Abstract
Irisin hormone, secreted mainly in skeletal, cardiac muscles, is proteolytically cleaved from the C-terminal moiety and secreted from the fibronectin domain-containing protein 5(FNDC5) receptor. This hormone carries carbohydrate moieties, which are glycosylated, and is a dimeric protein, and released as a hormone of 112 amino acids [1]. The dimerization of this hormone is not affected by glycosylation, although N-glycosylation is necessary for the stabilization of FNDC5 and secretion of irisin [2]. Quantitation of circulating human irisin by Tandem Mass Spectrometry was ∼ 3.6 ng/ml in sedentary individuals [3]. Irisin is secreted mainly in skeletal, cardiac muscles and adipose tissues.
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