Adiponectin is a protein hormone that modulates a number of metabolic processes, including glucose regulation and fatty acid catabolism.[3] Adiponectin is exclusively secreted from adipose tissue into the bloodstream and is very abundant inplasma relative to many hormones. Levels of the hormone are inversely correlated with body fat percentage in adults,[4] while the association in infants and young children is more unclear. The hormone plays a role in the suppression of the metabolic derangements that may result in type 2 diabetes,[4] obesity, atherosclerosis,[3] non-alcoholic fatty liver disease (NAFLD) and an independent risk factor for metabolic syndrome.[5]

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.[6]

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 exerts some of its weight reduction effects via the brain. This is similar to the action of leptin,[7] but the two hormones perform complementary actions, and can have additive effects.

  Maeda K, Okubo K, Shimomura I, Funahashi T, Matsuzawa Y, Matsubara K (April 1996). "cDNA cloning and expression of a novel adipose specific collagen-like factor, apM1 (AdiPose Most abundant Gene transcript 1)". Biochem. Biophys. Res. Commun. 221 (2): 286–9. doi:10.1006/bbrc.1996.0587. PMID 8619847.  
^ Shapiro L, Scherer PE (March 1998). "The crystal structure of a complement-1q family protein suggests an evolutionary link to tumor necrosis factor". Curr. Biol. 8 (6): 335–8. doi:10.1016/S0960-9822(98)70133-2. PMID 9512423.  
^ a b c d e Díez JJ, Iglesias P (March 2003). "The role of the novel adipocyte-derived hormone adiponectin in human disease". Eur. J. Endocrinol. 148 (3): 293–300. doi:10.1530/eje.0.1480293. PMID 12611609.  
^ a b c Ukkola O, Santaniemi M (November 2002). "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.  
^ a b Renaldi O, Pramono B, Sinorita H, Purnomo LB, Asdie RH, Asdie AH (January 2009). "Hypoadiponectinemia: a risk factor for metabolic syndrome". Acta Med Indones 41 (1): 20–4. doi:10.1267/science.040579197 (inactive 2009-03-05). PMID 19258676.  
^ Coppola A, Marfella R, Coppola L, Tagliamonte E, Fontana D, Liguori E, Cirillo T, Cafiero M, Natale S, Astarita C (March 2008). "Effect of weight loss on coronary circulation and adiponectin levels in obese women". Int. J. Cardiol.. doi:10.1016/j.ijcard.2007.12.087. PMID 18378021.  
^ a b c d e f g Nedvídková J, Smitka K, Kopský V, Hainer V (2005). "Adiponectin, an adipocyte-derived protein". Physiol Res 54 (2): 133–40. PMID 15544426. http://www.biomed.cas.cz/physiolres/pdf/54/54_133.pdf. 

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