PXD006424

PXD006424 is an original dataset announced via ProteomeXchange.

Title	Biomechanical rigidity and quantitative proteomics analyses of segmental regions of the ocular trabecular meshwork at physiologic and elevated pressures
Description	The extracellular matrix (ECM) of the ocular trabecular meshwork (TM) builds resistance to aqueous humor outflow, thereby regulating intraocular pressure (IOP). Glaucoma, a leading cause of blindness worldwide, is associated with changes in the ECM of the TM. The elastic modulus indicates glaucomatous TM is more rigid than age-matched normal TM; however, the biomechanical properties of segmental low (LF) and high flow (HF) TM regions in response to elevated pressure, are unknown. In this study, we measured the elastic modulus by atomic force microscopy (AFM) and measured protein expression differences in perfused human TM tissues by proteomics analyses. The elastic modulus of LF regions was 2.3-fold stiffer than HF regions at physiological (1x) pressure, and 7.4-fold or 3.5-fold stiffer than HF regions at elevated (2x) pressure after 24 or 72 hours, respectively. Quantitative proteomics using isobaric tandem mass tags (TMT), multi-notch isolation, high resolution, and extended multiplexing were used to compare protein expression levels between normal, LF, and HF regions at the two pressures. A total of 3730 proteins (2 peptides per protein) were identified from the ECM samples, and 2637 proteins were quantified. Statistically significant ECM proteins over expressed in LF compared with HF regions at 2x, and in HF regions at 1x compared with 2x pressure were determined. A sub-set of ECM proteins, including decorin, TGFβ-induced protein, keratocan, lumican, dermatopontin and thrombospondin 4, were common differential candidates in both comparisons. These data suggest a correlation between the biomechanical properties of TM regions and differential levels of specific ECM proteins in response to elevated pressure.
HostingRepository	PRIDE
AnnounceDate	2018-01-22
AnnouncementXML	Submission_2018-01-22_03:36:54.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Phillip Wilmarth
SpeciesList	scientific name: Homo sapiens (Human); NCBI TaxID: 9606;
ModificationList	TMT6plex-126 reporter+balance reagent acylated residue; monohydroxylated residue; iodoacetamide derivatized residue
Instrument	Orbitrap Fusion ETD

Revision	Datetime	Status	ChangeLog Entry
0	2017-05-02 05:40:39	ID requested
⏵ 1	2018-01-22 03:36:55	announced

Vranka JA, Staverosky JA, Reddy AP, Wilmarth PA, David LL, Acott TS, Russell P, Raghunathan VK, Biomechanical Rigidity and Quantitative Proteomics Analysis of Segmental Regions of the Trabecular Meshwork at Physiologic and Elevated Pressures. Invest Ophthalmol Vis Sci, 59(1):246-259(2018) [pubmed]

curator keyword: Biomedical

submitter keyword: human, biomechanical rigidity, trabecular mesh, glaucoma, high resolution mass spectrometry, multi-notch isolation, tandem mass tags, extended multiplexing, quantitative proteomics

Janice Vranka
contact affiliation	Department of Ophthalmology, Casey Eye Institute, Oregon Health & Science University, Portland, OR, USA
contact email	vranka@ohsu.edu
lab head
Phillip Wilmarth
contact affiliation	OHSU
contact email	wilmarth@ohsu.edu
dataset submitter

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PRIDE project URI

• PRIDE
  1. PXD006424
     1. Label: PRIDE project
     2. Name: Biomechanical rigidity and quantitative proteomics analyses of segmental regions of the ocular trabecular meshwork at physiologic and elevated pressures