Proteomic profiling of human plasma exosomes identifies PPARgamma as an exosome-associated protein.

Proteomic profiling of human plasma exosomes identifies PPARgamma as an exosome-associated protein.
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DOI:
10.1016/j.bbrc.2008.11.050
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发表时间:
2009-01-16
影响因子:
3.1
通讯作者:
Levine, Stewart J.
Levine, Stewart J.
中科院分区:
生物学4区
文献类型:
--
作者:
Looze, Christopher;Yui, David;Leung, Lester;Ingham, Matthew;Kaler, Maryann;Yao, Xianglan;Wu, Wells W.;Shen, Rong-Fong;Daniels, Mathew P.;Levine, Stewart J.

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Exosomes are nanovesicles that are released from cells as a mechanism of cell-free intercellular communication. Only a limited number of proteins have been identified from the plasma exosome proteome. Here, we developed a multi-step fractionation scheme incorporating gel exclusion chromatography, rate zonal centrifugation through continuous sucrose gradients, and high-speed centrifugation to purify exosomes from human plasma. Exosome-associated proteins were separated by SDS-PAGE and 66 proteins were identified by LC-MS/MS, which included both cellular and extracellular proteins. Furthermore, we identified and characterized peroxisome proliferator-activated receptor-γ (PPARγ), a nuclear receptor that regulates adipocyte differentiation and proliferation, as well as immune and inflammatory cell functions, as a novel component of plasma-derived exosomes. Given the important role of exosomes as intercellular messengers, the discovery of PPARγ as a component of human plasma exosomes identifies a potential new pathway for the paracrine transfer of nuclear receptors.
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