Functions of AMP‐activated protein kinase in adipose tissue

Journal of Physiology - Tập 574 Số 1 - Trang 55-62 - 2006
Marie Daval1, Fabienne Foufelle, Pascal Ferré
1INSERM Unit 671, Paris 75006, France.

Tóm tắt

AMP‐activated protein kinase (AMPK) is involved in cellular energy homeostasis. Its functions have been extensively studied in muscles and liver. AMPK stimulates pathways which increase energy production (glucose transport, fatty acid oxidation) and switches off pathways which consume energy (lipogenesis, protein synthesis, gluconeogenesis). This has led to the concept that AMPK has an interesting pharmaceutical potential in situations of insulin resistance and it is indeed the target of existing drugs and hormones which improve insulin sensitivity. Adipose tissue is a key player in energy metabolism through the release of substrates and hormones involved in metabolism and insulin sensitivity. Activation of AMPK in adipose tissue can be achieved through situations such as fasting and exercise. Leptin and adiponectin as well as hypoglycaemic drugs are activators of adipose tissue AMPK. This activation probably involves changes in the AMP/ATP ratio and the upstream kinase LKB1. When activated, AMPK limits fatty acid efflux from adipocytes and favours local fatty acid oxidation. Since fatty acids have a key role in insulin resistance, especially in muscles, activating AMPK in adipose tissue might be found to be beneficial in insulin‐resistant states, particularly as AMPK activation also reduces cytokine secretion in adipocytes.

Từ khóa


Tài liệu tham khảo

10.1016/0026-0495(71)90062-X

10.1074/jbc.273.1.215

10.1152/ajpendo.00144.2005

10.1016/S1043-2760(01)00524-0

10.1074/jbc.C200171200

10.1042/bj3460659

10.1111/j.1432-1033.1995.0558k.x

10.1016/j.bbrc.2005.11.159

10.1074/jbc.M414222200

10.1074/jbc.273.24.14767

10.1038/35007504

10.1073/pnas.98.4.2005

10.1111/j.1432-1033.1990.tb19116.x

10.1006/bbrc.2001.5484

10.1126/science.1123965

10.1074/jbc.M110355200

10.1111/j.1432-1033.1997.00259.x

10.1186/1475-4924-2-28

10.1016/j.cmet.2005.05.009

10.1111/j.1432-1033.1990.tb15295.x

10.1016/S0960-9822(02)01077-1

10.1016/j.ejphar.2005.06.016

10.1111/j.1432-1033.1995.108_c.x

10.1016/S0005-2728(03)00027-6

10.1016/j.cmet.2004.12.003

10.1055/s-2007-978684

10.1016/j.bbrc.2004.05.188

10.1016/S0014-5793(98)00745-5

10.1016/j.bbrc.2004.02.139

10.1016/j.febslet.2004.06.002

10.1161/01.ATV.0000099786.99623.EF

10.1038/415339a

10.1016/S0014-5793(98)01392-1

10.2337/diabetes.51.12.3368

10.1073/pnas.0308258100

10.1073/pnas.97.2.787

10.1074/jbc.M201692200

10.2337/diabetes.52.3.667

10.1046/j.0014-2956.2002.02627.x

10.1016/j.bbrc.2003.12.120

10.1152/ajpendo.00455.2001

10.1042/bj3340177

10.2337/diabetes.49.10.1649

10.1016/j.bbrc.2006.03.010

10.1073/pnas.0308061100

10.1073/pnas.94.9.4637

10.1016/0014-5793(88)80445-9

10.1016/j.febslet.2005.09.078

10.1074/jbc.271.2.611

10.1016/0014-5793(94)01006-4

10.1080/15216540400009968

10.2337/diabetes.53.8.2169

10.1016/S0014-2999(02)01430-9

10.2337/diabetes.53.9.2242

10.1038/oby.2001.15

10.1074/jbc.274.25.17541

10.1074/jbc.271.17.10282

10.1016/j.cmet.2005.06.005

10.1016/j.cub.2003.10.031

10.1016/S0014-5793(96)01209-4

10.2337/diabetes.52.6.1355

10.1038/nm788

10.1042/BJ20031811

10.1007/s00125-004-1436-1

10.1074/jbc.M308484200

10.1172/JCI13505

10.1126/science.1100747