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Mol. Cells 2013; 36(5): 410-416

Published online November 8, 2013

https://doi.org/10.1007/s10059-013-0170-2

© The Korean Society for Molecular and Cellular Biology

Cholesterol-Responsive Metabolic Proteins Are Required for Larval Development in Caenorhabditis elegans

Ichiro Kawasaki, Myung-Hwan Jeong, Yu-Joun Yun, Yun-Kyung Shin, and Yhong-Hee Shim

Department of Bioscience and Biotechnology, 2Institute of KU Biotechnology, Konkuk University, Seoul 143-701, Korea

Received: June 3, 2013; Revised: September 7, 2013; Accepted: September 9, 2013

Abstract

Caenorhabditis elegans, a cholesterol auxotroph, showed defects in larval development upon cholesterol starvation (CS) in a previous study. To identify cholesterol-respon-sive proteins likely responsible for the larval arrest upon CS, a comparative proteomic analysis was performed between C. elegans grown in normal medium supplemented with cholesterol (CN) and those grown in medium not supplemented with cholesterol (cholesterol starvation, CS). Our analysis revealed significant change (more than 2.2-fold, p < 0.05) in nine proteins upon CS. Six proteins were down-regulated [CE01270 (EEF-1A.1), CE08852 (SAMS-1), CE11068 (PMT-2), CE09015 (ACDH-1), CE12564 (R07H5.8), and CE09655 (RLA-0)], and three proteins were up-regu-lated [CE29645 (LEC-1), CE16576 (LEC-5), and CE01431 (NEX-1)]. RNAi phenotypes of two of the down-regulated genes, R07H5.8 (adenosine kinase) and rla-0 (ribosomal protein), in CN were similar to that of larval arrest in CS, and RNAi of a down-regulated gene, R07H5.8, in CS further enhanced the effects of CS, suggesting that down-regulation of these genes is likely responsible for the larval arrest in CS. All three up-regulated genes con-tain putative DAF-16 binding sites and mRNA levels of these three genes were all decreased in daf-16 mutants in CN, suggesting that DAF-16 activates expression of these genes.

Keywords C. elegans development, cholesterol, proteomic analysis

Article

Research Article

Mol. Cells 2013; 36(5): 410-416

Published online November 30, 2013 https://doi.org/10.1007/s10059-013-0170-2

Copyright © The Korean Society for Molecular and Cellular Biology.

Cholesterol-Responsive Metabolic Proteins Are Required for Larval Development in Caenorhabditis elegans

Ichiro Kawasaki, Myung-Hwan Jeong, Yu-Joun Yun, Yun-Kyung Shin, and Yhong-Hee Shim

Department of Bioscience and Biotechnology, 2Institute of KU Biotechnology, Konkuk University, Seoul 143-701, Korea

Received: June 3, 2013; Revised: September 7, 2013; Accepted: September 9, 2013

Abstract

Caenorhabditis elegans, a cholesterol auxotroph, showed defects in larval development upon cholesterol starvation (CS) in a previous study. To identify cholesterol-respon-sive proteins likely responsible for the larval arrest upon CS, a comparative proteomic analysis was performed between C. elegans grown in normal medium supplemented with cholesterol (CN) and those grown in medium not supplemented with cholesterol (cholesterol starvation, CS). Our analysis revealed significant change (more than 2.2-fold, p < 0.05) in nine proteins upon CS. Six proteins were down-regulated [CE01270 (EEF-1A.1), CE08852 (SAMS-1), CE11068 (PMT-2), CE09015 (ACDH-1), CE12564 (R07H5.8), and CE09655 (RLA-0)], and three proteins were up-regu-lated [CE29645 (LEC-1), CE16576 (LEC-5), and CE01431 (NEX-1)]. RNAi phenotypes of two of the down-regulated genes, R07H5.8 (adenosine kinase) and rla-0 (ribosomal protein), in CN were similar to that of larval arrest in CS, and RNAi of a down-regulated gene, R07H5.8, in CS further enhanced the effects of CS, suggesting that down-regulation of these genes is likely responsible for the larval arrest in CS. All three up-regulated genes con-tain putative DAF-16 binding sites and mRNA levels of these three genes were all decreased in daf-16 mutants in CN, suggesting that DAF-16 activates expression of these genes.

Keywords: C. elegans development, cholesterol, proteomic analysis

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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