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Isolation of extracellular fluids reveals novel secreted bioactive proteins from muscle and fat tissues

ABSTRACT: Isolation of extracellular fluids reveals novel secreted bioactive proteins from muscle and fat tissues

PROVIDER: PRJNA892075 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR21972723_1.fastq.gz	Fastqsanger.gz
	SRR21972723_2.fastq.gz	Fastqsanger.gz
	SRR21972724_1.fastq.gz	Fastqsanger.gz
	SRR21972724_2.fastq.gz	Fastqsanger.gz
	SRR21972725_1.fastq.gz	Fastqsanger.gz

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Isolation of extracellular fluids reveals novel secreted bioactive proteins from muscle and fat tissues

Project description:Proteins are secreted from cells to send information to neighboring cells or distant tissues. Because of the highly integrated nature of energy balance systems, there has been particular interest in myokines and adipokines. These are challenging to study through proteomics because serum or plasma contain highly abundant proteins that limit the detection of proteins with lower abundance. We show here that extracellular fluid (EF) from muscle and fat tissues of mice show a different protein composition than either serum or tissues. Mass spectrometry analyses of EFs from mice with physiological perturbations, like exercise or cold exposure, allowed quantification of many potentially novel myokines and adipokines. Using this approach, we identify prosaposin as a secreted product of muscle and fat. Prosaposin expression stimulates thermogenic gene expression and induces mitochondrial respiration in primary fat cells. These studies together illustrate the utility of EF isolation as a discovery tool for adipokines and myokines.

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Isolation of interstitial fluids reveals novel secreted bioactive proteins from muscle and fat tissues

Project description:Proteins are secreted from various cells to send information to neighboring cells or distant tissues. Because of the highly integrated nature of energy balance systems, there has been a great deal of interest in myokines and adipokines, proteins secreted from muscle and fat tissues, respectively. These have been challenging to study through proteomics because serum is loaded with super-abundant proteins that limit the detection of proteins that have a low, hormone-like abundance. We show here that interstitial fluids (IFs) can be harvested easily from muscle and fat tissues of mice by very low-speed centrifugation and these fluids show a very different protein constellation than that of plasma or tissues. Under several different perturbations in vivo, like exercise or cold, quantitative Mass Spectrometry of these IFs allowed for the identification of many novel myokines and adipokines, including factors both increased and decreased in abundance. Finally, we identify prosaposin, a well-known neurotrophic factor, as a secreted product of both muscle and fat tissues; recombinant prosaposin stimulates a gene program related to thermogenesis in primary fat cells, indicating one potential function for PSAP.

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Isolation of extracellular fluids reveals novel secreted bioactive proteins from muscle and fat tissues.

Project description:Proteins are secreted from cells to send information to neighboring cells or distant tissues. Because of the highly integrated nature of energy balance systems, there has been particular interest in myokines and adipokines. These are challenging to study through proteomics because serum or plasma contains highly abundant proteins that limit the detection of proteins with lower abundance. We show here that extracellular fluid (EF) from muscle and fat tissues of mice shows a different protein composition than either serum or tissues. Mass spectrometry analyses of EFs from mice with physiological perturbations, like exercise or cold exposure, allowed the quantification of many potentially novel myokines and adipokines. Using this approach, we identify prosaposin as a secreted product of muscle and fat. Prosaposin expression stimulates thermogenic gene expression and induces mitochondrial respiration in primary fat cells. These studies together illustrate the utility of EF isolation as a discovery tool for adipokines and myokines.

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