Proteomic analysis for inhibitory effect of chitosan oligosaccharides on 3T3‐L1 adipocyte differentiation

Abstract

In the present study, we performed a differential proteomic analysis using 2-DE combined with MS to clarify the molecular mechanism for the suppressive effect of chitosan oligosaccharides (CO) during differentiation of adipocyte 3T3-L1. Cell differentiation was significantly inhibited by CO at the concentration of 4 mg/mL. Protein mapping of adipocyte homogenates by 2-DE revealed that numerous protein spots were differentially altered in response to CO treatment. Out of 50 identified proteins showing significant alterations, six were up-regulated and 44 were down-regulated by CO treatment in comparison to control mature adipocytes. Among them, most of the proteins are associated with lipid metabolism, cytoskeleton, and redox regulation, in which the levels of farnesyl diphosphate synthetase (FDS), dedicator of cytokinesis 9 (DOCK9), and chloride intracellular channel 1 (CLIC1) were significantly reduced (>two-fold) with CO treatment. These results have not previously been examined in the context of adipogenesis, and thus can be used as novel biomarkers. Taken together with immunoblot analysis, it was concluded that the inhibitory effect of CO on adipocyte differentiation was mediated by C/EBPalpha and PPARgamma pathway through significant downregulations of important adipogenic molecules such as fatty acid binding protein and glucose transporter 4.

The expression and clinical significance of CLIC1 and HSP27 in lung adenocarcinoma

“…CLIC1 has been shown to interacts with Sedlin. Sedlin which as a components of TRAPP complex, has been reported to be involved in a defect in cartilage transport from endoplasmic reticulum to the Golgi complex [22].CLIC1 is also involved in cell cycle regulation [23] and in the regulation of cell proliferation and differentiation [24,25]. Recently, several studies have shown that CLIC1 is highly expressed in malignant tumors, such as gastric [26], colon [27], and liver [28,29] cancers.…”

Platycodin D inhibits adipogenesis of 3T3‐L1 cells by modulating kruppel‐like factor 2 and peroxisome proliferator‐activated receptor γ

“…Adipogenesis is known to be closely related to the etiologies of obesity and obesity-related metabolic disorders (Spiegelman et al, 1993). A mouse preadipocyte cell line 3T3-L1, originally derived from a mouse embryo, can be differentiated into adipocytes, and has been widely used as an in vitro model for studying obesity (Green and Meuth, 1974;Harmon and Harp, 2001;Madsen et al, 2005;Rahman et al, 2008). During adipogenesis, 3T3-L1 cells change from fi broblast-like preadipocytes to spherical adipocytes and accumulate large fat droplets containing triglycerides (Jessen and Stevens, 2002).…”

Protein hydrolysates from β‐conglycinin enriched soybean genotypes inhibit lipid accumulation and inflammation in vitro

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