Adiponectin

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Adiponectin, C1Q and collagen domain containing
PBB Protein ADIPOQ image.jpg
PDB rendering based on 1c28.
Identifiers
Symbol(s) ADIPOQ; ACDC; ACRP30; APM-1; APM1; GBP28; adiponectin
External IDs OMIM: 605441 MGI106675 Homologene3525
RNA expression pattern

PBB GE ADIPOQ 207175 at tn.png

More reference expression data

Orthologs
Human Mouse
Entrez 9370 11450
Ensembl ENSG00000181092 ENSMUSG00000022878
Uniprot Q15848 Q6GTX4
Refseq NM_004797 (mRNA)
NP_004788 (protein)
NM_009605 (mRNA)
NP_033735 (protein)
Location Chr 3: 188.04 - 188.06 Mb Chr 16: 23.06 - 23.07 Mb
Pubmed search [1] [2]
adiponectin receptor 1
Identifiers
Symbol ADIPOR1
Entrez 51094
HUGO 24040
OMIM 607945
RefSeq NM_015999
UniProt Q96A54
Other data
Locus Chr. 1 q32.1
adiponectin receptor 2
Identifiers
Symbol ADIPOR2
Entrez 79602
HUGO 24041
OMIM 607946
RefSeq NM_024551
UniProt Q86V24
Other data
Locus Chr. 12 p13

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Editor-In-Chief: C. Michael Gibson, M.S., M.D. [3] Phone:617-632-7753



Adiponectin (also referred to as Acrp30, apM1) is a protein hormone that modulates a number of metabolic processes, including glucose regulation and fatty acid catabolism. Adiponectin is exclusively secreted from adipose tissue into the bloodstream and is very abundant in plasma relative to many hormones. Levels of the hormone are inversely correlated with body fat percentage. The hormone plays a role in the suppression of the metabolic derangements that may result in type 2 diabetes, obesity, atherosclerosis and non-alcoholic fatty liver disease (NAFLD).

Research history

Adiponectin was first characterised in mice as a transcript overexpressed in preadipocytes (precursors of fat cells) differentiating into adipocytes. The human homologue was identified as the most abundant transcript in adipose tissue. Contrary to expectations, despite being produced in adipose tissue, adiponectin was found to be decreased in obesity. This downregulation has not been fully explained. The gene was localised to chromosome 3p27, a region highlighted as affecting genetic susceptibility to type 2 diabetes and obesity. Supplementation by differing forms of adiponectin were able to improve insulin control, blood glucose and triglyceride levels in mouse models.

The gene was investigated for variants that predispose to type 2 diabetes. Several single nucleotide polymorphisms in the coding region and surrounding sequence were identified from several different populations, with varying prevalences, degrees of association and strength of effect on type 2 diabetes.

Structure and function

Adiponectin is a 244-amino-acid-long polypeptide. There are four distinct regions of adiponectin. The first is a short signal squence that targets the hormone for secretion outside the cell; next is a short region that varies between species; the third is a 65-amino acid region with similarity to collagenous proteins; the last is a globular domain. Overall this gene shows similarity to the complement 1Q factors. However, when the 3-dimensional structure of the globular region was determined, a striking similarity to TNFα was observed, despite unrelated protein sequences.

Adiponectin is secreted into the bloodsteam where it accounts for approximately 0.01% of all plasma protein at around 5-10 μg/mL. Plasma concentrations reveal a sexual dimorphism, with females having higher levels than males. Levels of adiponectin are reduced in diabetics compared to non-diabetics. Weight reduction significantly increases circulating levels.

Adiponectin automatically self-associates into larger structures. Initially, three adiponectin molecules bind together to form a homotrimer. The trimers continue to self-associate and form hexamers or dodecamers. Like the plasma concentration, the relative levels of the higher-order structures are sexually dimorphic, where females have increased proportions of the high-molecular weight forms. Questions remain about what the physiologically active forms of the protein are and how they carry out their action.

Adiponectin binds to a number of receptors. So far, two receptors have been identified, with homology to G protein-coupled receptors. These have distinct tissue specificities within the body and have different affinities to the various forms of adiponectin. The receptors affect the downstream target AMP kinase, an important cellular metabolic rate control point. Expression of the receptors are correlated with insulin levels, as well as reduced in mouse models of diabetes, particularly in skeletal muscle and adipose tissue.

Adiponectin exerts some of its weight reduction effects via the brain. This is similar to the action of leptin, but the two hormones perform complementary actions, and can have additive effects.

Metabolic effects

Adiponectin affects:

Pharmaceutical therapy

Because adiponectin is a novel hormone, no therapy has yet been developed with adiponectin and it may be some years before clinical trials commence. One obvious pharmaceutical treatment would be the administration of adiponectin; in mouse models such administration has shown positive effects. Problems to be overcome prior to human administration include establishing what the biologically active molecule is, what role post-translational modifications have upon the function and associated difficulties in generating biologically active molecules on a large scale. However, this remains a promising area of research for clinical therapy in diseases such as obesity, type 2 diabetes and fatty liver disease.

Further reading

  • Ukkola O, Santaniemi M (2003). "Adiponectin: a link between excess adiposity and associated comorbidities?". J. Mol. Med. 80 (11): 696-702. doi:10.1007/s00109-002-0378-7. PMID 12436346.
  • Díez JJ, Iglesias P (2003). "The role of the novel adipocyte-derived hormone adiponectin in human disease.". Eur. J. Endocrinol. 148 (3): 293-300. PMID 12611609.
  • Vasseur F, Leprêtre F, Lacquemant C, Froguel P (2003). "The genetics of adiponectin.". Curr. Diab. Rep. 3 (2): 151-8. PMID 12728641.
  • Matsuzawa Y, Funahashi T, Kihara S, Shimomura I (2004). "Adiponectin and metabolic syndrome.". Arterioscler. Thromb. Vasc. Biol. 24 (1): 29-33. doi:10.1161/01.ATV.0000099786.99623.EF. PMID 14551151.
  • Nedvídková J, Smitka K, Kopský V, Hainer V (2006). "Adiponectin, an adipocyte-derived protein.". Physiological research / Academia Scientiarum Bohemoslovaca 54 (2): 133-40. PMID 15544426.
  • Hug C, Lodish HF (2005). "The role of the adipocyte hormone adiponectin in cardiovascular disease.". Current opinion in pharmacology 5 (2): 129-34. doi:10.1016/j.coph.2005.01.001. PMID 15780820.
  • Hara K, Yamauchi T, Kadowaki T (2005). "Adiponectin: an adipokine linking adipocytes and type 2 diabetes in humans.". Curr. Diab. Rep. 5 (2): 136-40. PMID 15794918.
  • Vasseur F, Meyre D, Froguel P (2007). "Adiponectin, type 2 diabetes and the metabolic syndrome: lessons from human genetic studies.". Expert reviews in molecular medicine 8 (27): 1-12. doi:10.1017/S1462399406000147. PMID 17112391.
  • Menzaghi C, Trischitta V, Doria A (2007). "Genetic influences of adiponectin on insulin resistance, type 2 diabetes, and cardiovascular disease.". Diabetes 56 (5): 1198-209. doi:10.2337/db06-0506. PMID 17303804.
  • Lara-Castro C, Fu Y, Chung BH, Garvey WT (2007). "Adiponectin and the metabolic syndrome: mechanisms mediating risk for metabolic and cardiovascular disease.". Curr. Opin. Lipidol. 18 (3): 263-70. doi:10.1097/MOL.0b013e32814a645f. PMID 17495599.
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