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.
Secreted Phosphoprotein 1 (SPP1) is a secreted multifunctional glycoprotein. Its putative functions include roles in bone metabolism, immune regulation, wound healing, cell survival, and tumor progression. Based on gene structure and chromosomal location, SPP1 is a member of the small integrin-binding ligand N-linked glycoprotein (SIBLING) family that also includes bone sialoprotein (BSP), dentin matrix protein 1 (DMP1), dentin sialophosphoprotein (DSPP), enamelin (ENAM), and matrix extracellular phosphoglycoprotein (MEPE). SPP1 is expressed in bone, although it is also expressed in other tissues. SPP1 acts as a cytokine that is involved in enhancing production of interferon-gamma and interleukin-12 and reducing production of interleukin-10. It is essential in the pathway that leads to type I immunity. Osteopontin has been implicated as an important factor in bone remodeling. Specifically, research suggests it plays a role in anchoring osteoclasts to the mineral matrix of bones. The fact that SPP1 interacts with multiple cell surface receptors which are ubiquitously expressed makes it an active player in many physiological and pathological processes including wound healing, bone turnover, tumorigenesis, inflammation and ischemia. Therefore, manipulation of plasma Osteopontin levels may be useful in the treatment of autoimmune diseases, cancer metastasis, osteoporosis and some forms of stress.
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