,45556</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=16976634$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/15976526$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Haorah, James</creatorcontrib><creatorcontrib>Heilman, David</creatorcontrib><creatorcontrib>Knipe, Bryan</creatorcontrib><creatorcontrib>Chrastil, Jesse</creatorcontrib><creatorcontrib>Leibhart, Jessica</creatorcontrib><creatorcontrib>Ghorpade, Anuja</creatorcontrib><creatorcontrib>Miller, Donald W.</creatorcontrib><creatorcontrib>Persidsky, Yuri</creatorcontrib><title>Ethanol-Induced Activation of Myosin Light Chain Kinase Leads to Dysfunction of Tight Junctions and Blood-Brain Barrier Compromise</title><title>Alcoholism, clinical and experimental research</title><addtitle>Alcohol Clin Exp Res</addtitle><description>Background:
Brain endothelial cells form the blood‐brain barrier (BBB) that regulates solute and macromolecule flux in and out of the brain, leukocyte migration, and maintains the homeostasis of the central nervous system. BBB dysfunction is associated with disruption of tight junctions (TJ) in the brain endothelium. We propose that alcohol abuse may impair BBB permeability through TJ modification.
Methods:
Primary cultured bovine brain microvascular endothelial cells (BBMEC) were treated with 50 mM ethanol (EtOH), and monolayer tightness was assessed by measurement of transendothelial electrical resistance (TEER). Changes in TEER were correlated with alterations in TJ protein distribution occludin, zonula occludens‐1 (ZO‐1), claudin‐5 using immunofluorescence (IF). Expression of myosin light chain (MLC) kinase (MLCK), ZO‐1, claudin‐5, and phosphorylated MLC, occludin and claudin‐5 were determined by immunoprecipitation and Western blot. EtOH‐induced changes in monocyte migration across in vitro BBB constructs were also examined.
Results:
EtOH induced a decrease in TEER of BBMEC monolayers that was reversed by EtOH withdrawal. Treatment of BBMEC with EtOH or its metabolite, acetaldehyde, prior to monocyte application resulted in a 2‐fold increase in monocyte migration across the BBB. IF demonstrated decrease in claudin‐5 staining, occludin translocation from cell borders to cytoplasm and gap formation in EtOH‐treated BBMEC monolayer. These changes paralleled significant increase in phosphorylation of MLC, occludin and claudin‐5. EtOH‐treated BBMEC showed reduction of total occludin and claudin‐5 without changes in ZO‐1 or MLC. TEER decrease, changes in occludin/claudin staining, increase in MLC, occludin and claudin‐5 phosphorylation and enhanced monocyte migration across the BBB were all reversed by inhibition of MLCK. Inhibition of EtOH metabolism in BBMEC also reversed these events.
Conclusion:
These results suggest that EtOH activates MLCK leading to phosphorylation of MLC, occludin and claudin‐5. Cytoskeletal alterations (MLC) and TJ changes (occludin and claudin‐5 phosphorylation) result in BBB impairment (decrease in TEER). TJ compromise is associated with increased monocyte migration across the BBB.</description><subject>Alcoholism and acute alcohol poisoning</subject><subject>Animals</subject><subject>Biological and medical sciences</subject><subject>Blood-Brain Barrier - drug effects</subject><subject>Blood-Brain Barrier - enzymology</subject><subject>Blood-Brain Barrier - physiopathology</subject><subject>Capillary Permeability - drug effects</subject><subject>Capillary Permeability - physiology</subject><subject>Cattle</subject><subject>Cell Movement - drug effects</subject><subject>Cell Movement - physiology</subject><subject>Cells, Cultured</subject><subject>Electric Impedance</subject><subject>Endothelial Cells - drug effects</subject><subject>Endothelial Cells - enzymology</subject><subject>Endothelial Cells - metabolism</subject><subject>Enzyme Activation - drug effects</subject><subject>Ethanol - pharmacokinetics</subject><subject>Ethanol - pharmacology</subject><subject>In Vitro Techniques</subject><subject>Medical sciences</subject><subject>Membrane Proteins - drug effects</subject><subject>Membrane Proteins - metabolism</subject><subject>Microscopy, Fluorescence</subject><subject>Monocytes - drug effects</subject><subject>Monocytes - metabolism</subject><subject>Myosin-Light-Chain Kinase - drug effects</subject><subject>Myosin-Light-Chain Kinase - metabolism</subject><subject>Tight Junctions - enzymology</subject><subject>Tight Junctions - metabolism</subject><subject>Toxicology</subject><issn>0145-6008</issn><issn>1530-0277</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2005</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqVkUGP1CAcxRujccfVr2CIid5aoVAoXkynOzvu2tVkXbOJF0KBOridskKrztVPLrtTnbNcIOT33vvDS5IXCGYIcvYaoqxq6gzGhSjlhGSMc0QyWD1IFqjAMIU5Yw-TBUSkSCmE5VHyJIRvkSclpY-TI1RwRoucLpLfq3EjB9enZ4OelNGgUqP9IUfrBuA6cLFzwQ6gsV83I6g3Mp7f20EGAxojdQCjAye70E2D-qu4ukfP55sA5KDBsndOp0t_J19K763xoHbbW--2NpinyaNO9sE8m_fj5PPp6qp-lzYf12d11aSKEMRTXnYUFox2rUJdbnJMizJXOVZcSq10kau2VLjFypSsYJp0RilEWStzTLSGGB8nr_a-Mff7ZMIoYroyfS8H46YgKOMUc15G8M0eVN6F4E0nbr3dSr8TCIq7BgREIjYgDg2I-wYErKL4-ZwytVujD9L5yyPwcgZkULLvvByUDQeORo5iErm3e-6n7c3uP0YQVb265JxHh3TvYMNofv1zkP4mvhWzQlx_WIuL80_ry5Mv1-IU_wHXm7JT</recordid><startdate>200506</startdate><enddate>200506</enddate><creator>Haorah, James</creator><creator>Heilman, David</creator><creator>Knipe, Bryan</creator><creator>Chrastil, Jesse</creator><creator>Leibhart, Jessica</creator><creator>Ghorpade, Anuja</creator><creator>Miller, Donald W.</creator><creator>Persidsky, Yuri</creator><general>Blackwell Publishing Ltd</general><general>Lippincott Williams & Wilkins</general><scope>BSCLL</scope><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>200506</creationdate><title>Ethanol-Induced Activation of Myosin Light Chain Kinase Leads to Dysfunction of Tight Junctions and Blood-Brain Barrier Compromise</title><author>Haorah, James ; Heilman, David ; Knipe, Bryan ; Chrastil, Jesse ; Leibhart, Jessica ; Ghorpade, Anuja ; Miller, Donald W. ; Persidsky, Yuri</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4419-98f60576fbc1f2e236582c23c9aadcd52cb8c3b3ce8757d4fecc167ba234dd033</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2005</creationdate><topic>Alcoholism and acute alcohol poisoning</topic><topic>Animals</topic><topic>Biological and medical sciences</topic><topic>Blood-Brain Barrier - drug effects</topic><topic>Blood-Brain Barrier - enzymology</topic><topic>Blood-Brain Barrier - physiopathology</topic><topic>Capillary Permeability - drug effects</topic><topic>Capillary Permeability - physiology</topic><topic>Cattle</topic><topic>Cell Movement - drug effects</topic><topic>Cell Movement - physiology</topic><topic>Cells, Cultured</topic><topic>Electric Impedance</topic><topic>Endothelial Cells - drug effects</topic><topic>Endothelial Cells - enzymology</topic><topic>Endothelial Cells - metabolism</topic><topic>Enzyme Activation - drug effects</topic><topic>Ethanol - pharmacokinetics</topic><topic>Ethanol - pharmacology</topic><topic>In Vitro Techniques</topic><topic>Medical sciences</topic><topic>Membrane Proteins - drug effects</topic><topic>Membrane Proteins - metabolism</topic><topic>Microscopy, Fluorescence</topic><topic>Monocytes - drug effects</topic><topic>Monocytes - metabolism</topic><topic>Myosin-Light-Chain Kinase - drug effects</topic><topic>Myosin-Light-Chain Kinase - metabolism</topic><topic>Tight Junctions - enzymology</topic><topic>Tight Junctions - metabolism</topic><topic>Toxicology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Haorah, James</creatorcontrib><creatorcontrib>Heilman, David</creatorcontrib><creatorcontrib>Knipe, Bryan</creatorcontrib><creatorcontrib>Chrastil, Jesse</creatorcontrib><creatorcontrib>Leibhart, Jessica</creatorcontrib><creatorcontrib>Ghorpade, Anuja</creatorcontrib><creatorcontrib>Miller, Donald W.</creatorcontrib><creatorcontrib>Persidsky, Yuri</creatorcontrib><collection>Istex</collection><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Alcoholism, clinical and experimental research</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Haorah, James</au><au>Heilman, David</au><au>Knipe, Bryan</au><au>Chrastil, Jesse</au><au>Leibhart, Jessica</au><au>Ghorpade, Anuja</au><au>Miller, Donald W.</au><au>Persidsky, Yuri</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Ethanol-Induced Activation of Myosin Light Chain Kinase Leads to Dysfunction of Tight Junctions and Blood-Brain Barrier Compromise</atitle><jtitle>Alcoholism, clinical and experimental research</jtitle><addtitle>Alcohol Clin Exp Res</addtitle><date>2005-06</date><risdate>2005</risdate><volume>29</volume><issue>6</issue><spage>999</spage><epage>1009</epage><pages>999-1009</pages><issn>0145-6008</issn><eissn>1530-0277</eissn><coden>ACRSDM</coden><abstract>Background:
Brain endothelial cells form the blood‐brain barrier (BBB) that regulates solute and macromolecule flux in and out of the brain, leukocyte migration, and maintains the homeostasis of the central nervous system. BBB dysfunction is associated with disruption of tight junctions (TJ) in the brain endothelium. We propose that alcohol abuse may impair BBB permeability through TJ modification.
