Protein Related to DAN and Cerberus Is a Bone Morphogenetic Protein Antagonist That Participates in Ovarian Paracrine Regulation

Protein related to DAN and cerberus is a bone morphogenetic protein antagonist that participates in ovarian paracrine regulation.

Bone morphogenetic proteins (BMPs) are important for body patterning and morphogenesis, whereas several BMP antagonists regulate the functions of BMPs during embryonic development and tissue differentiation. Protein related to DAN and cerberus (PRDC) is a secreted protein with a cystine knot structure identified by gene trapping in embryonic stem cells. Although PRDC shows sequence homology wit...

Protein Related to DAN and Cerberus (PRDC) is a BMP Antagonist that Participates in Ovarian Paracrine Regulation

Structure of protein related to Dan and Cerberus: insights into the mechanism of bone morphogenetic protein antagonism.

The bone morphogenetic proteins (BMPs) are secreted ligands largely known for their functional roles in embryogenesis and tissue development. A number of structurally diverse extracellular antagonists inhibit BMP ligands to regulate signaling. The differential screening-selected gene aberrative in neuroblastoma (DAN) family of antagonists represents the largest group of BMP inhibitors; however,...

DAN is a secreted glycoprotein related to Xenopus cerberus

We report that DAN, a potential cell cycle regulator and tumour suppressor, is a secreted glycoprotein related to Xenopus cerberus. DAN, cerberus, its mouse relative Cer-1/cer-l/Cerberus-like/Cerr1, and the recently described factor DRM/Gremlin, appear to be members of the cystine knot superfamily, which includes TGFbetas and BMPs. Like cerberus and mCer-1, DAN-induced cement glands as well as ...

Inhibin is an antagonist of bone morphogenetic protein signaling.

Inhibins are endogenous antagonists of activin signaling, long recognized as important regulators of gonadal function and pituitary FSH release. Inhibin, in concert with its co-receptor, betaglycan, can compete with activin for binding to type II activin receptors and, thus, prevent activin signaling. Because bone morphogenetic proteins (BMPs) also utilize type II activin receptors, we hypothes...