GPNMB belongs to the PMEL / NMB family, also known as Osteoactivin and Hematopoietic growth factor-inducible neurokinin 1 ( HGFIN ), is a transmembrane glycoprotein that is expressed in numerous cells, including osteoclasts, macrophages, dendritic cells, and tumor cells. It is suggested to influence osteoblast maturation, cell adhesion, and migration. GPNMB protein acts as a downstream mediator of BMP-2 effects on osteoblast differentiation and function. GPNMB participates in bone mineralization and functions as a negative regulator of inflammation in macrophages. Osteoactivin is expressed at high levels in normal and inflammatory liver macrophages suggesting a significant role in acute liver injury. The early-phase upregulation of Osteoactivin expression in the tubular epithelium in response to renal injury might play a role in triggering renal interstitial fibrosis via activation of matrix metalloproteinase expression and collagen remodeling in rats. Osteoactivin is a protein that is expressed in aggressive human breast cancers and is capable of promoting breast cancer metastasis to bone.
GPR114 belongs to the G-protein coupled receptor 2 family. Members of this family share a common molecular architecture which consists of seven transmembrane domains, three extracellular loops, three intracellular loops, an amino-terminal extracellular domain and an intracellular carboxyl terminus. It is thought that light acts as the activating stimulus of a G-protein-coupled receptor (GPCR). GPCRs are expected to have molecular function (G-protein coupled receptor activity) and to localize in various compartments (endoplasmic reticulum membrane, plasma membrane, integral to membrane). Family B of the GPCRs is a small but structurally and functionally diverse group of proteins that includes receptors for polypeptide hormones, molecules thought to mediate intercellular interactions at the plasma membrane and a group of Drosophila proteins that regulate stress responses and longevity. GPR114 contains 1 GPS domain. GPR114 gene has been proposed to participate in processes (G-protein coupled receptor protein signaling pathway, neuropeptide signaling pathway).
GPR37 (cathepsin Z) is an orphan receptor which belongs to the G-protein coupled receptor 1 family. G protein coupled receptors is a large protein family comprised by transmembrane receptors that sense molecules outside the cell and activate inside signal transduction pathways and, ultimately, cellular responses. They only exists in eukaryotes, including yeast, choanoflagellates, and animals. These receptors are binded and activated by light-sensitive compounds, odors, pheromones, hormones, and neurotransmitters. These ligands vary in size from small molecules to peptides to large proteins. G protein-coupled receptors are involved in many diseases, and are also the target of approximately 40% of all modern medicinal drugs. GPR37 is expressed in brain and spinal cord, and at lower levels in testis, placenta and liver, but no detectable expression observed in any other tissue. GPR37 may have a unique functional role in the central nervous system.
The cluster of differentiation (CD) system is commonly used as cell markers in immunophynotyping. Different kinds of cells in the immune system can be identified through the surface CD molecules which associating with the immune function of the cell. There are more than 320 CD unique clusters and subclusters have been identified. Some of the CD molecules serve as receptors or ligands important to the cell through initiating a signal cascade which then alter the behavior of the cell. Some CD proteins do not take part in cell signal process but have other functions such as cell adhesion. Cluster of differentiation 1 (CD1) is a member of CD system. It's a family of glycoproteins expressed on the surface of various human antigen- presenting cells which are implicated in the presentation of lipid antigens to T-cells. Due to the different lipid anchoring, the CD1 family is classified into two groups: group1 (CD1a-c) and group2 (CD1d). CD1d with lipid antigens activate NK T-cells which rapidly produce Th1 and Th2 cytokines after been activated.
Grancalcin (GCA) is a cytoplasmic granule membrane protein that contains 4 EF-hand domains. GCA is calcium-binding protein and particularly abundant in human neutrophils. GCA is highly expressed in bone marrow; and it can be detected in neutrophils and macrophages. Calcium-binding protein GCA cooperates with SRI and LCP1; so it may play a role in the adhesion of neutrophils to fibronectin. GCA also may play a role in the formation of focal adhesions.
Grancalcin (GCA) is a member of the penta EF hand subfamily which includes sorcin; calpain and ALG2. Grancalcin is highly expressed bone marrow and also can detected in neutrophils and macrophages. Grancalcin interacts with L-plastin which known to have actin bundling activity. It indicates that Grancalcin may play an important role in the adhesion of neutrophils to fibronectin. Furthermore; Grancalcin localization is dependent upon calcium and magnesium. It associates with both the granule and membrane fractions; which suggested a role for grancalcin in granule-membrane fusion and degranulation.
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