The epithelial membrane protein 1 is a novel tight junction protein of the blood-brain barrier
In the central nervous system, a constant microenvironment required for neuronal cell activity is maintained by the blood—brain barrier (BBB). The BBB is formed by the brain microvascular endothelial cells (BMEC), which are sealed by tight junctions (TJ). To identify genes that are differentially ex...
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| Veröffentlicht in: | Journal of cerebral blood flow and metabolism 2008-06, Vol.28 (6), p.1249-1260 |
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| container_title | Journal of cerebral blood flow and metabolism |
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| creator | Bangsow, Thorsten Baumann, Ewa Bangsow, Carmen Jaeger, Martina H Pelzer, Bernhard Gruhn, Petra Wolf, Sabine von Melchner, Harald Stanimirovic, Danica B |
| description | In the central nervous system, a constant microenvironment required for neuronal cell activity is maintained by the blood—brain barrier (BBB). The BBB is formed by the brain microvascular endothelial cells (BMEC), which are sealed by tight junctions (TJ). To identify genes that are differentially expressed in BMEC compared with peripheral endothelial cells, we constructed a subtractive cDNA library from porcine BMEC (pBMEC) and aortic endothelial cells (AOEC). Screening the library for differentially expressed genes yielded 26 BMEC-specific transcripts, such as solute carrier family 35 member F2 (SLC35F2), ADP-ribosylation factor-like 5B (ARL5B), TSC22 domain family member 1 (TSC22D1), integral membrane protein 2A (ITM2A), and epithelial membrane protein 1 (EMP1). In this study, we show that EMP1 transcript is enriched in pBMEC compared with brain tissue and that EMP1 protein colocalizes with the TJ protein occludin in mouse BMEC by coimmunoprecipitation and in rat brain vessels by immunohistochemistry. Epithelial membrane protein 1 expression was transiently induced in laser-capture microdissected rat brain vessels after a 20-min global cerebral ischemia, in parallel with the loss of occludin immunoreactivity. The study identifies EMP1 as a novel TJ-associated protein of the BBB and suggests its potential role in the regulation of the BBB function in cerebral ischemia. |
| doi_str_mv | 10.1038/jcbfm.2008.19 |
| format | Article |
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The BBB is formed by the brain microvascular endothelial cells (BMEC), which are sealed by tight junctions (TJ). To identify genes that are differentially expressed in BMEC compared with peripheral endothelial cells, we constructed a subtractive cDNA library from porcine BMEC (pBMEC) and aortic endothelial cells (AOEC). Screening the library for differentially expressed genes yielded 26 BMEC-specific transcripts, such as solute carrier family 35 member F2 (SLC35F2), ADP-ribosylation factor-like 5B (ARL5B), TSC22 domain family member 1 (TSC22D1), integral membrane protein 2A (ITM2A), and epithelial membrane protein 1 (EMP1). In this study, we show that EMP1 transcript is enriched in pBMEC compared with brain tissue and that EMP1 protein colocalizes with the TJ protein occludin in mouse BMEC by coimmunoprecipitation and in rat brain vessels by immunohistochemistry. Epithelial membrane protein 1 expression was transiently induced in laser-capture microdissected rat brain vessels after a 20-min global cerebral ischemia, in parallel with the loss of occludin immunoreactivity. The study identifies EMP1 as a novel TJ-associated protein of the BBB and suggests its potential role in the regulation of the BBB function in cerebral ischemia.</description><identifier>ISSN: 0271-678X</identifier><identifier>EISSN: 1559-7016</identifier><identifier>DOI: 10.1038/jcbfm.2008.19</identifier><identifier>PMID: 18382472</identifier><identifier>CODEN: JCBMDN</identifier><language>eng</language><publisher>London, England: SAGE Publications</publisher><subject>Amino Acid Sequence ; Animals ; Biological and medical sciences ; Blood-Brain Barrier - metabolism ; Brain Ischemia - genetics ; Brain Ischemia - metabolism ; Cells, Cultured ; Conserved Sequence ; Gene Expression Regulation ; Humans ; Injuries of the nervous system and the skull. Diseases due to physical agents ; Medical sciences ; Molecular Sequence Data ; Neoplasm Proteins - chemistry ; Neoplasm Proteins - genetics ; Neoplasm Proteins - metabolism ; Neurology ; Receptors, Cell Surface - chemistry ; Receptors, Cell Surface - genetics ; Receptors, Cell Surface - metabolism ; Sequence Alignment ; Swine ; Tight Junctions - metabolism ; Traumas. 