Methods:
Primary cultured bovine brain microvascular endothelial cells (BBMEC) were treated with 50 mM ethanol (EtOH), and monolayer tightness was assessed by measurement of transendothelial electrical resistance (TEER). Changes in TEER were correlated with alterations in TJ protein distribution occludin, zonula occludens‐1 (ZO‐1), claudin‐5 using immunofluorescence (IF). Expression of myosin light chain (MLC) kinase (MLCK), ZO‐1, claudin‐5, and phosphorylated MLC, occludin and claudin‐5 were determined by immunoprecipitation and Western blot. EtOH‐induced changes in monocyte migration across in vitro BBB constructs were also examined.
Results:
EtOH induced a decrease in TEER of BBMEC monolayers that was reversed by EtOH withdrawal. Treatment of BBMEC with EtOH or its metabolite, acetaldehyde, prior to monocyte application resulted in a 2‐fold increase in monocyte migration across the BBB. IF demonstrated decrease in claudin‐5 staining, occludin translocation from cell borders to cytoplasm and gap formation in EtOH‐treated BBMEC monolayer. These changes paralleled significant increase in phosphorylation of MLC, occludin and claudin‐5. EtOH‐treated BBMEC showed reduction of total occludin and claudin‐5 without changes in ZO‐1 or MLC. TEER decrease, changes in occludin/claudin staining, increase in MLC, occludin and claudin‐5 phosphorylation and enhanced monocyte migration across the BBB were all reversed by inhibition of MLCK. Inhibition of EtOH metabolism in BBMEC also reversed these events.
Conclusion:
These results suggest that EtOH activates MLCK leading to phosphorylation of MLC, occludin and claudin‐5. Cytoskeletal alterations (MLC) and TJ changes (occludin and claudin‐5 phosphorylation) result in BBB impairment (decrease in TEER). TJ compromise is associated with increased monocyte migration across the BBB.</abstract><cop>Oxford, UK</cop><pub>Blackwell Publishing Ltd</pub><pmid>15976526</pmid><doi>10.1097/01.ALC.0000166944.79914.0A</doi><tpages>11</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0145-6008 |
| ispartof | Alcoholism, clinical and experimental research, 2005-06, Vol.29 (6), p.999-1009 |
| issn | 0145-6008 1530-0277 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_67963998 |
| source | MEDLINE; Wiley Online Library Journals Frontfile Complete; Journals@Ovid Complete |
| subjects | Alcoholism and acute alcohol poisoning Animals Biological and medical sciences Blood-Brain Barrier - drug effects Blood-Brain Barrier - enzymology Blood-Brain Barrier - physiopathology Capillary Permeability - drug effects Capillary Permeability - physiology Cattle Cell Movement - drug effects Cell Movement - physiology Cells, Cultured Electric Impedance Endothelial Cells - drug effects Endothelial Cells - enzymology Endothelial Cells - metabolism Enzyme Activation - drug effects Ethanol - pharmacokinetics Ethanol - pharmacology In Vitro Techniques Medical sciences Membrane Proteins - drug effects Membrane Proteins - metabolism Microscopy, Fluorescence Monocytes - drug effects Monocytes - metabolism Myosin-Light-Chain Kinase - drug effects Myosin-Light-Chain Kinase - metabolism Tight Junctions - enzymology Tight Junctions - metabolism Toxicology |
| title | Ethanol-Induced Activation of Myosin Light Chain Kinase Leads to Dysfunction of Tight Junctions and Blood-Brain Barrier Compromise |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-20T08%3A54%3A52IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Ethanol-Induced%20Activation%20of%20Myosin%20Light%20Chain%20Kinase%20Leads%20to%20Dysfunction%20of%20Tight%20Junctions%20and%20Blood-Brain%20Barrier%20Compromise&rft.jtitle=Alcoholism,%20clinical%20and%20experimental%20research&rft.au=Haorah,%20James&rft.date=2005-06&rft.volume=29&rft.issue=6&rft.spage=999&rft.epage=1009&rft.pages=999-1009&rft.issn=0145-6008&rft.eissn=1530-0277&rft.coden=ACRSDM&rft_id=info:doi/10.1097/01.ALC.0000166944.79914.0A&rft_dat=%3Cproquest_cross%3E67963998%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=67963998&rft_id=info:pmid/15976526&rfr_iscdi=true |