Global Phosphotyrosinylated Protein Profile of Cell-Matrix Adhesion Complexes of Trabecular Meshwork Cells.

Global Phosphotyrosinylated Protein Profile of Cell-Matrix Adhesion Complexes of Trabecular Meshwork Cells.
Am J Physiol Cell Physiol. 2020 May 20;:
Authors: Maddala R, Rao PV
Abstract
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 ~1000 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.
PMID: 32432933 [PubMed - as supplied by publisher]

Source: Am J Physiol Cell Ph... - May 19, 2020 Category: Cytology Authors: Maddala R, Rao PV Tags: Am J Physiol Cell Physiol Source Type: research