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Integrins are transmembrane receptors that help cell–cell and cell–extracellular matrix (ECM) adhesion. [3] Upon ligand binding, integrins activate signal transduction pathways that mediate cellular signals such as regulation of the cell cycle, organization of the intracellular cytoskeleton, and movement of new receptors to the cell membrane. [4]
These experiments yielded the protein name “integrin” as a description of the proteins' integral role in cellular adhesion processes and the transmembrane association between the extracellular matrix and the cytoskeleton. [2] LFA-1, a leukocyte integrin, was first discovered by Timothy Springer in mice in the 1980s. [2]
These short amino acid sequences are the minimum motif of a larger protein that is necessary for binding to a cell surface receptor that drives cell adhesion. [40] The majority (89%) of published studies on biomaterials functionalized with cell adhesive peptides use RGD, whereas IKVAV and YIGSR are used in 6%, and 4% of those studies ...
Integrin, alpha L (antigen CD11A (p180), lymphocyte function-associated antigen 1; alpha polypeptide), also known as ITGAL, is a protein that in humans is encoded by the ITGAL gene. [5] CD11a functions in the immune system. It is involved in cellular adhesion and costimulatory signaling. It is the target of the drug efalizumab.
The major cell-matrix adhesion receptors are integrins and therefore the adhesome of cell-matrix adhesion is referred to as the integrin adhesome. [4] Cell-cell adhesion is primarily mediated by cadherin receptors and therefore the adhesome of cell-cell adhesion is referred to as the cadherin adhesome or cadhesome. [5]
The process is highly regulated by cell adhesion molecules, particularly, the addressin also known as MADCAM1. This antigen is known for its role in tissue-specific adhesion of lymphocytes to high endothelium venules. [23] Through these interactions they play a crucial role in orchestrating circulating lymphocytes.