Related Experiment Video
Updated: Jul 13, 2026

Static Adhesion Assay for the Study of Integrin Activation in T Lymphocytes
Published on: June 13, 2014
Either integrin subunit beta1 or beta3 is involved in mediating monocyte adhesion, IL-1beta protein and mRNA
Amy S Chung1, Qiang Gao, Weiyuan John Kao
1School of Pharmacy, University of Wisconsin-Madison, Madison, WI 53705, USA.
Abstract:
We synthesized gelatin-based, interpenetrating network (IPN) scaffolds immobilized with fibronectin (FN)-derived peptides to assess monocyte-biomaterial interaction. Human primary monocytes were seeded onto peptide-grafted IPN or tissue-culture polystyrene (TCPS) pre-adsorbed with FN or FN-derived peptides. Monocyte cell density on both TCPS and IPN surfaces was higher in the presence of the arginine-glycine-aspartic acid (RGD) peptide. Pretreatment with anti-integrin beta1 or beta3 antibody decreased monocyte density on all ligand-modified TCPS and IPN. Interleukin-1 beta (IL-1beta) protein levels of cells on modified TCPS decreased over time. IL-1beta expression of monocytes in the presence of IPNs peaked at 24 h and then decreased through 168 h. Ligand identity did not affect IL-1beta expression in either TCPS or IPN samples. Pretreatment with anti-integrin beta1 or beta3 antibody reduced IL-1beta levels from both TCPS and IPN samples in a ligand-independent manner, particularly at 24 h. Monocytic IL-1beta mRNA expression in IPN samples without antibody pretreatment was highest at 2 h and decreased over time. IL-1beta mRNA expression in cells with anti-integrin beta1 or beta3 antibody pretreatment was similar to those without antibody pretreatment, except for methoxygrafted IPN samples. The change in IL-1beta mRNA expression did not correlate with changes in protein expression. The results indicate that monocyte adhesion was affected by the substrate and the RGD sequence and beta1 or beta3 containing integrin receptors. beta1- or beta3-containing integrin receptors were also involved in IL-1beta gene and protein expression in monocytes adhered to gelatin-based biomaterial surfaces.
Related Concept Videos
Integrins
Some ECM proteins assemble into a basement membrane to which the remaining components adhere. Proteoglycans typically form the bulk of the ECM while fibrous proteins, like collagen,...
Intracellular Signaling Affects Focal Adhesions
Some...
Activation of Integrins
In "outside-in signaling," external factors in the extracellular space bind to exposed ligand binding sites on integrins. This causes the inactive protein to undergo a conformational change to become active. Integrins are often clustered on the cell membrane. Repetitive and regularly spaced ligand binding events provide an effective stimulus.
Fibronectins Connect Cells with ECM
Both proteoglycans and collagen are attached to fibronectin proteins, which, in turn, are attached to integrin proteins. These integrin proteins interact with transmembrane...
Immunoglobulin-like Cell Adhesion Molecules
Ig-CAMs exhibit either homophilic binding (to other Ig-CAMs) or heterophilic binding (to other ligands such as integrins). While most Ig-CAMs...
Overview of Cell-Matrix Interactions

