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Suh, Pann-Ghill
BioSignal Network Lab (BSN)
Research Interests
  • Signal transduction, cancer, metabolism, phospholipase C

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Comparative proteomic analysis of the insulin-induced L6 myotube secretome

Cited 26 times inthomson ciCited 27 times inthomson ci
Title
Comparative proteomic analysis of the insulin-induced L6 myotube secretome
Author
Yoon, Jong HyukYea, KyungmooKim, JaeyoonChoi, Yoon SupPark, SehoonLee, HyeongjiLee, Chang SupSuh, Pann-GhillRyu, Sung Ho
Keywords
Liquid chromatography-tandem mass spectrometry; Secreted protein; Shotgun proteomics
Issue Date
200901
Publisher
WILEY-BLACKWELL
Citation
PROTEOMICS, v.9, no.1, pp.51 - 60
Abstract
Emerging evidence has revealed an endocrine function for skeletal muscle; in fact, certain antiinflammatory cytokines are secreted only from contractile skeletal muscle. However, the skeletal muscle secretome as a whole is poorly characterized, as is how it changes in response to extracellular stimuli. Herein, we sought to identify and characterize the members of the skeletal muscle secretome, and to determine which protein secretion levels were modulated in response to insulin stimulation. To conduct these studies, we treated differentiated L6 rat skeletal muscle cells with insulin or left them untreated, and we comparatively analyzed the proteins secreted into the media. We fractionated this conditioned media using offline RP HPLC, digested the fractionated proteins, and analyzed the resulting peptides with LC-ESI-MS/MS. We identified a total of 254 proteins, and by using three different filtering methods, we identified 153 of these as secretory proteins. Fourteen proteins were secreted at higher levels under insulin stimulation, including several proteins known to be highly secreted in metabolic diseases; 19 proteins were secreted at lower levels under insulin stimulation. These result not only pinpointed several previously unknown, insulin induced, secretory proteins of skeletal muscle, it also described a novel approach for conditioned secretome analysis.
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DOI
http://dx.doi.org/10.1002/pmic.200800187
ISSN
1615-9853
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