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Mol. Cells 2010; 29(1): 93-98

Published online January 8, 2010

https://doi.org/10.1007/s10059-010-0040-0

© The Korean Society for Molecular and Cellular Biology

Blood-Brain Barrier Defects Associated with Rbp9 Mutation

Jihyun Kim, Young-Joon Kim1, and Jeongsil Kim-Ha*

Department of Molecular Biology, College of Life Sciences, Sejong University, Seoul 143-747, Korea, 1Department of Biochemistry, Yonsei University, Seoul 120-749, Korea

Correspondence to : *Correspondence: jsha@sejong.ac.kr

Received: November 12, 2009; Revised: November 30, 2009; Accepted: December 7, 2009

Abstract

Rbp9 is a Drosophila RNA-binding protein that shares a high level of sequence similarity with Drosophila elav and human Hu proteins. Loss of function alleles of elav are embryonic lethal causing abnormal central nervous system (CNS) development, and Hu is implicated in the development of paraneoplastic neurological syndrome associated with small cell lung cancer. To elucidate the role of Rbp9, we generated Rbp9 mutant flies and examined them for symptoms related to paraneoplastic encephalomyelitis. Although Rbp9 proteins begin to appear from the middle of the pupal period in the cortex of the CNS, the Rbp9 mutants showed no apparent defects in development. However, as the mutant adult flies grew older, they showed reduced locomotor activi-ties and lived only one-half of the life expectancy of wild-type flies. To understand the molecular mechanism underlying this symptom, gene expression profiles in Rbp9 mutants were analyzed and potential target genes were further characterized. Reduced expression of cell adhesion molecules was detected, and defects in the blood-brain barrier (BBB) of Rbp9 mutant brains could be seen. Putative Rbp9-binding sites were found in introns of genes that function in cell adhesion. Therefore, Rbp9 may regulate the splicing of cell adhesion molecules, critical for the formation of the BBB.

Keywords adhesion, blood brain barrier, Drosophila, elav, Rbp9

Article

Research Article

Mol. Cells 2010; 29(1): 93-98

Published online January 31, 2010 https://doi.org/10.1007/s10059-010-0040-0

Copyright © The Korean Society for Molecular and Cellular Biology.

Blood-Brain Barrier Defects Associated with Rbp9 Mutation

Jihyun Kim, Young-Joon Kim1, and Jeongsil Kim-Ha*

Department of Molecular Biology, College of Life Sciences, Sejong University, Seoul 143-747, Korea, 1Department of Biochemistry, Yonsei University, Seoul 120-749, Korea

Correspondence to:*Correspondence: jsha@sejong.ac.kr

Received: November 12, 2009; Revised: November 30, 2009; Accepted: December 7, 2009

Abstract

Rbp9 is a Drosophila RNA-binding protein that shares a high level of sequence similarity with Drosophila elav and human Hu proteins. Loss of function alleles of elav are embryonic lethal causing abnormal central nervous system (CNS) development, and Hu is implicated in the development of paraneoplastic neurological syndrome associated with small cell lung cancer. To elucidate the role of Rbp9, we generated Rbp9 mutant flies and examined them for symptoms related to paraneoplastic encephalomyelitis. Although Rbp9 proteins begin to appear from the middle of the pupal period in the cortex of the CNS, the Rbp9 mutants showed no apparent defects in development. However, as the mutant adult flies grew older, they showed reduced locomotor activi-ties and lived only one-half of the life expectancy of wild-type flies. To understand the molecular mechanism underlying this symptom, gene expression profiles in Rbp9 mutants were analyzed and potential target genes were further characterized. Reduced expression of cell adhesion molecules was detected, and defects in the blood-brain barrier (BBB) of Rbp9 mutant brains could be seen. Putative Rbp9-binding sites were found in introns of genes that function in cell adhesion. Therefore, Rbp9 may regulate the splicing of cell adhesion molecules, critical for the formation of the BBB.

Keywords: adhesion, blood brain barrier, Drosophila, elav, Rbp9

Mol. Cells
May 31, 2023 Vol.46 No.5, pp. 259~328
COVER PICTURE
The alpha-helices in the lamin filaments are depicted as coils, with different subdomains distinguished by various colors. Coil 1a is represented by magenta, coil 1b by yellow, L2 by green, coil 2a by white, coil 2b by brown, stutter by cyan, coil 2c by dark blue, and the lamin Ig-like domain by grey. In the background, cells are displayed, with the cytosol depicted in green and the nucleus in blue (Ahn et al., pp. 309-318).

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