Dataset Information

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

ABSTRACT: Identification of Tyrosine phosphorylated proteins in the ECM enriched fraction isolated from Human TM cells. Bottom up LC-MS/MS analysis of pY antibody enriched peptides from mouse ECM.

INSTRUMENT(S): Q Exactive

ORGANISM(S): Homo Sapiens (human)

SUBMITTER: Erik Soderblom

LAB HEAD: Erik Soderblom

PROVIDER: PXD015377 | Pride | 2020-06-02

REPOSITORIES: pride

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Dataset's files

Source:

			Action	DRS
	ID31564_01_901B_4749_072017.dat	Other
	ID31564_01_901B_4749_072017.raw	Raw
	ID37398_01_FSN20357_4749_042818.dat	Other
	ID37398_01_FSN20357_4749_042818.raw	Raw

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Global phosphotyrosinylated protein profile of cell-matrix adhesion complexes of trabecular meshwork cells.

Maddala Rupalatha R Rao Ponugoti Vasantha PV

American journal of physiology. Cell physiology 20200520 2

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 ...[more]

PMID: 32432933

Similar Datasets

Project description:Dr. Panjwani's laboratory is focusing on the mechanism by which galectins-3 and 7 mediate corneal epithelial cell migration. We are currently performing studies to: (i) identify and characterize the corneal epithelial cell surface and extracellular matrix (ECM) molecules which serve as counterreceptors of galectin-3 and -7, to establish whether the lectins modulate corneal epithelial cell migration by binding to well known integrins, growth factor receptors, and/or ECM molecules and (ii) determine whether galectin-3 mediates corneal epithelial cell migration indirectly by modulating the expression of key adhesion and/or signal transduction molecules by using small interfering RNA, cDNA microarrays and glycogene arrays. This study seeks the role of carbohydrate-based recognition system in the pathogenesis of glaucoma. In this study, RNA preparations of four normal and five glaucoma TM samples harvested over the last year from cadavers were hybridized and analyzed using the GLYCOv2 array. We have an NIH RO3 grant award to study the role of carbohydrate-based recognition system in the pathogenesis of glaucoma. In particular, it is known that a carbohydrate-binding protein, ELAM, serves as a marker for glaucoma. Other preliminary studies in my lab have shown that galectin-8 plays a role in the adhesion and spreading of trabecular meshwork cells (TM; the cells which modulate ocular pressure) and galectin-3 influences phagocytic capacity of TM cells. These studies suggest that galectins as well as ELAM and their counterreceptors may contribute to the pathogenesis of glaucoma. We would therefore like to compare glycogene expression patterns of normal and glaucomatous TM tissue. To this end, last month we submitted RNA preparations of five each of normal and glaucoma TM tissue harvested over the last year from cadavers. The data of these samples are now being analyzed. Meanwhile, we have analyzed RNA preparations of TM cells grown in culture from five normal and six glaucoma eyes. It is our hope that data from the two projects will enable us conclusively identify glycogenes which are differentially expressed in normal and glaucoma TM cell. Overall, the goal is to shed light on the role of carbohydrate-based recognition system and the carbohydrate-binding proteins in the pathogenesis of glaucoma.