Junctional adhesion molecule-A (JAM-A); also known as F11 receptor (F11R) or Cluster of Differentiation 321 (CD321); is a transmembrane protein expressed at tight junctions of epithelial and endothelial cells; as well as on circulating leukocytes. JAM-A protein serves as a serotype-independent receptor for mammalian orthoreoviruses (reoviruses). It is also a ligand for the integrin LFA1; involves in leukocyte transmigration. As a cell adhesion molecule of the immunoglobulin superfamily; JAM-A protein involves in platelet adhesion; secretion and aggregation; and plays a crucial role in inflammatory thrombosis and atherosclerosis. In addition; it may be a potential therapeutic target for breast cancer.
Junctional Adhesion Molecule A (JAM-A) is a single-pass type I membrane protein that belongs to the immunoglobulin superfamily. JAM-A contains 2 Ig-like V-type (immunoglobulin-like) domains and Interacts with the ninth PDZ domain. JAM-A is localized to the tight junctions of both epithelial and endothelial cells. JAM-A seems to be involved in epithelial tight junction formation. JAM-A appears early in primordial forms of cell junctions and recruits PARD3. The association of the PARD6-PARD3 complex may prevent the interaction of PARD3 with JAM-A, thereby preventing tight junction assembly. JAM-A plays a role in regulating monocyte transmigration involved in regulating integrity of the epithelial barrier. In the case of orthoreovirus infection, JAM-A serves as receptor for the virus.
Junctional Adhesion Molecule B (JAM-B) is a single-pass type I membrane protein that belongs to the juctional adhesion molecules family. JAM-B includes a signal sequence (aa 1-28); an extracellular region (aa 29-238) with one Ig-like C2-type domain and one Ig-like V-type domain; a transmembrane segment (aa 239-259); and a cytoplasmic domain (aa 260 - 298). JAMB is localized to the tight junctions between endothelial cells or epithelial cells. JAM-B is prominently expressed in the heart; placenta; lung; foreskin and lymph node. It is also present on the endothelia of other vessels. JAM-B acts as an adhesive ligand for interacting with a variety of immune cell types and may play a role in lymphocyte homing to secondary lymphoid organs.
Junctional adhesion molecules (JAMs) are endothelial and epithelial adhesion molecules involved in the recruitment of circulating leukocytes to inflammatory sites. JAML (Junctional adhesion molecule-like), also known as AMICA1 (Adhesion molecule interacting with CXADR antigen 1), a protein related to the JAM family, is restricted to leukocytes and promotes their adhesion to endothelial cells. It contains 2 extracellular immunoglobulin-like domains, a transmembrane segment, and a cytoplasmic tail involved in activation signaling. Monocytic JAML/AMICA1 plays a critical role in regulating monocyte transendothelial migration (TEM) probably via binding to the endothelial coxsackie and adenovirus receptor (CAR) and other tight junction-associated adhesive molecules. The Expression of JAML/AMICA1 is restricted to the hematopoietic tissues with the exception of liver. JAML may function in transmigration of leukocytes through epithelial and endothelial tissues. Expressed at the plasma membrane of polymorphonuclear leukocytes, JAML/AMICA1 also enhances myeloid leukemia cell adhesion to endothelial cells.
Mitogen-activated protein kinase 8 (MAPK8), also known as JNK1, is a member of the MAP kinase family. MAP kinases act as an integration point for multiple biochemical signals, and are involved in a wide variety of cellular processes such as proliferation, differentiation, transcription regulation and development. The protein kinases JNK1 has been found to serve as critical molecular links between obesity, metabolic inflammation, and disorders of glucose homeostasis. It is critically involved in the promotion of diet-induced obesity, metabolic inflammation and beta-cell dysfunction. The selective deficiency of JNK1 in the murine nervous system is sufficient to suppress diet-induced obesity. Genetic analysis indicates that the effects of JNK1 can be separated from effects of JNK1 on obesity. JNK1 is a potential pharmacological target for the development of drugs that might be useful for the treatment of metabolic syndrome, and type 2 diabetes. Furthermore, JNK1 plays a major role in the hypoxic cellular damage. JNK1 protein might be an attractive target for antihypoxic therapy in increasing resistance to many pathological conditions and diseases, leading to the oxygen deficit.
Responds to activation by environmental stress and pro-inflammatory cytokines by phosphorylating a number of transcription factors, primarily components of AP-1 such as JUN, JDP2 and ATF2 and thus regulates AP-1 transcriptional activity. In T-cells, JNK1 and JNK2 are required for polarized differentiation of T-helper cells into Th1 cells. Phosphorylates heat shock factor protein 4.
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