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5 results on '"brain endothelial cell"'

1. Tumor necrosis factor-α reduces beta-amyloid accumulation primarily by lowering cellular prion protein levels in a brain endothelial cell line.

Author

Yuki Yasutaka, Takuya Watanabe, Akio Nakashima, Junichi Matsumoto, Koujiro Futagami, Atsushi Yamauchi, and Yasufumi Kataoka

Subjects
*TUMOR necrosis factors, *AMYLOID beta-protein, *PRIONS, *BLOOD-brain barrier, *ENDOTHELIAL cells, *ALZHEIMER'S disease
Abstract

Disruption of beta-amyloid (Aß) transport across the blood-brain barrier is thought to cause Aß accumulation in the brain, thus leading to the development of Alzheimer's disease (AD). As AD patients show increased serum tumor necrosis factor-a (TNFa) levels, we examined the effect of TNFa on the function and expression of Aß transport-related proteins including cellular prion protein (PrPC) in the mouse brain microvascular endothelial cell line MBEC4. TNFa decreased PrPC levels and intracellular radiolabeled Aß. Similarly, anti-prion protein antibody also decreased radiolabeled Aß. These results suggest that TNFa lowers PrPC levels, which in turn, reduces Aß in the brain endothelium. [ABSTRACT FROM AUTHOR]

Published
2015
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2. Involvement of Rho/ROCK signalling in small cell lung cancer migration through human brain microvascular endothelial cells

Author

Li, Bo, Zhao, Wei-Dong, Tan, Zhi-Min, Fang, Wen-Gang, Zhu, Li, and Chen, Yu-Hua

Subjects
*SMALL cell lung cancer, *PROTEIN kinase C, *METASTASIS, *BRAIN diseases
Abstract

Abstract: Small cell lung cancer (SCLC) cells migration across human brain microvascular endothelial cells (HBMECs) is an essential step of brain metastases. Here we investigated signalling pathways in HBMECs contributing to the process. Inhibition of endothelial Rho kinase (ROCK) with Y27632 and overexpression of ROCK dominant-negative mutant prevented SCLC cells, NCI-H209, transendothelial migration and the concomitant changes of tight junction. Conversely, inhibition of phosphatidylinositol 3-kinase (PI3K) and protein kinase C (PKC) had no effects. Furthermore, endothelial RhoA protein was activated during NCI-H209 cells transendothelial migration. Rho/ROCK participated in NCI-H209 cells transendothelial migration through regulating actin cytoskeleton reorganization. These results suggested that Rho/ROCK was required for SCLC cells transendothelial migration. [Copyright &y& Elsevier]

Published
2006
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3. Tumor necrosis factor-α reduces beta-amyloid accumulation primarily by lowering cellular prion protein levels in a brain endothelial cell line

Author

Yuki Yasutaka, Akio Nakashima, Koujiro Futagami, Atsushi Yamauchi, Takuya Watanabe, Junichi Matsumoto, and Yasufumi Kataoka

Subjects
medicine.medical_specialty, Amyloid, Prions, animal diseases, Biophysics, Beta-amyloid, Biology, Biochemistry, Cell Line, Mice, Structural Biology, Internal medicine, Genetics, medicine, Animals, Beta (finance), Molecular Biology, Gene, P-glycoprotein, Amyloid beta-Peptides, Tumor Necrosis Factor-alpha, Brain, Cell Biology, nervous system diseases, Tumor necrosis factor-α, Endothelial stem cell, Endocrinology, Prion protein, Immunology, biology.protein, Brain endothelial cell, Tumor necrosis factor alpha, Alzheimer’s disease, Function (biology), Intracellular
Abstract

Disruption of beta-amyloid (Aβ) transport across the blood–brain barrier is thought to cause Aβ accumulation in the brain, thus leading to the development of Alzheimer’s disease (AD). As AD patients show increased serum tumor necrosis factor-α (TNFα) levels, we examined the effect of TNFα on the function and expression of Aβ transport-related proteins including cellular prion protein (PrPC) in the mouse brain microvascular endothelial cell line MBEC4. TNFα decreased PrPC levels and intracellular radiolabeled Aβ. Similarly, anti-prion protein antibody also decreased radiolabeled Aβ. These results suggest that TNFα lowers PrPC levels, which in turn, reduces Aβ in the brain endothelium.

Published
2014
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4. Involvement of Rho/ROCK signalling in small cell lung cancer migration through human brain microvascular endothelial cells

Author

Zhi-Min Tan, Bo Li, Yu-Hua Chen, Wei-Dong Zhao, Wen-Gang Fang, and Li Zhu

Subjects
Lung Neoplasms, Pyridines, Biophysics, Biology, Protein Serine-Threonine Kinases, Biochemistry, chemistry.chemical_compound, Structural Biology, Cell Movement, Cell Line, Tumor, Genetics, Humans, Phosphatidylinositol, Carcinoma, Small Cell, Enzyme Inhibitors, Neoplasm Metastasis, Molecular Biology, Rho-associated protein kinase, Tight junction, PI3K/AKT/mTOR pathway, Protein kinase C, Cytoskeleton, Genes, Dominant, Regulation of gene expression, rho-Associated Kinases, Small cell lung cancer, Rho/ROCK, Brain Neoplasms, Actin cytoskeleton reorganization, Intracellular Signaling Peptides and Proteins, Endothelial Cells, Cell Biology, Amides, Cell biology, Neoplasm Proteins, Gene Expression Regulation, Neoplastic, chemistry, Cell culture, Brain endothelial cell, Signal Transduction
Abstract

Small cell lung cancer (SCLC) cells migration across human brain microvascular endothelial cells (HBMECs) is an essential step of brain metastases. Here we investigated signalling pathways in HBMECs contributing to the process. Inhibition of endothelial Rho kinase (ROCK) with Y27632 and overexpression of ROCK dominant-negative mutant prevented SCLC cells, NCI-H209, transendothelial migration and the concomitant changes of tight junction. Conversely, inhibition of phosphatidylinositol 3-kinase (PI3K) and protein kinase C (PKC) had no effects. Furthermore, endothelial RhoA protein was activated during NCI-H209 cells transendothelial migration. Rho/ROCK participated in NCI-H209 cells transendothelial migration through regulating actin cytoskeleton reorganization. These results suggested that Rho/ROCK was required for SCLC cells transendothelial migration.

Published
2006

5. Tumor necrosis factor-α reduces beta-amyloid accumulation primarily by lowering cellular prion protein levels in a brain endothelial cell line.

Author

Yasutaka Y, Watanabe T, Nakashima A, Matsumoto J, Futagami K, Yamauchi A, and Kataoka Y

Subjects
Animals, Cell Line, Mice, Amyloid beta-Peptides metabolism, Brain metabolism, Prions metabolism, Tumor Necrosis Factor-alpha metabolism
Abstract

Disruption of beta-amyloid (Aβ) transport across the blood-brain barrier is thought to cause Aβ accumulation in the brain, thus leading to the development of Alzheimer's disease (AD). As AD patients show increased serum tumor necrosis factor-α (TNFα) levels, we examined the effect of TNFα on the function and expression of Aβ transport-related proteins including cellular prion protein (PrP(C)) in the mouse brain microvascular endothelial cell line MBEC4. TNFα decreased PrP(C) levels and intracellular radiolabeled Aβ. Similarly, anti-prion protein antibody also decreased radiolabeled Aβ. These results suggest that TNFα lowers PrP(C) levels, which in turn, reduces Aβ in the brain endothelium., (Copyright © 2014 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.)

Published
2015
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