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Open AccessArticle

Proteomic Analysis of 3T3-L1 Adipocytes Treated with Insulin and TNF-α

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Department of Computer Science, Purdue University, West Lafayette, IN 47907, USA
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College of Agriculture, Purdue University, West Lafayette, IN 47907, USA
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Purdue Proteomics Facility, Bindley Bioscience Center, Purdue University, West Lafayette, IN 47907, USA
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Purdue Institute of Inflammation, Immunology and Infectious Disease, Purdue University, West Lafayette, IN 47907, USA
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Department of Nutrition Science, Purdue University, West Lafayette, IN 47907, USA
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Department of Comparative Pathobiology, College of Veterinary Medicine, Purdue University, West Lafayette, IN 47907, USA
*
Author to whom correspondence should be addressed.
Present addresses: Indiana University School of Medicine, West Lafayette, IN 47907, USA.
Present addresses: Division of Digital Psychiatry, Harvard Medical School, Boston, MA 02111, USA.
§
Present addresses: Pharmavite, Los Angeles, CA 90089, USA.
Proteomes 2019, 7(4), 35; https://doi.org/10.3390/proteomes7040035
Received: 29 August 2019 / Revised: 14 October 2019 / Accepted: 17 October 2019 / Published: 20 October 2019
Insulin resistance is an indication of early stage Type 2 diabetes (T2D). Insulin resistant adipose tissues contain higher levels of insulin than the physiological level, as well as higher amounts of intracellular tumor necrosis factor-α (TNF-α) and other cytokines. However, the mechanism of insulin resistance remains poorly understood. To better understand the roles played by insulin and TNF-α in insulin resistance, we performed proteomic analysis of differentiated 3T3-L1 adipocytes treated with insulin (Ins), TNF-α (TNF), and both (Ins + TNF). Out of the 693 proteins identified, the abundances of 78 proteins were significantly different (p < 0.05). Carnitine parmitoyltransferase-2 (CPT2), acetyl CoA carboxylase 1 (ACCAC-1), ethylmalonyl CoA decarboxylase (ECHD1), and methylmalonyl CoA isomerase (MCEE), enzymes required for fatty acid β-oxidation and respiratory electron transport, and β-glucuronidase, an enzyme responsible for the breakdown of complex carbohydrates, were down-regulated in all the treatment groups, compared to the control group. In contrast, superoxide dismutase 2 (SOD2), protein disulfide isomerase (PDI), and glutathione reductase, which are the proteins responsible for cytoskeletal structure, protein folding, degradation, and oxidative stress responses, were up-regulated. This suggests higher oxidative stress in cells treated with Ins, TNF, or both. We proposed a conceptual metabolic pathway impacted by the treatments and their possible link to insulin resistance or T2D. View Full-Text
Keywords: 3T3-L cells; insulin; tumor necrosis factor-α; type II diabetes; quantitative proteomics; mass spectrometry 3T3-L cells; insulin; tumor necrosis factor-α; type II diabetes; quantitative proteomics; mass spectrometry
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MDPI and ACS Style

Chan, H.; Bhide, K.P.; Vaidyam, A.; Hedrick, V.; Sobreira, T.J.P.; Sors, T.G.; Grant, R.W.; Aryal, U.K. Proteomic Analysis of 3T3-L1 Adipocytes Treated with Insulin and TNF-α. Proteomes 2019, 7, 35.

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