Hypoxia up-regulated protein 1, also known as 150 kDa oxygen-regulated protein, 170 kDa glucose-regulated protein, ORP-150, GRP-170 and HYOU1, is a member of theheat shock protein 70 family. Seven members from four different heat shock protein (HSP) families were identified including HYOU1 (ORP150), HSPC1 (HSP86), HSPA5 (Bip), HSPD1 (HSP60), and several isoforms of the two testis-specific HSP70 chaperones HSPA2 and HSPA1L. HYOU1 is highly expressed in tissues that contain well-developed endoplasmic reticulum and synthesize large amounts of secretory proteins. It is highly expressed in liver and pancreas. HYOU1 is also expressed in macrophages within aortic atherosclerotic plaques, and in breast cancers. HYOU1 has a pivotal role in cytoprotective cellular mechanisms triggered by oxygen deprivation. It may play a role as a molecular chaperone and participate in protein folding. Suppression of HYOU1 is associated with accelerated apoptosis. It is suggested to have an important cytoprotective role in hypoxia-induced cellular perturbation. This protein has been shown to be up-regulated in tumors, especially in breast tumors, and thus it is associated with tumor invasiveness.
Oncostatin-M specific receptor subunit beta also known as the oncostatin M receptor (OSMR) and Interleukin-31 receptor subunit beta (IL-31RB), is one of the receptor proteins for oncostatin M. OSMR is a member of the type I cytokine receptor family. IL-31RB/OSMR heterodimerizes with interleukin 6 signal transducer to form the type II oncostatin M receptor and with interleukin 31 receptor A to form the interleukin 31 receptor, and thus transduces oncostatin M and interleukin 31 induced signaling events. Mutations in IL-31RB/OSMR have been associated with familial primary localized cutaneous amyloidosis. Defects in IL-31RB/OSMR are the cause of amyloidosis primary localized cutaneous type 1 (PLCA1), also known as familial lichen amyloidosis or familial cutaneous lichen amyloidosis. PLCA1 is a hereditary primary amyloidosis characterized by localized cutaneous amyloid deposition. This condition usually presents with itching (especially on the lower legs) and visible changes of skin hyperpigmentation and thickening (lichenification) that may be exacerbated by chronic scratching and rubbing. The amyloid deposits probably reflect a combination of degenerate keratin filaments, serum amyloid P component, and deposition of immunoglobulins.
Oncostatin-M-Specific Receptor Subunit β (OSMRβ) is a 150 - 180 kDa member of the IL-6 receptor family. OSMRβ associates with gp130 to form the type II OSM receptor, the receptor is responsive to OSM. Gp130 subunit is shared by other IL-6 family cytokine receptors, and OSMRβ associates with gp130-like receptor (GPL) to form a receptor complex responsive to IL-31. The human OSMRβ cDNA encodes a 979 amino acid (aa) precursor, the precursor includes a 27 aa signal sequence, a 712 aa extracellular domain (ECD), a 22 aatransmembrane segment, and a 218 aa cytoplasmic domain. The ECD contains one partial and one complete hematopoietin domain, an Ig-like domain, and three Fibronectin type-III domains.
Osteocalcin, also known as Bone gamma-Carboxyglutamic Acid Protein, is a secreted protein whose expression is restricted to cells of the osteoblast lineage. It has been frequently used as a marker for osteoblast lineage cells.
Osteocrin is a secreted protein which is primarily expressed in bone and muscle. It is synthesized as a proprotein that undergoes proteolytic processing to generate a mature 50 amino acid C-terminal active peptide.Human Osteocrin proprotein shares 77% and 78% amino acid sequence identity with the rat and mouse protein, respectively. It appears to modulate osteoblastic differentiation. It could also function as an autocrine and paracrine factor linked to glucose metabolism in skeletal muscle.
Osteomodulin (OMD), also known as Osteoadherin (OSAD), Keratan sulfate proteoglycan osteomodulin, KSPG osteomodulin, and SLRR2C, is a secreted protein which belongs to the small leucine-rich proteoglycan (SLRP) family and Class II subfamily. SLRP family proteins are normally found in extracellular matrices, but Osteomodulin is the only member restricted to mineralized tissues. Osteomodulin is primarily expressed by osteoblasts and might have a role in regulation of mineralization. In bone OSAD has been localized in primary spongiosa within the bovine fetal rib growth plate. Moreover, in situ hybridization has shown expression of OSAD in osteoblasts close to the cartilage and bone border in the growth plate of rat femur. OSAD may play an important role during tooth development and biomineralization of dentin. Osteomodulin is a cell binding keratan sulfate proteoglycan which was recently isolated from mineralized bovine bone and subsequently cloned and sequenced. Osteomodulin may be implicated in biomineralization processes. It has a function in binding of osteoblasts via the alpha (V) beta (3)-integrin. It is likely that Osteomodulin is an osteoblast maturation marker that is induced by osteoclast activity. Osteomodulin is also an early marker for terminally differentiated matrix producing osteoblasts.
Secreted Protein Acidic and Rich in Cysteine (SPARC) is a secreted, evolutionarily conserved collagen-binding glycoprotein and belongs to the SPARC family. SPARC has 286 amino acids and contains an EF-hand in C-termina domain, a follistatin-like domain with Kazal-like sequences. There are two calcium binding sites, one binds 5 - 8 Ca2+ with a low affinity and other on an EF-hand loop that binds a Ca2+ ion with a high affinity. It is highly expressed in tissues undergoing morphogenesis, remodeling and wound repair. SPARC regulate cell growth through interactions with the extracellular matrix (ECM) and cytokines. SPARC bind to numerous proteins of the ECM, affect ECM protein expression, influence cellular adhesion and migration, and modulate growth factor-induced cell proliferation and angiogenesis. SPARC also binds several types of collagen, albumin, thrombospondin, PDGF and cell membranes.
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