Sonic HedgeHog; also known as sonic hedgehog protein; belongs to the hedgehog family. It cannot be detected in adult tissues while can be found in fetal intestine; liver; lung; and kidney. Sonic HedgeHog is a protein that is vital in guding the early embryo. It has been associated as the major inductive signal in patterning of the ventral neural tube; the anterior-posterior limb axis; and the ventral somites. Sonic HedgeHog intercellular signal is essential for a various patterning events during development: signal produced by the notochord that induces ventral cell fate in the neural tube and somites; and the polarizing signal for patterning of the anterior-posterior axis of the developing limb bud. Sonic HedgeHog binds to the patched receptor; which functions in association with smoothened; to activate the transcription of target genes. In the absence of sonic HedgeHog; patched receptor represses the constitutive signaling activity of smoothened. Sonic HedgeHog also regulates another factor; the gli oncogene. Defects in sonic hedgehog can cause microphthalmia isolated with coloboma type 5; triphalangeal thumb-polysyndactyly syndrome and holoprosencephaly type 3.
Sonic Hedgehog Homolog (SHH) belongs to a three-protein family called Hedgehog. The other two family members are Indian Hedgehog (IHH) and Desert Hedgehog (DHH). Hedgehog proteins are key signaling molecules in embryonic development. SHH is expressed in various embryonic tissues and plays critical roles in regulating the patterning of many systems; such as limbs and brain. SHH also plays an important role in adult; including the division of adult stem cells and the development of certain cancers and other diseases. Human SHH is expressed as a 45kDa precursor; and undergoes a series of processing during secretion. After the removal of the signal peptide; a protease within the C-terminal domain catalyzes the cleavage of SHH into a 20 kDa N-terminal signaling domain (SHH-N) and a 25 kDa C-terminal domain (SHH-C). SHH-N has the “all signaling” capability. SHH-N binds to the 12 pass transmembrane protein Patched (Ptc) on cell surface; which releases the repression of the activity of Smoothened (Smo); a G-protein coupled receptor; by Ptc.
VPS10 domain-containing receptor SorCS1, also known as SORCS1 and SORCS, is a single-pass type I membrane protein which belongs to theSORCS family and SORCS1 subfamily. SORCS1 contains fiveBNR repeats and onePKD domain. SorCS1 is a member of the Vps10p-domain receptor family comprised of Sortilin, SorCS1, SorCS2, SorCS3, and SorLA. The common characteristic of these receptors is an N-terminal Vps10p domain, which either represents the only module of the luminal/extracellular moiety or is combined with additional domains. Family members play roles in protein transport and signal transduction. The individual receptors bind and internalize a variety of ligands, such as neuropeptides and trophic factors, and Sortilin and SorLA mediate trans-Golgi network-to-endosome sorting. Their prominent neuronal expression, several of the identified ligands, and results support the notion that members of this receptor family have important functions in neurogenesis, plasticity-related processes, and functional maintenance of the nervous system. Sortilin and SorLA mediate intracellular protein trafficking and sorting. SorCS1 binds platelet-derived growth factor-BB (PDGF-BB) and is expressed in isoforms differing only in their cytoplasmic domains. SorCS1 binds platelet-derived growth factor, a growth factor crucial for pericyte recruitment to the microvasculature, and may thus have a role in expanding or maintaining the islet vasculature.
Sorbitol dehydrogenase, also known as L-iditol 2-dehydrogenase and SORD, is a member of the zinc-containing alcohol dehydrogenase family. SORD exsits in a homotetramer and binds one zinc ion per subunit. SORD is expressed in kidney and epithelial cells of both benign and malignant prostate tissue. SORD can converts sorbitol to fructose and catalyzes the interconversion of polyols and their corresponding ketoses, and together with aldose reductase to make up the sorbitol pathway. SORD is up-regulated by androgens and down-regulated by castration. SORD may play a role in the sperm motility by providing an energetic source for sperm.
Functions as a sorting receptor in the Golgi compartment and as a clearance receptor on the cell surface. Required for protein transport from the Golgi apparatus to the lysosomes by a pathway that is independent of the mannose-6-phosphate receptor (M6PR). Lysosomal proteins bind specifically to the receptor in the Golgi apparatus and the resulting receptor-ligand complex is transported to an acidic prelysosomal compartment where the low pH mediates the dissociation of the complex. The receptor is then recycled back to the Golgi for another round of trafficking through its binding to the retromer. Also required for protein transport from the Golgi apparatus to the endosomes. Promotes neuronal apoptosis by mediating endocytosis of the proapoptotic precursor forms of BDNF (proBDNF) and NGFB (proNGFB). Also acts as a receptor for neurotensin. May promote mineralization of the extracellular matrix during osteogenic differentiation by scavenging extracellular LPL. Probably required in adipocytes for the formation of specialized storage vesicles containing the glucose transporter SLC2A4/GLUT4 (GLUT4 storage vesicles, or GSVs). These vesicles provide a stable pool of SLC2A4 and confer increased responsiveness to insulin. May also mediate transport from the endoplasmic reticulum to the Golgi.
Sclerostin, also known as SOST, is a member of the Cerberus/DAN family of BMP antagonists. SOST is asecreted glycoprotein with a C-terminal cysteine knot-like (CTCK) domain. It shows sequence similarity to the DAN (differential screening-selected gene aberrative in neuroblastoma) family of bone morphogenetic protein (BMP) antagonists. SOST is produced by the osteocyte and has anti-anabolic effects on bone formation. It is a negative regulator of bone growth that acts through inhibition of Wnt signaling and bone formation.
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