Insulin is a secreted peptide hormone that elicits metabolic effects such as increases in glucose uptake and glycogen synthesis leading to a decrease in blood glucose concentration. Insulin is first formed as a precursor molecule, preproinsulin, which is later cleaved to proinsulin and finally to the mature insulin hormone. Insulin-like peptides (INSL proteins), also designated Relaxinlike factors, are members of the insulin family, which regulate cell growth, metabolism and tissue-specific functions. INSL1-7 are mostly secreted proteins that are expressed mainly in testis, placenta, uterus or prenatal tissues. INSL4 is a 139 amino acid secreted protein expressed in the placenta, uterus and in fetal perichondrium. It may play an important role in the regulation of bone formation and in trophoblast development.
Early placenta insulin-like peptide; early placenta insulin-like peptide (EPIL); Early placenta insulin-like peptide A chain; Early placenta insulin-like peptide B chain; EPIL; insulin-like 4 (placenta); Insulin-like peptide 4; Placentin