Day and night isotope labelling reveal metabolic pathway specific regulation of protein synthesis rates in Arabidopsis

2022 ◽  
Author(s):  
Owen Duncan ◽  
A. Harvey Millar
Keyword(s):  
Protein Synthesis ◽  
Metabolic Pathway ◽  
Isotope Labelling ◽  
Specific Regulation

Oxidant-specific regulation of protein synthesis in Candida albicans

2014 ◽  
Vol 67 ◽  
pp. 15-23 ◽  
Author(s):  
Arunkumar Sundaram ◽  
Chris M. Grant
Keyword(s):  
Protein Synthesis ◽  
Candida Albicans ◽  
Specific Regulation

Stable isotope-labelling analysis of the impact of inhibition of the mammalian target of rapamycin on protein synthesis

2012 ◽  
Vol 444 (1) ◽  
pp. 141-151 ◽  
Author(s):  
Yilin Huo ◽  
Valentina Iadevaia ◽  
Zhong Yao ◽  
Isabelle Kelly ◽  
Sabina Cosulich ◽  
...  
Keyword(s):  
Protein Synthesis ◽  
Stable Isotope ◽  
Mammalian Target Of Rapamycin ◽  
Mrna Translation ◽  
Target Of Rapamycin ◽  
Stable Isotope Labelling ◽  
Isotope Labelling ◽  
Cell Functions ◽  
Specific Mrnas ◽  
The Impact

mTORC1 [mTOR (mammalian target of rapamycin) complex 1] regulates diverse cell functions. mTORC1 controls the phosphorylation of several proteins involved in mRNA translation and the translation of specific mRNAs, including those containing a 5′-TOP (5′-terminal oligopyrimidine). To date, most of the proteins encoded by known 5′-TOP mRNAs are proteins involved in mRNA translation, such as ribosomal proteins and elongation factors. Rapamycin inhibits some mTORC1 functions, whereas mTOR-KIs (mTOR kinase inhibitors) interfere with all of them. mTOR-KIs inhibit overall protein synthesis more strongly than rapamycin. To study the effects of rapamycin or mTOR-KIs on synthesis of specific proteins, we applied pSILAC [pulsed SILAC (stable isotope-labelling with amino acids in cell culture)]. Our results reveal, first, that mTOR-KIs and rapamycin differentially affect the synthesis of many proteins. Secondly, mTOR-KIs inhibit the synthesis of proteins encoded by 5′-TOP mRNAs much more strongly than rapamycin does, revealing that these mRNAs are controlled by rapamycin-insensitive outputs from mTOR. Thirdly, the synthesis of certain other proteins shows a similar pattern of inhibition. Some of them appear to be encoded by ‘novel’ 5′-TOP mRNAs; they include proteins which, like known 5′-TOP mRNA-encoded proteins, are involved in protein synthesis, whereas others are enzymes involved in intermediary or anabolic metabolism. These results indicate that mTOR signalling may promote diverse biosynthetic processes through the translational up-regulation of specific mRNAs. Lastly, a SILAC-based approach revealed that, although rapamycin and mTOR-KIs have little effect on general protein stability, they stabilize proteins encoded by 5′-TOP mRNAs.

scholarly journals Dynamics of murine brain protein synthesis in vivo identify the hippocampus, cortex and cerebellum as highly active metabolic sites

2019 ◽  
Author(s):  
Ser Sue Ng ◽  
Jung Eun Park ◽  
Wei Meng ◽  
Christopher Li-Hsian Chen ◽  
Raj N. Kalaria ◽  
...  
Keyword(s):  
Amino Acids ◽  
Cell Culture ◽  
Protein Synthesis ◽  
Stable Isotope ◽  
Density Lipoprotein ◽  
Apolipoprotein A1 ◽  
Stable Isotope Labelling ◽  
Isotope Labelling ◽  
Highly Active

