Pulsed SILAM reveals in vivo dynamics of murine brain protein translation

Identification of proteins that are synthesized de novo in response to specific microenvironmental cues is critical for understanding molecular mechanisms that underpin vital physiological processes and pathologies. Here, we report that a brief period of SILAM (Stable Isotope Labeling of Mammals) di...

Full description

Saved in:
Bibliographic Details
Main Authors: Ng, Ser Sue, Park, Jung Eun, Meng, Wei, Chen, Christopher P., Kalaria, Raj N., McCarthy, Neil E., Sze, Siu Kwan
Other Authors: School of Biological Sciences
Format: Article
Language:English
Published: 2020
Subjects:
Online Access:https://hdl.handle.net/10356/142786
Tags: Add Tag
No Tags, Be the first to tag this record!
Institution: Nanyang Technological University
Language: English
id sg-ntu-dr.10356-142786
record_format dspace
spelling sg-ntu-dr.10356-1427862023-02-28T16:56:14Z Pulsed SILAM reveals in vivo dynamics of murine brain protein translation Ng, Ser Sue Park, Jung Eun Meng, Wei Chen, Christopher P. Kalaria, Raj N. McCarthy, Neil E. Sze, Siu Kwan School of Biological Sciences Science::Biological sciences Protein Identification Peptides and Proteins Identification of proteins that are synthesized de novo in response to specific microenvironmental cues is critical for understanding molecular mechanisms that underpin vital physiological processes and pathologies. Here, we report that a brief period of SILAM (Stable Isotope Labeling of Mammals) diet enables the determination of biological functions corresponding to actively translating proteins in the mouse brain. Our results demonstrate that the synapse, dendrite, and myelin sheath are highly active neuronal structures that display rapid protein synthesis, producing key mediators of chemical signaling as well as nutrient sensing, lipid metabolism, and amyloid precursor protein processing/stability. Together, these findings confirm that protein metabolic activity varies significantly between brain functional units in vivo. Our data indicate that pulsed SILAM approaches can unravel complex protein expression dynamics in the murine brain and identify active synthetic pathways and associated functions that are likely impaired in neurodegenerative diseases. MOE (Min. of Education, S’pore) Published version 2020-06-30T07:17:59Z 2020-06-30T07:17:59Z 2020 Journal Article Ng, S. S., Park, J. E., Meng, W., Chen, C. P., Kalaria, R. N., McCarthy, N. E., & Sze, S. K. (2020). Pulsed SILAM reveals in vivo dynamics of murine brain protein translation. ACS Omega, 5(23), 13528-13540. doi:10.1021/acsomega.9b04439 2470-1343 https://hdl.handle.net/10356/142786 10.1021/acsomega.9b04439 32566817 2-s2.0-85085742737 23 5 13528 13540 en ACS Omega © 2020 American Chemical Society. This is an open access article published under an ACS AuthorChoice License, which permits copying and redistribution of the article or any adaptations for non-commercial purposes. application/pdf
institution Nanyang Technological University
building NTU Library
continent Asia
country Singapore
Singapore
content_provider NTU Library
collection DR-NTU
language English
topic Science::Biological sciences
Protein Identification
Peptides and Proteins
spellingShingle Science::Biological sciences
Protein Identification
Peptides and Proteins
Ng, Ser Sue
Park, Jung Eun
Meng, Wei
Chen, Christopher P.
Kalaria, Raj N.
McCarthy, Neil E.
Sze, Siu Kwan
Pulsed SILAM reveals in vivo dynamics of murine brain protein translation
description Identification of proteins that are synthesized de novo in response to specific microenvironmental cues is critical for understanding molecular mechanisms that underpin vital physiological processes and pathologies. Here, we report that a brief period of SILAM (Stable Isotope Labeling of Mammals) diet enables the determination of biological functions corresponding to actively translating proteins in the mouse brain. Our results demonstrate that the synapse, dendrite, and myelin sheath are highly active neuronal structures that display rapid protein synthesis, producing key mediators of chemical signaling as well as nutrient sensing, lipid metabolism, and amyloid precursor protein processing/stability. Together, these findings confirm that protein metabolic activity varies significantly between brain functional units in vivo. Our data indicate that pulsed SILAM approaches can unravel complex protein expression dynamics in the murine brain and identify active synthetic pathways and associated functions that are likely impaired in neurodegenerative diseases.
author2 School of Biological Sciences
author_facet School of Biological Sciences
Ng, Ser Sue
Park, Jung Eun
Meng, Wei
Chen, Christopher P.
Kalaria, Raj N.
McCarthy, Neil E.
Sze, Siu Kwan
format Article
author Ng, Ser Sue
Park, Jung Eun
Meng, Wei
Chen, Christopher P.
Kalaria, Raj N.
McCarthy, Neil E.
Sze, Siu Kwan
author_sort Ng, Ser Sue
title Pulsed SILAM reveals in vivo dynamics of murine brain protein translation
title_short Pulsed SILAM reveals in vivo dynamics of murine brain protein translation
title_full Pulsed SILAM reveals in vivo dynamics of murine brain protein translation
title_fullStr Pulsed SILAM reveals in vivo dynamics of murine brain protein translation
title_full_unstemmed Pulsed SILAM reveals in vivo dynamics of murine brain protein translation
title_sort pulsed silam reveals in vivo dynamics of murine brain protein translation
publishDate 2020
url https://hdl.handle.net/10356/142786
_version_ 1759856877649264640