Biology:JAM1
Junctional adhesion molecule A (JAM-A) is a protein that in humans is encoded by the F11R gene.[1] JAM-A (also known as F11R, JAM-1) was the first of the junctional adhesion molecules to be discovered, and is located in the tight junctions of both epithelial and endothelial cells.[2]
Functions
JAM-1 interacts with cells in a homophilic manner in order to preserve the structure of the junction while moderating its permeability. It can also interact with receptors as a heterophilic structure by acting as a ligand for LFA-1 and facilitating leukocyte transmigration.[2] JAM-1 also plays a significant role in many different cellular functions, including being both a reovirus receptor and a platelet receptor.[2]
References
- ↑ "Cutting edge: combined treatment of TNF-alpha and IFN-gamma causes redistribution of junctional adhesion molecule in human endothelial cells". Journal of Immunology 163 (2): 553–7. Jul 1999. doi:10.4049/jimmunol.163.2.553. PMID 10395639.
- ↑ 2.0 2.1 2.2 Naik, U. P.; Eckfeld, K. (2003). "Junctional adhesion molecule 1 (JAM-1)". Journal of Biological Regulators and Homeostatic Agents 17 (4): 341–347. ISSN 0393-974X. PMID 15065765. https://pubmed.ncbi.nlm.nih.gov/15065765.
This article incorporates text from the United States National Library of Medicine, which is in the public domain.
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