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The BBB is formed by the brain microvascular endothelial cells (BMEC), which are sealed by tight junctions (TJ). To identify genes that are differentially expressed in BMEC compared with peripheral endothelial cells, we constructed a subtractive cDNA library from porcine BMEC (pBMEC) and aortic endothelial cells (AOEC). Screening the library for differentially expressed genes yielded 26 BMEC-specific transcripts, such as solute carrier family 35 member F2 (SLC35F2), ADP-ribosylation factor-like 5B (ARL5B), TSC22 domain family member 1 (TSC22D1), integral membrane protein 2A (ITM2A), and epithelial membrane protein 1 (EMP1). In this study, we show that EMP1 transcript is enriched in pBMEC compared with brain tissue and that EMP1 protein colocalizes with the TJ protein occludin in mouse BMEC by coimmunoprecipitation and in rat brain vessels by immunohistochemistry. Epithelial membrane protein 1 expression was transiently induced in laser-capture microdissected rat brain vessels after a 20-min global cerebral ischemia, in parallel with the loss of occludin immunoreactivity. The study identifies EMP1 as a novel TJ-associated protein of the BBB and suggests its potential role in the regulation of the BBB function in cerebral ischemia.</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Biological and medical sciences</subject><subject>Blood-Brain Barrier - metabolism</subject><subject>Brain Ischemia - genetics</subject><subject>Brain Ischemia - metabolism</subject><subject>Cells, Cultured</subject><subject>Conserved Sequence</subject><subject>Gene Expression Regulation</subject><subject>Humans</subject><subject>Injuries of the nervous system and the skull. Diseases due to physical agents</subject><subject>Medical sciences</subject><subject>Molecular Sequence Data</subject><subject>Neoplasm Proteins - chemistry</subject><subject>Neoplasm Proteins - genetics</subject><subject>Neoplasm Proteins - metabolism</subject><subject>Neurology</subject><subject>Receptors, Cell Surface - chemistry</subject><subject>Receptors, Cell Surface - genetics</subject><subject>Receptors, Cell Surface - metabolism</subject><subject>Sequence Alignment</subject><subject>Swine</subject><subject>Tight Junctions - metabolism</subject><subject>Traumas. 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Diseases due to physical agents</topic><topic>Medical sciences</topic><topic>Molecular Sequence Data</topic><topic>Neoplasm Proteins - chemistry</topic><topic>Neoplasm Proteins - genetics</topic><topic>Neoplasm Proteins - metabolism</topic><topic>Neurology</topic><topic>Receptors, Cell Surface - chemistry</topic><topic>Receptors, Cell Surface - genetics</topic><topic>Receptors, Cell Surface - metabolism</topic><topic>Sequence Alignment</topic><topic>Swine</topic><topic>Tight Junctions - metabolism</topic><topic>Traumas. 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The BBB is formed by the brain microvascular endothelial cells (BMEC), which are sealed by tight junctions (TJ). To identify genes that are differentially expressed in BMEC compared with peripheral endothelial cells, we constructed a subtractive cDNA library from porcine BMEC (pBMEC) and aortic endothelial cells (AOEC). Screening the library for differentially expressed genes yielded 26 BMEC-specific transcripts, such as solute carrier family 35 member F2 (SLC35F2), ADP-ribosylation factor-like 5B (ARL5B), TSC22 domain family member 1 (TSC22D1), integral membrane protein 2A (ITM2A), and epithelial membrane protein 1 (EMP1). In this study, we show that EMP1 transcript is enriched in pBMEC compared with brain tissue and that EMP1 protein colocalizes with the TJ protein occludin in mouse BMEC by coimmunoprecipitation and in rat brain vessels by immunohistochemistry. Epithelial membrane protein 1 expression was transiently induced in laser-capture microdissected rat brain vessels after a 20-min global cerebral ischemia, in parallel with the loss of occludin immunoreactivity. The study identifies EMP1 as a novel TJ-associated protein of the BBB and suggests its potential role in the regulation of the BBB function in cerebral ischemia.</abstract><cop>London, England</cop><pub>SAGE Publications</pub><pmid>18382472</pmid><doi>10.1038/jcbfm.2008.19</doi><tpages>12</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | Journal of cerebral blood flow and metabolism, 2008-06, Vol.28 (6), p.1249-1260 |
| issn | 0271-678X 1559-7016 |
| language | eng |
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| source | MEDLINE; SAGE Complete A-Z List |
| subjects | Amino Acid Sequence Animals Biological and medical sciences Blood-Brain Barrier - metabolism Brain Ischemia - genetics Brain Ischemia - metabolism Cells, Cultured Conserved Sequence Gene Expression Regulation Humans Injuries of the nervous system and the skull. Diseases due to physical agents Medical sciences Molecular Sequence Data Neoplasm Proteins - chemistry Neoplasm Proteins - genetics Neoplasm Proteins - metabolism Neurology Receptors, Cell Surface - chemistry Receptors, Cell Surface - genetics Receptors, Cell Surface - metabolism Sequence Alignment Swine Tight Junctions - metabolism Traumas. Diseases due to physical agents Vascular diseases and vascular malformations of the nervous system |
| title | The epithelial membrane protein 1 is a novel tight junction protein of the blood-brain barrier |
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