Soluble soy protein peptic hydrolysate stimulates adipocyte differentiation in 3T3-L1 cells
Article first published online: 8 MAR 2013
© 2013 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim
Molecular Nutrition & Food Research
Special Issue: Lipidomics: Approaches and Applications in Nutrition Research
Volume 57, Issue 8, pages 1435–1445, August 2013
How to Cite
Goto, T., Mori, A. and Nagaoka, S. (2013), Soluble soy protein peptic hydrolysate stimulates adipocyte differentiation in 3T3-L1 cells. Mol. Nutr. Food Res., 57: 1435–1445. doi: 10.1002/mnfr.201200573
- Issue published online: 2 AUG 2013
- Article first published online: 8 MAR 2013
- Manuscript Accepted: 16 JAN 2013
- Manuscript Revised: 26 DEC 2012
- Manuscript Received: 27 AUG 2012
- Ministry of Education, Culture, Sports, Science and Technology of Japan. Grant Numbers: 22780816, 24688015
- Uehara Memorial Foundation, and the Iijima Memorial Foundation
- Adipocyte differentiation;
- Soy peptides;
- Soybean protein peptic hydrolysate
The molecular mechanisms underlying the potential health benefit effects of soybean proteins on obesity-associated metabolic disorders have not been fully clarified. In this study, we investigated the effects of soluble soybean protein peptic hydrolysate (SPH) on adipocyte differentiation by using 3T3-L1 murine preadipocytes.
Methods and results
The addition of SPH increased lipid accumulation during adipocyte differentiation. SPH increased the mRNA expression levels of an adipogenic marker gene and decreased that of a preadipocyte marker gene, suggesting that SPH promotes adipocyte differentiation. SPH induced antidiabetic and antiatherogenic adiponectin mRNA expression and secretion. Moreover, SPH increased the mRNA expression levels of insulin-responsive glucose transporter 4 and insulin-stimulated glucose uptake. The expression levels of peroxisome proliferator-activated receptor γ (PPARγ), a key regulator of adipocyte differentiation, during adipocyte differentiation were up-regulated in 3T3-L1 cells treated with SPH, and lipid accumulation during adipocyte differentiation induced by SPH was inhibited in the presence of a PPARγ antagonist. However, SPH did not exhibit PPARγ ligand activity.
These findings indicate that SPH stimulates adipocyte differentiation, at least in part, via the up-regulation of PPARγ expression levels. These effects of SPH might be important for the health benefit effects of soybean proteins on obesity-associated metabolic disorders.