author(s)
Amir Amin Sheikh, Aditya Mishra, Rouf Rashid Dar, Neeti Lakhani, Rakshanda Bhagat, Pooja Dogra and Uttarani Maibam

abstract
Adiponectin, a hormone product of APM1 gene, composed of 244 amino acids with a molecular weight of 30 kDa, performs a very important role in vascular physiology thus prevents from atherosclerosis and other cardiovascular diseases. Its structure is divided into three domains: the N-terminal domain, colla¬gen-like domain and the globular domain of the C-ter¬minal region. Adiponectin is largely secreted by adipocytes, also secreted from cardiomyocytes, hepatocytes and placenta but in lower concentrations. Secretion of adiponectin is strictly controlled by the retention of protein thiols, so that two molecular endoplasmic reticulum chaperones play a critical role: 44 kDa ER proteins (endoplasmic reticulum protein 44, ERp44) and Ero1-La (endoplasmic reticulum oxidoreductin 1-like alpha), both induced during adipogenesis. ERp44 forms the disulphide bond with adiponectin whereas Erol-La weakens the disulphide bond, responsible for its release. Atheroprotection is con¬ferred by different actions of this protein, including anti-in-flammatory effects, stimulation of nitric oxide production, mitigation of pro-atherogenic mediators and coronary plaque vulnerability modulation.