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Review
. 2021 Apr 2;13(4):1180.
doi: 10.3390/nu13041180.

Adiponectin: Structure, Physiological Functions, Role in Diseases, and Effects of Nutrition

Kayvan Khoramipour  1 , Karim Chamari  2 , Amirhosein Ahmadi Hekmatikar  3 , Amirhosein Ziyaiyan  4 , Shima Taherkhani  5 , Nihal M Elguindy  6 , Nicola Luigi Bragazzi  7
Affiliations
Review

Adiponectin: Structure, Physiological Functions, Role in Diseases, and Effects of Nutrition

Kayvan Khoramipour et al. Nutrients. .

Abstract

Adiponectin (a protein consisting of 244 amino acids and characterized by a molecular weight of 28 kDa) is a cytokine that is secreted from adipose tissues (adipokine). Available evidence suggests that adiponectin is involved in a variety of physiological functions, molecular and cellular events, including lipid metabolism, energy regulation, immune response and inflammation, and insulin sensitivity. It has a protective effect on neurons and neural stem cells. Adiponectin levels have been reported to be negatively correlated with cancer, cardiovascular disease, and diabetes, and shown to be affected (i.e., significantly increased) by proper healthy nutrition. The present review comprehensively overviews the role of adiponectin in a range of diseases, showing that it can be used as a biomarker for diagnosing these disorders as well as a target for monitoring the effectiveness of preventive and treatment interventions.

Keywords: adipokine; adiponectin; adipose tissues; biomarker; cancer; disease; nutrition.

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Conflict of interest statement

The authors declare no conflict of interest.

Figures

Figure 1
Figure 1
Three structural types of adiponectin with different molecular weight (trimer, hexamer, and multimer). A full-length adiponectin (~30 kDa) consists of a globular domain, a collagenous domain, a species-specific domain, and a signal peptide. Oligomerization facilitates the formation of the trimer, hexamer, and high-molecular weight (HMW) adiponectin. Full-length adiponectin can undergo proteolytic cleavage, whose proteolytic fragment corresponds to the globular adiponectin. AdipoR1 has a greater affinity for the globular form, whereas AdipoR2 has a moderate affinity for both globular and full-length forms.
Figure 2
Figure 2
Adiponectin and its receptors and schematic representation of adiponectin-induced signaling pathway. Adiponectin interacts with the C-terminus (carboxyl end) of receptors, which interacts with the protein-adaptive protein (APPL1) in most of the seven regions with its intramuscular N terminus. T-cadherin is a receptor with a high affinity for high molecular weight adiponectin (HMW) isoforms, leading to a complex cascade of events.
Figure 3
Figure 3
The proposed role of adiponectin in kidney pathophysiology [44].
See this image and copyright information in PMC

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