FNDC5 was first characterized in 2002 as a transmembrane protein expressed in various tissues, including skeletal muscle, heart, and brain . The protein contains a fibronectin type III domain, which is a common structural motif involved in cell adhesion and receptor binding. The human FNDC5 gene is located on chromosome 1 and is known to produce multiple transcript variants through alternative splicing .
The most intriguing aspect of FNDC5 is its role as the precursor to irisin. During physical exercise, the ectodomain of FNDC5 is cleaved to release irisin, a 112-amino acid hormone . Irisin was named after the Greek messenger goddess Iris, reflecting its role in conveying signals within the body . This hormone has been shown to induce the browning of white adipose tissue, a process that increases energy expenditure and has potential implications for combating obesity and metabolic disorders .
Research on FNDC5 and irisin has expanded rapidly since the discovery of irisin in 2012. Studies have explored the hormone’s effects on various physiological processes:
Despite the promising findings, the study of FNDC5 and irisin is not without challenges. Some researchers have questioned the accuracy of assays used to measure irisin levels in plasma, leading to discrepancies in reported data . Additionally, while animal studies have shown significant effects of irisin on adipose tissue and metabolism, similar results in humans have been less consistent .
Human recombinant FNDC5 is produced through recombinant DNA technology, allowing for the study of this protein in various experimental settings. This recombinant form is crucial for investigating the detailed mechanisms of FNDC5 and irisin, as well as their potential therapeutic applications.