Alteration in cellular acetylcholine influences dauer formation in Caenorhabditis elegans

Jeeyong Lee, Kwang Youl Kim, Young-Ki Paik

Research output: Contribution to journalArticle

2 Citations (Scopus)

Abstract

Altered acetylcholine (Ach) homeostasis is associated with loss of viability in flies, developmental defects in mice, and cognitive deficits in human. Here, we assessed the importance of Ach in Caenorhabditis elegans development, focusing on the role of Ach during dauer formation. We found that dauer formation was disturbed in choline acetyltransferase (cha-1) and acetylcholinesterase (ace) mutants defective in Ach biosynthesis and degradation, respectively. When examined the potential role of G-proteins in dauer formation, goa-1 and egl-30 mutant worms, expressing mutated versions of mammalian Go and Gq homolog, respectively, showed some abnormalities in dauer formation. Using quantitative mass spectrometry, we also found that dauer larvae had lower Ach content than did reproductively grown larvae. In addition, a proteomic analysis of acetylcholinesterase mutant worms, which have excessive levels of Ach, showed differential expression of metabolic genes. Collectively, these results indicate that alterations in Ach release may influence dauer formation in C. elegans.

Original languageEnglish
Pages (from-to)80-85
Number of pages6
JournalBMB reports
Volume47
Issue number2
DOIs
Publication statusPublished - 2014 Jan 1

Fingerprint

Caenorhabditis elegans
Acetylcholine
Acetylcholinesterase
Larva
Choline O-Acetyltransferase
Biosynthesis
GTP-Binding Proteins
Diptera
Proteomics
Mass spectrometry
Mass Spectrometry
Homeostasis
Genes
Gene Expression
Degradation
Defects

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology

Cite this

@article{e9fa07683e6a4e33b50e7131268c1c12,
title = "Alteration in cellular acetylcholine influences dauer formation in Caenorhabditis elegans",
abstract = "Altered acetylcholine (Ach) homeostasis is associated with loss of viability in flies, developmental defects in mice, and cognitive deficits in human. Here, we assessed the importance of Ach in Caenorhabditis elegans development, focusing on the role of Ach during dauer formation. We found that dauer formation was disturbed in choline acetyltransferase (cha-1) and acetylcholinesterase (ace) mutants defective in Ach biosynthesis and degradation, respectively. When examined the potential role of G-proteins in dauer formation, goa-1 and egl-30 mutant worms, expressing mutated versions of mammalian Go and Gq homolog, respectively, showed some abnormalities in dauer formation. Using quantitative mass spectrometry, we also found that dauer larvae had lower Ach content than did reproductively grown larvae. In addition, a proteomic analysis of acetylcholinesterase mutant worms, which have excessive levels of Ach, showed differential expression of metabolic genes. Collectively, these results indicate that alterations in Ach release may influence dauer formation in C. elegans.",
author = "Jeeyong Lee and Kim, {Kwang Youl} and Young-Ki Paik",
year = "2014",
month = "1",
day = "1",
doi = "10.5483/BMBRep.2014.47.2.100",
language = "English",
volume = "47",
pages = "80--85",
journal = "BMB Reports",
issn = "1976-6696",
publisher = "The Biochemical Society of the Republic of Korea",
number = "2",

}

Alteration in cellular acetylcholine influences dauer formation in Caenorhabditis elegans. / Lee, Jeeyong; Kim, Kwang Youl; Paik, Young-Ki.

In: BMB reports, Vol. 47, No. 2, 01.01.2014, p. 80-85.

Research output: Contribution to journalArticle

TY - JOUR

T1 - Alteration in cellular acetylcholine influences dauer formation in Caenorhabditis elegans

AU - Lee, Jeeyong

AU - Kim, Kwang Youl

AU - Paik, Young-Ki

PY - 2014/1/1

Y1 - 2014/1/1

N2 - Altered acetylcholine (Ach) homeostasis is associated with loss of viability in flies, developmental defects in mice, and cognitive deficits in human. Here, we assessed the importance of Ach in Caenorhabditis elegans development, focusing on the role of Ach during dauer formation. We found that dauer formation was disturbed in choline acetyltransferase (cha-1) and acetylcholinesterase (ace) mutants defective in Ach biosynthesis and degradation, respectively. When examined the potential role of G-proteins in dauer formation, goa-1 and egl-30 mutant worms, expressing mutated versions of mammalian Go and Gq homolog, respectively, showed some abnormalities in dauer formation. Using quantitative mass spectrometry, we also found that dauer larvae had lower Ach content than did reproductively grown larvae. In addition, a proteomic analysis of acetylcholinesterase mutant worms, which have excessive levels of Ach, showed differential expression of metabolic genes. Collectively, these results indicate that alterations in Ach release may influence dauer formation in C. elegans.

AB - Altered acetylcholine (Ach) homeostasis is associated with loss of viability in flies, developmental defects in mice, and cognitive deficits in human. Here, we assessed the importance of Ach in Caenorhabditis elegans development, focusing on the role of Ach during dauer formation. We found that dauer formation was disturbed in choline acetyltransferase (cha-1) and acetylcholinesterase (ace) mutants defective in Ach biosynthesis and degradation, respectively. When examined the potential role of G-proteins in dauer formation, goa-1 and egl-30 mutant worms, expressing mutated versions of mammalian Go and Gq homolog, respectively, showed some abnormalities in dauer formation. Using quantitative mass spectrometry, we also found that dauer larvae had lower Ach content than did reproductively grown larvae. In addition, a proteomic analysis of acetylcholinesterase mutant worms, which have excessive levels of Ach, showed differential expression of metabolic genes. Collectively, these results indicate that alterations in Ach release may influence dauer formation in C. elegans.

UR - http://www.scopus.com/inward/record.url?scp=84894612147&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84894612147&partnerID=8YFLogxK

U2 - 10.5483/BMBRep.2014.47.2.100

DO - 10.5483/BMBRep.2014.47.2.100

M3 - Article

VL - 47

SP - 80

EP - 85

JO - BMB Reports

JF - BMB Reports

SN - 1976-6696

IS - 2

ER -