AbstractIdentification of proteins that are synthesized de novo in response to specific microenvironmental cues is critical to understanding the molecular mechanisms that underpin key physiological processes and pathologies. Here we report that a brief period of pulsed SILAC diet (Stable Isotope Labelling by Amino acids in Cell culture) enables determination of biological functions corresponding to actively translating proteins in the mouse brain. Our data demonstrate that the hippocampus, cortex and cerebellum are highly active sites of protein synthesis, rapidly expressing key mediators of nutrient sensing and lipid metabolism, as well as critical regulators of synaptic function, axon guidance, and circadian entrainment. Together, these findings confirm that protein metabolic activity varies significantly between brain regions in vivo and indicate that pSILAC-based approaches can identify specific anatomical sites and biological pathways likely to be suitable for drug targeting in neurodegenerative disorders.AbbreviationsApoA1: Apolipoprotein A1, ApoA4: Apolipoprotein A4, ApoE: Apolipoprotein E, ApoJ/Clu: Apolipoprotein J/Clusterin, App: Amyloid-β precursor/A4 protein: App, HDL: high density lipoprotein, Lrp1: Low density lipoprotein receptor-related protein 1, pSILAC: pulsed SILAC, pSIVOM: pulsed-SILAC in vivo labelling in mouse, SILAC: Stable Isotope Labelling by Amino acids in Cell culture)

Tissue-specific regulation of protein synthesis by insulin and free fatty acids

2003 ◽  
Vol 285 (4) ◽  
pp. E754-E762 ◽  
Author(s):  
Stephen J. Crozier ◽  
Joshua C. Anthony ◽  
Charles M. Schworer ◽  
Ali K. Reiter ◽  
Tracy G. Anthony ◽  
...  
Keyword(s):  
Protein Synthesis ◽  
Translational Control ◽  
Mammalian Target Of Rapamycin ◽  
Diabetic Rats ◽  
Mtor Signaling ◽  
Initiation Factor ◽  
Energy Status ◽  
Cellular Energy ◽  
Specific Regulation ◽  
Induced Changes

The purpose of the study described herein was to investigate how the mammalian target of rapamycin (mTOR)-signaling pathway and eukaryotic initiation factor 2B (eIF2B) activity, both having key roles in the translational control of protein synthesis in skeletal muscle, are regulated in cardiac muscle of rats in response to two different models of altered free fatty acid (FFA) and insulin availability. Protein synthetic rates were reduced in both gastrocnemius and heart of 3-day diabetic rats. The reduction was associated with diminished mTOR-mediated signaling and eIF2B activity in the gastrocnemius but only with diminished mTOR signaling in the heart. In response to the combination of acute hypoinsulinemia and hypolipidemia induced by administration of niacin, protein synthetic rates were also diminished in both gastrocnemius and heart. The niacin-induced changes were associated with diminished mTOR signaling and eIF2B activity in the heart but only with decreased mTOR signaling in the gastrocnemius. In the heart, mTOR signaling and eIF2B activity correlated with cellular energy status and/or redox potential. Thus FFAs may contribute to the translational control of protein synthesis in the heart but not in the gastrocnemius. In contrast, insulin, but not FFAs, is required for the maintenance of protein synthesis in the gastrocnemius.

EFFECT OF PROGESTERONE ON RNA AND PROTEIN SYNTHESIS IN THE RAT UTERUS

1973 ◽  
Vol 73 (4) ◽  
pp. 740-750 ◽  
Author(s):  
G. Trams ◽  
H. Brewitt ◽  
H. Möllmann ◽  
H. Maass
Keyword(s):  
Protein Synthesis ◽  
Nucleic Acid ◽  
Cell Membrane ◽  
Inhibitory Effect ◽  
Rat Uterus ◽  
Isotope Labelling ◽  
Uridine Incorporation ◽  
Rna And Protein Synthesis ◽  
Modifying Effect

ABSTRACT The effect of gestagenic compounds on the oestrogen induced nucleic acid and protein synthesis of the rat uterus after castration was investigated. Progesterone causes an inhibition of 3H-uridine incorporation into uterine RNA. The inhibitory effect is strongest when progesterone is administered within 1 hour before isotope labelling. Evaluation of the free labelled nucleotides shows that this effect is not achieved by a blockade of permeability at the cell membrane or by reduction of the phosphorylation process. As a result of this progesterone-induced inhibition, protein synthesis is also reduced. These results are discussed with regard to the modifying effect of progesterone on oestrogen dependent functions in the uterus.

scholarly journals Hepatocytes produce nitrogen oxides from L-arginine in response to inflammatory products of Kupffer cells.

