Receptor-type tyrosine-protein phosphatase-like N (PTPRN) belongs to the protein-tyrosine phosphatase family and receptor class 8 subfamily. PTPRN contains 1 tyrosine-protein phosphatase domain, is expressed in neuroendocrine cells only. PTPs are known to be signaling molecules that regulate a variety of cellular processes including cell growth, differentiation, mitotic cycle, and oncogenic transformation. It implicated in neuroendocrine secretory processes. It may be involved in processes specific for neurosecretory granules, such as their biogenesis, trafficking or regulated exocytosis or may have a general role in neuroendocrine functions. It seems to lack intrinsic enzyme activity, may play a role in the regulation of secretory granules via its interaction with SNTB2. This PTP was found to be an autoantigen that is reactive with insulin-dependent diabetes mellitus (IDDM) patient sera, and thus may be a potential target of autoimmunity in diabetes mellitus.
Receptor-type tyrosine-protein phosphatase-like N (PTPRN) belongs to the protein-tyrosine phosphatase family and receptor class 8 subfamily. PTPRN contains 1 tyrosine-protein phosphatase domain; is expressed in neuroendocrine cells only. PTPs are known to be signaling molecules that regulate a variety of cellular processes including cell growth; differentiation; mitotic cycle; and oncogenic transformation. It implicated in neuroendocrine secretory processes. It may be involved in processes specific for neurosecretory granules; such as their biogenesis; trafficking or regulated exocytosis or may have a general role in neuroendocrine functions. It seems to lack intrinsic enzyme activity; may play a role in the regulation of secretory granules via its interaction with SNTB2. This PTP was found to be an autoantigen that is reactive with insulin-dependent diabetes mellitus (IDDM) patient sera; and thus may be a potential target of autoimmunity in diabetes mellitus.
Intercellular adhesion molecule-1 (ICAM-1, or CD54) is a 90 kDa member of the immunoglobulin (Ig) superfamily and is critical for the firm arrest and transmigration of leukocytes out of blood vessels and into tissues. ICAM-1 is constitutively present on endothelial cells, but its expression is increased by proinflammatory cytokines. The endothelial expression of ICAM-1 is increased in atherosclerotic and transplant-associated atherosclerotic tissue and in animal models of atherosclerosis. Additionally, ICAM-1 has been implicated in the progression of autoimmune diseases. ICAM-1 is a ligand for LFA-1(integrin). When activated, leukocytes bind to endothelial cells via ICAM-1/LFA-1 interaction and then transmigrate into tissues. Presence with heavy glycosylation and other structural characteristics, ICAM-1 possesses binding sites for a number of immune-associated ligands and serves as the binding site for entry of the major group of human Rhinovirus (HRV) into various cell types. ICAM-1 also becomes known for its affinity for Plasmodium falciparum-infected erythrocytes (PFIE), providing more of a role in infectious disease. Previous studies have shown that ICAM-1 is involved in inflammatory reactions and that a defect in ICAM-1 gene inhibits allergic contact hypersensitivity.
Inter-Cellular Adhesion Molecule 1 (ICAM1) is a type of intercellular adhesion molecule continuously present in low concentrations in the membranes of leukocytes and endothelial cells. As an endothelial and leukocyte-associated transmembrane protein, ICAM1 is well known for its importance in stabilizing cell-cell interactions and facilitating leukocyte endothelial transmigration. The presence of heavy glycosylation and other structural characteristics lend ICAM1 binding sites for a number of immune-associated ligands. Notably, ICAM-1 binds to macrophage adhesion ligand-1 (Mac-1; ITGB2 / ITGAM), leukocyte function associated antigen-1 (LFA-1/integrin), and fibrinogen.ICAM-1 expressed by respiratory epithelial cells is also the binding site for rhinovirus, the causative agent of most common colds.
Inter-Cellular Adhesion Molecule 1 (ICAM1) is a type of intercellular adhesion molecule continuously present in low concentrations in the membranes of leukocytes and endothelial cells. As an endothelial and leukocyte-associated transmembrane protein, ICAM1 is well known for its importance in stabilizing cell-cell interactions and facilitating leukocyte endothelial transmigration. The presence of heavy glycosylation and other structural characteristics lend ICAM1 binding sites for a number of immune-associated ligands. Notably, ICAM-1 binds to macrophage adhesion ligand-1 (Mac-1, ITGB2 / ITGAM), leukocyte function associated antigen-1 (LFA-1/integrin), and fibrinogen.ICAM-1 expressed by respiratory epithelial cells is also the binding site for rhinovirus, the causative agent of most common colds.
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