Leptin-induced matrix metalloproteinase-2 secretion is suppressed by trans-10,cis-12 conjugated linoleic acid.
It has long been recognized that leptin, a hormone made by adipocytes, is an important circulating signal for the regulation of body weight. In addition, matrix metalloproteinase (MMP), especially MMP-2, an adipocyte-secreted protein which promotes multi-cellular adipose clusters, is up-regulated in obesity. The present study is designed to evaluate whether trans-10,cis-12 conjugated linoleic acid (t-CLA) can suppress leptin-induced MMP-2 secretion in 3T3-L1 cells. The result showed that expressions of adipocyte marker proteins were significantly reduced by t-CLA-treated cultures, but not by linoleic acid (LA)-treated ones. Interestingly, MMP-2 secretion was significantly increased by leptin-treated cultures, thereby leading to accelerate adipocyte differentiation, indicating that MMP-2 was a necessary mediator of adipogenesis. However, increasing concentration of t-CLA significantly reduced leptin-induced MMP-2 secretion and triglyceride (TG) content. These findings provide support for a role for t-CLA in the regulation of metabolism in leptin-induced adipose tissue development.
Moon
Hyun-Seuk
HS
School of Agricultural Biotechnology, Seoul National University, Seoul 151-921, Republic of Korea.
Lee
Hong-Gu
HG
Seo
Ji-Hye
JH
Chung
Chung-Soo
CS
Guo
Ding-Ding
DD
Kim
Tae-Gyu
TG
Choi
Yun-Jaie
YJ
Cho
Chong-Su
CS
D041721:3T3-L1 Cells; D017667:Adipocytes / Q000187:drug effects / Q000201:enzymology*; D050156:Adipogenesis / Q000187:drug effects / Q000502:physiology*; D000818:Animals; D004338:Drug Combinations; D020738:Leptin / Q000008:administration & dosage*; D044243:Linoleic Acids, Conjugated / Q000008:administration & dosage*; D020778:Matrix Metalloproteinase 2 / Q000378:metabolism*; D051379:Mice; D015398:Signal Transduction / Q000187:drug effects / Q000502:physiology*
D004338:Drug Combinations; D020738:Leptin; D044243:Linoleic Acids, Conjugated; C496197:trans-10,cis-12-conjugated linoleic acid; D020778:Matrix Metalloproteinase 2