FSTL1 Human

FSTL1 comprises a secretion signal, a Follistatin- and a Kazal-like domain, two EF-hand domains, and a von Willebrand factor type C domain . The human FSTL1 protein sequence (Genbank: Q12841) is highly similar to the mouse sequence (Genbank Q62356), with a high degree of similarity in the remaining 272 amino acids .

FSTL1 is involved in multiple signaling pathways and biological processes, including vascularization and regulation of the immune response . It displays expression changes during development and disease, such as cardiovascular disease, cancer, and arthritis . The cardioprotective role of FSTL1 has been intensively studied, though its mechanism of action remains elusive .

FSTL1 binds to various receptors, including DIP2A, TLR4, and BMP receptors, but other molecular partners likely exist . The glycosylation state of FSTL1 is a determinant of its biological activity, with the glycosylated form promoting proliferation in cardiomyocytes and the non-glycosylated form working anti-apoptotic . Additionally, the glycosylation state shows differences between species and tissues, which might underlie the differences observed in in vitro studies .

FSTL1 has been reported to be upregulated in the sera of patients with various cardiovascular diseases (CVDs) . It is associated with CVD and predicts poor outcomes . Animal studies have shown that FSTL1 has a protective effect in various models of heart disease, including inhibiting inflammation, preventing remodeling and fibrosis, and promoting angiogenesis and hypertrophy .

Recombinant human FSTL1 is used in research to study its biological functions and potential therapeutic applications. It is produced using recombinant DNA technology, which allows for the production of large quantities of the protein with high purity and consistency .