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JAM-A protein plays protective role in pathogenesis of age related diseases as Atherosclerosis, Apoplexy, thrombosis, Hypertension, Ophthalmological pathology.Short peptides Lys (show LYZ Proteins)-Glu (show DCTN1 Proteins), Lys (show LYZ Proteins)-Glu (show DCTN1 Proteins)-Asp (show ASIP Proteins), and Ala-Glu (show DCTN1 Proteins)-Asp (show ASIP Proteins)-Gly could influence on F11R gene expression leading to recovery of JAM-A synthesis in cells.
Dysregulation of JAM-A via p63 (show RPE65 Proteins)/GATA-3 (show GATA3 Proteins) signaling pathway occurs in squamous cell carcinomas of the head and neck.
JAM family members differentially regulate CXCR4 (show CXCR4 Proteins) function and CXCL12 (show CXCL12 Proteins) secretion in the bone marrow niche.
Our observations suggest that increased expression of JAM-A promotes neoplasia of lung adenocarcinoma. In addition, an anti-JAM-A antibody efficiently reduced cell proliferation and provoked apoptosis, indicating the potential feasibility of JAM-A-inhibitory cancer therapy.
a new role for CD321 in endothelial cells
We have shown that tension on JAM-A activates RhoA (show RHOA Proteins) to control cell stiffness. Phosphorylation of JAM-A at S284 is required for activation of RhoA (show RHOA Proteins) and increased cell stiffness in response to tension on the protein
Using patient-derived glioblastoma cancer stem cells, we confirmed that JAM-A is suppressed by miR (show MLXIP Proteins)-145
Screening of a library of human cell surface membrane proteins showed that the Hom-1 vesivirus could utilize human junctional adhesion molecule 1 as a receptor to enter cells and initiate replication.
Our results showed that APOC3 (show APOC3 Proteins) was closely associated with the inflammatory process in ECs, and that this process was characterized by the increased expression of TNF-alpha (show TNF Proteins). Inflammatory processes further disrupted the tight junctions (TJs) between HUVECs by causing increased expression of JAM-1.
High expression of junctional adhesion molecule-A and EphB2 (show EPHB2 Proteins) can predict poor overall survival and high mortality rate, and EphB2 (show EPHB2 Proteins) is an independent prognostic biomarker in lung adenocarcinoma patients.
Deletion JAM-A from platelets increases early-stage neointima formation after carotid artery wire injury in hyperlipidemic mice.
JAM-A is present in the prostate and seminal vesicles and in all three regions of the epididymis where it is secreted in epididymosomes in the luminal fluid and can be delivered to sperm.
Soluble JAM-A secreted from cardiac progenitor cells reduces infiltration of neutrophils after myocardial infarction and ameliorates tissue damage through prevention of excess inflammation.
JAM-A up-regulation can increase the proliferation, cytokine secretion and wound-homing ability of MSCs, thus accelerating the repair rate of full-thickness skin defects
Endothelial JAM-A but not hematopoietic JAM-A facilitates reovirus T1L (show CERS6 Proteins) bloodstream entry and egress.
Deletion of JAM-A causes a gain-of-function in platelets, with lower activation thresholds and increased inflammatory activities. This leads to an increase of plaque formation, particularly in early stages of the disease.
The F11r gene is directly regulated by retinoic acid in the embryonic mesoderm.
Redistribution of JAM-A in endothelial cells after stimulation with pro-atherogenic oxidized lipoproteins results in increased transmigration of mononuclear cells.
JAM-A has a prominent role in regulating leukocyte infiltration after brain I/R injury and could be a new target in limiting post-ischemic inflammation.
JAM-A regulates epithelial permeability via association with ZO-2 (show TJP2 Proteins), afadin, and PDZ-GEF1 (show RAPGEF2 Proteins) to activate Rap2c (show RAP2C Proteins) and control contraction of the apical cytoskeleton.
Tight junctions represent one mode of cell-to-cell adhesion in epithelial or endothelial cell sheets, forming continuous seals around cells and serving as a physical barrier to prevent solutes and water from passing freely through the paracellular space. The protein encoded by this immunoglobulin superfamily gene member is an important regulator of tight junction assembly in epithelia. In addition, the encoded protein can act as (1) a receptor for reovirus, (2) a ligand for the integrin LFA1, involved in leukocyte transmigration, and (3) a platelet receptor. Multiple 5' alternatively spliced variants, encoding the same protein, have been identified but their biological validity has not been established.
junctional adhesion molecule 1
, junctional adhesion molecule A
, platelet F11 receptor
, platelet adhesion molecule 1
, BV11 antigen
, F11 receptor/F11R
, junction cell adhesion molecule A
, junction cell adhesion molecule1