Sclerostin / SOST抗体

Sclerostin, also known as SOST, is a glycoprotein with a signal peptide for secretion and a C-terminal cysteine knot-like (CTCK) domain and belongs to the Cerberus/DAN family of bone morphogenetic protein (BMP) antagonists including Dan, Cerberus, Gremlin, PRDC, and Caronte. Sclerostin is expressed at significant levels in bone, cartilage, kidney, and liver, and was originally identified as an important regulator of bone remodeling, homeostasis, and links bone resorption and bone apposition. It negatively regulates the formation of bone by repressing the differentiation and/or function of osteoblasts induced by BMPs. It has been shown that Sclerostin binds BMP-5, -6, and -7 with high affinity and BMP-2 and -4 with low affinity. Recent studies have revealed that Sclerostin inhibits the bone growth probably by binding to the extracellular domain of the Wnt coreceptors LRP5 and LRP6 and disrupts the Wnt signaling. Loss-of-function mutations of Sclerostin are associated with sclerosteosis which is an autosomal-recessive bone dysplasia characterized by progressive skeletal overgrowth, and reduced sclerostin expression results in a milder form of the disorder called van Buchem disease.
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