Global phosphotyrosinylated protein profile of cell-matrix adhesion complexes of trabecular meshwork cells.
Rupalatha MaddalaPonugoti Vasantha RaoPublished in: American journal of physiology. Cell physiology (2020)
Dysregulation of the mechanical properties and cell adhesive interactions of trabecular meshwork (TM) are known to impair aqueous humor drainage and elevate intraocular pressure in glaucoma patients. The identity of regulatory mechanisms underlying TM mechanotransduction, however, remains elusive. Here we analyzed the phosphotyrosine proteome of human TM cell-extracellular matrix (ECM) adhesion complexes, which play a key role in sensing and transducing extracellular chemical and mechanical cues into intracellular activities, using a two-level affinity pull-down (phosphotyrosine antibody and titanium dioxide beads) method and mass spectrometry. This analysis identified ~1,000 tyrosine-phosphorylated proteins of TM cell-ECM adhesion complexes. Many consensus adhesome proteins were found to be tyrosine phosphorylated. Interestingly, several of the phosphotyrosinylated proteins found in TM cell-ECM adhesion complexes are known to be required for podocyte glomerular filtration, indicating the existence of molecular parallels that are likely relevant to the shared fluid barrier and filtration functions of the two mechanosensitive cell types.
Keyphrases
- single cell
- extracellular matrix
- cell therapy
- mass spectrometry
- endothelial cells
- end stage renal disease
- chronic kidney disease
- stem cells
- newly diagnosed
- pseudomonas aeruginosa
- signaling pathway
- liquid chromatography
- postmenopausal women
- biofilm formation
- oxidative stress
- mesenchymal stem cells
- small molecule
- ionic liquid
- simultaneous determination
- high glucose
- cell death
- cell cycle arrest
- binding protein
- pi k akt
- pluripotent stem cells