科学家找到了一种可能让身体消耗更多能量的新方法，研究论文发表于2月3日《细胞代谢》杂志。
这种新方法聚焦于一种间接控制“能量主开关”活动性的酶，这种酶叫Fyn激酶，如果给实验室老鼠注射抑制这种酶的化学物质，它们几乎马上开始燃烧更多脂肪。美国艾伯特爱因斯坦医学和神经系统科学院的克莱尔巴斯特说：“当我们的摄入热量和燃烧热量不平衡时，肥胖问题就来了，这是一种帮助身体燃烧额外热量的新机制。”
巴斯特研究组发现，缺乏Fyn激酶的老鼠燃烧脂肪酸更多，消耗能量更多，也越来越瘦。这是“能量主开关”磷酸化腺苷酸活化蛋白激酶在它们脂肪和肌肉组织中含量较少的结果。 这些发现显示，这种酶有可能帮助开发一种减肥新药。现在，这项研究为用SU6656 药抑制Fyn激酶明显利于老鼠新陈代谢的说法提供了新的支持。
推荐原始出处：
Cell Metabolism, Volume 11, Issue 2, 113-124, 3 February 2010 DOI:10.1016/j.cmet.2009.12.010
Fyn-Dependent Regulation of Energy Expenditure and Body Weight Is Mediated by Tyrosine Phosphorylation of LKB1
Eijiro Yamada, Jeffrey E. Pessin, Irwin J. Kurland, Gary J. Schwartz, Claire C. Bastie
Fyn null mice display reduced adiposity associated with increased fatty acid oxidation, energy expenditure, and activation of the AMP-dependent protein kinase (AMPK) in skeletal muscle and adipose tissue. The acute pharmacological inhibition of Fyn kinase activity with SU6656 in wild-type mice reproduces these metabolic effects and induced a specific reduction in fat mass with no change in lean mass. LKB1, the main upstream AMPK kinase (AMPKK) in peripheral tissues, was redistributed from the nucleus into the cytoplasm of cells treated with SU6656 and in cells expressing a kinase-deficient, but not a constitutively kinase-active, Fyn mutant. Moreover, Fyn kinase directly phosphorylated LKB1 on tyrosine 261 and 365 residues, and mutations of these sites resulted in LKB1 export into the cytoplasm and increased AMPK phosphorylation. These data demonstrate a crosstalk between Fyn tyrosine kinase and the AMPK energy-sensing pathway, through Fyn-dependent regulation of the AMPK upstream activator LKB1.
