Protein Jagged 1, also known as JAG1, JAGL1 and CD339, is a single-pass type I membrane protein which contains 1DSL domain and 15EGF-like domains. JAG1/Jagged 1 is widely expressed in adult and fetal tissues. The expression of JAG1/Jagged 1 is up-regulated in cervical squamous cell carcinoma. JAG1/Jagged 1 is also expressed in bone marrow cell line HS-27a which supports the long-term maintenance of immature progenitor cells. JAG1/Jagged 1 is a ligand for multiple Notch receptors. It is involved in the mediation of Notch signaling. JAG1/Jagged 1 may be involved in cell-fate decisions during hematopoiesis. JAG1/Jagged 1 seems to be involved in early and late stages of mammalian cardiovascular development. It inhibits myoblast differentiation and enhances fibroblast growth factor-induced angiogenesis. Defects in JAG1/Jagged 1 are the cause of Alagille syndrome type 1 (ALGS1). Alagille syndrome is an autosomal dominant multisystem disorder defined clinically by hepatic bile duct paucity and cholestasis in association with cardiac, skeletal, and ophthalmologic manifestations. Defects in JAG1/Jagged 1 are also a cause of tetralogy of Fallot (TOF). TOF is a congenital heart anomaly which consists of pulmonary stenosis, ventricular septal defect, dextroposition of the aorta (aorta is on the right side instead of the left) and hypertrophy of the right ventricle. This condition results in a blue baby at birth due to inadequate oxygenation.
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.
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