PXD005461-1

PXD005461 is an original dataset announced via ProteomeXchange.

Title	Galectin-1 and Galectin-3 interactors
Description	Identification of interactors is a major attempt in cell biology. Not only protein-protein but also protein-carbohydrate interactions are of high relevance for signal transduction in biological systems. Here we aim to identify novel interacting binding partners for the β-galactoside-binding proteins Galectin-1 (Gal-1) and Galectin-3 (Gal-3) in context of the eye disease proliferative vitreoretinopathy (PVR). PVR is one of the most common failures after retinal detachment surgeries and is characterized by the migration, adhesion and epithelial-to-mesenchymal transition (EMT) of retinal pigment epithelial cells (RPE) and the subsequent formation of sub- and epiretinal fibrocellular membranes. Gal-1 and Gal-3 bind in a dose- and carbohydrate-dependent manner to mesenchymal RPE cells and inhibit cellular processes like attachment and spreading. Yet knowledge about glycan-dependent interactors of Gal-1 and Gal-3 on RPE cells is very limited, although this is a prerequisite to unravel the influence of galectins on distinct cellular processes in RPE cells. In this approach, we identified by galectin pull-down experiments and quantitative proteomic screening 131 Galectin-3 and 15 Galectin-1 interactors. They mainly play a role in multiple binding processes and are mostly membrane proteins. Here we focused on two novel identified interactors of Gal-1 and Gal-3 in the context of PVR: the low-density lipoprotein receptor LRP1 and the platelet-derived growth factor receptor beta PDGFRB. We observed crosslinking and lattice formation of exogenous Gal-1 and Gal-3 with LRP1/PDGFRB and ITGB1 on the cell surface of human RPE cells. Weaker binding of Gal-1 and Gal-3 on these interactors and no lattice formation on the cell surface was seen, when complex-type-N-glycosylation was inhibited by treatment of the cells with Kifunensine. In conclusion, the identified specific glycoprotein ligands for Gal-1 and Gal-3 give us new insights in the highly specific binding of galectins to dedifferentiated RPE cells and the resulting prevention of PVR-associated cellular events.
HostingRepository	PRIDE
AnnounceDate	2017-06-06
AnnouncementXML	Submission_2017-06-06_05:11:35.xml
DigitalObjectIdentifier	https://dx.doi.org/10.6019/PXD005461
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Supported dataset by repository
PrimarySubmitter	Jara Obermann
SpeciesList	scientific name: Homo sapiens (Human); NCBI TaxID: 9606;
ModificationList	Deamidated; Oxidation; Carbamidomethyl
Instrument	LTQ Orbitrap XL

Revision	Datetime	Status	ChangeLog Entry
0	2016-11-30 00:23:19	ID requested
⏵ 1	2017-06-06 05:11:36	announced

Obermann J, Priglinger CS, Merl-Pham J, Geerlof A, Priglinger S, G, ö, tz M, Hauck SM, Proteome-wide Identification of Glycosylation-dependent Interactors of Galectin-1 and Galectin-3 on Mesenchymal Retinal Pigment Epithelial (RPE) Cells. Mol Cell Proteomics, 16(8):1528-1546(2017) [pubmed]

curator keyword: Biological

submitter keyword: galectin, pull-down, retina, interactors

Stefanie Hauck
contact affiliation	Research Unit Protein Science Helmholtz Center Munich Germany
contact email	hauck@helmholtz-muenchen.de
lab head
Jara Obermann
contact affiliation	Helmholtz Centre Munich
contact email	jara.obermann@helmholtz-muenchen.de
dataset submitter

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PRIDE project URI

• PRIDE
  1. PXD005461
     1. Label: PRIDE project
     2. Name: Galectin-1 and Galectin-3 interactors