The secrets of protein secretion: what are the key features of comparative secretomics?

Stühler, Kai

doi:10.1080/14789450.2020.1881890

Cited by 5 publications

(2 citation statements)

References 16 publications

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“…Traditional fractionation techniques, such as density centrifugation are being used to enrich for exosomes and extracellular vesicles and are followed by analysis of the cargo proteins within [45,46]. Attention has also focused on methods to measure the proteins present in the extracellular matrix [46,47], including secreted proteins [48] such as those in the senescence associated secretory phenotype (SASP), in which senescent cells express and secrete proteins in response to DNA damage [49].…”

Section: Subcellular Organelle and Extracellular Fractionationmentioning

confidence: 99%

Proximity labeling and other novel mass spectrometric approaches for spatiotemporal protein dynamics

Pino

Schilling

2021

Expert Review of Proteomics

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Background: Proteins are highly dynamic and their biological function is controlled by not only temporal abundance changes but also via regulated protein-protein interaction networks, which respond to internal and external perturbations. A wealth of novel analytical reagents and workflows allow studying spatiotemporal protein environments with great granularity while maintaining high throughput and ease of analysis. Areas covered: We review technology advances for measuring protein-protein proximity interactions with an emphasis on proximity labeling, and briefly summarize other spatiotemporal approaches including protein localization, and their dynamic changes over time, specifically in human cells and mammalian tissues. We focus especially on novel technologies and workflows emerging within the past 5 years. This includes enrichment-based techniques (proximity labeling and crosslinking), separationbased techniques (organelle fractionation and size exclusion chromatography), and finally sortingbased techniques (laser capture microdissection and mass spectrometry imaging). Expert opinion: Spatiotemporal proteomics is a key step in assessing biological complexity, understanding refined regulatory mechanisms, and forming protein complexes and networks. Studying protein dynamics across space and time holds promise for gaining deep insights into how protein networks may be perturbed during disease and aging processes, and offer potential avenues for therapeutic interventions, drug discovery, and biomarker development.

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Section: Subcellular Organelle and Extracellular Fractionationmentioning

confidence: 99%

Proximity labeling and other novel mass spectrometric approaches for spatiotemporal protein dynamics

Pino

Schilling

2021

Expert Review of Proteomics

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show abstract

“…The secretome of a cell or an organism consists of proteins secreted by the endoplasmic reticulum (ER)–Golgi secretory pathway and other direct or vesicle-based mechanisms ( 10 , 11 , 12 ). In addition, ectodomains of membrane proteins can be proteolytically released into the extracellular environment.…”

mentioning

confidence: 99%

Interval-Based Secretomics Unravels Acute-Phase Response in Hepatocyte Model Systems

Knecht

Eberl

Bantscheff

2022

Molecular & Cellular Proteomics

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The cytotoxicity of PM2.5 and its effect on the secretome of normal human bronchial epithelial cells

Sui

Song

et al. 2022

Environ Sci Pollut Res

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The secrets of protein secretion: what are the key features of comparative secretomics?

Cited by 5 publications

References 16 publications

Proximity labeling and other novel mass spectrometric approaches for spatiotemporal protein dynamics

Proximity labeling and other novel mass spectrometric approaches for spatiotemporal protein dynamics

Interval-Based Secretomics Unravels Acute-Phase Response in Hepatocyte Model Systems

The cytotoxicity of PM2.5 and its effect on the secretome of normal human bronchial epithelial cells

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