1989 ◽  
Vol 170 (5) ◽  
pp. 1769-1774 ◽  
Author(s):  
R D Curran ◽  
T R Billiar ◽  
D J Stuehr ◽  
K Hofmann ◽  
R L Simmons
Keyword(s):  
Endothelial Cells ◽  
Protein Synthesis ◽  
Nitrogen Oxides ◽  
Kupffer Cells ◽  
Metabolic Pathway ◽  
Active Compound ◽  
Total Protein ◽  
Biologically Active ◽  
Biologically Active Compound

A metabolic pathway by which L-arginine (L-arg) is converted to the biologically active compound NO. has recently been described in macrophages (M phi) and endothelial cells. This report demonstrates that transferable products from activated Kupffer cells (KC) induce the conversion of large quantities of L-arg to nitrogen oxides within hepatocytes (HC). In M phi and endothelial cells, citrulline and NO2-/NO3- are the stable endproducts of this metabolic pathway. In contrast, HC L-arg metabolism resulted in significantly greater production of NO2-/NO3- than citrulline. The generation of NO. within HC was associated with a concurrent decrease in total protein synthesis.

scholarly journals Tissue-Specific Regulation of Mitochondrial and Cytoplasmic Protein Synthesis Rates by Insulin

Diabetes ◽  
2001 ◽  
Vol 50 (12) ◽  
pp. 2652-2658 ◽  
Author(s):  
Y. Boirie ◽  
K. R. Short ◽  
B. Ahlman ◽  
M. Charlton ◽  
K. S. Nair
Keyword(s):  
Protein Synthesis ◽  
Cytoplasmic Protein ◽  
Tissue Specific ◽  
Specific Regulation

Metabolic pathway structures for recombinant protein synthesis in Escherichia coli

2005 ◽  
Vol 68 (6) ◽  
pp. 737-746 ◽  
Author(s):  
Natarajan Vijayasankaran ◽  
Ross Carlson ◽  
Friedrich Srienc
Keyword(s):  
Escherichia Coli ◽  
Protein Synthesis ◽  
Recombinant Protein ◽  
Metabolic Pathway

scholarly journals mTORC1 mediates fiber type-specific regulation of protein synthesis and muscle size during denervation

2021 ◽  
Vol 7 (1) ◽  
Author(s):  
Jae-Sung You ◽  
Kookjoo Kim ◽  
Nathaniel D. Steinert ◽  
Jie Chen ◽  
Troy A. Hornberger
Keyword(s):  
Skeletal Muscle ◽  
Protein Synthesis ◽  
Fiber Type ◽  
Muscle Fibers ◽  
Mammalian Target Of Rapamycin ◽  
Muscle Size ◽  
Muscle Denervation ◽  
Pronounced Increase ◽  
Specific Regulation ◽  
Net Protein

AbstractSkeletal muscle denervation occurs in diverse conditions and causes severe muscle atrophy. Signaling by mammalian target of rapamycin complex 1 (mTORC1) plays a central role in the maintenance of skeletal muscle mass by regulating net protein balance; yet, its role in denervation-induced atrophy is unclear. In this study, by using skeletal muscle-specific and inducible raptor knockout mice, we demonstrate that signaling through mTORC1 is activated during denervation and plays an essential role in mitigating the atrophy of non-type IIB muscle fibers. Measurements of protein synthesis rates of individual fibers suggest that denervation increases protein synthesis specifically in non-type IIB muscle fibers and that mTORC1 is required for this event. Furthermore, denervation induced a more pronounced increase in the level of phosphorylated ribosomal S6 protein in non-type IIB muscle fibers than in type IIB muscle fibers. Collectively, our results unveil a novel role for mTORC1 in mediating a fiber type-specific regulation of muscle size and protein synthesis during denervation.

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