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标题:Role of leptin and adiponectin in insulin resistance.
时间:2019-11-19 23:46:57
DOI:10.1016/j.cca.2012.12.007
PMID:23266767
作者:Yadav, Amita; Kataria, Megha A.; Saini, Vandana
关键词:Insulin resistance; NF-kappa B; Inflammation; Adipose tissue; Adipokine
出版源: Clinica Chimica Acta ,417 :80-84
摘要:Adipose tissue is a major source of energy for the human body. It is also a source of major adipocytokines adiponectin and leptin. Insulin resistance is a condition in which insulin action is impaired in adipose tissue and is more strongly linked to intra-abdominal fat than to fat in other depots. The expression of adiponectin decreases with increase in the adiposity. Adiponectin mediates insulin-sensitizing effect through binding to its receptors AdipoR1 and AdipoR2, leading to activation of adenosine monophosphate dependent kinase (AMPK), PPAR-alpha, and presumably other yet-unknown signalling pathways. Weight loss significantly elevates plasma adiponectin levels. Reduction of adiponectin has been associated with insulin resistance, dyslipidemia, and atherosclerosis in humans. The other major adipokine is leptin. Leptin levels increase in obesity and subcutaneous fat has been a major determinant of circulating leptin levels. The leptin signal is transmitted by the Janus kinase, signal transducer and activator of transcription (JAK-STAT) pathway. The net action of leptin is to inhibit appetite, stimulate thermogenesis, enhance fatty acid oxidation, decrease glucose, and reduce body weight and fat. (c) 2012 Elsevier B.V. All rights reserved.
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目录:
  • Role of leptin and adiponectin in insulin resistance
    • 1. Introduction
      • 1.1. Adipose tissue
    • 2. Adiponectin
      • 2.1. Protein structure of adiponectin
      • 2.2. Adiponectin receptors
      • 2.3. Mechanism of action of adiponectin
        • 2.3.1. Insulin-sensitizing actions
    • 3. Leptin
      • 3.1. Structure of leptin
      • 3.2. Receptor and site of action
      • 3.3. Mechanism of action
    • 4. Future trends for adiponectin and leptin
      • 4.1. Adiponectin
      • 4.2. Leptin
    • 5. Conclusions
    • 6. Limitation
    • References

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