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  SILAC-Based Proteomics of Human Primary Endothelial Cell Morphogenesis Unveils Tumor Angiogenic Markers

Zanivan, S., Maione, F., Hein, M. Y., Hernandez-Fernaud, J. R., Ostasiewicz, P., Giraudo, E., et al. (2013). SILAC-Based Proteomics of Human Primary Endothelial Cell Morphogenesis Unveils Tumor Angiogenic Markers. MOLECULAR & CELLULAR PROTEOMICS, 12(12), 3599-3611. doi:10.1074/mcp.M113.031344.

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 Creators:
Zanivan, Sara1, Author              
Maione, Federica2, Author
Hein, Marco Y.1, Author              
Hernandez-Fernaud, Juan Ramon2, Author
Ostasiewicz, Pawel1, Author              
Giraudo, Enrico2, Author
Mann, Matthias1, Author              
Affiliations:
1Mann, Matthias / Proteomics and Signal Transduction, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565159              
2external, ou_persistent22              

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Free keywords: TRANSGENIC MICE; BASEMENT-MEMBRANE; VESSEL FORMATION; GENE-EXPRESSION; BLOOD-VESSELS; IN-VIVO; VASCULATURE; REVEALS; CARCINOGENESIS; IDENTIFICATION
 Abstract: Proteomics has been successfully used for cell culture on dishes, but more complex cellular systems have proven to be challenging and so far poorly approached with proteomics. Because of the complexity of the angiogenic program, we still do not have a complete understanding of the molecular mechanisms involved in this process, and there have been no in depth quantitative proteomic studies. Plating endothelial cells on matrigel recapitulates aspects of vessel growth, and here we investigate this mechanism by using a spike-in SILAC quantitative proteomic approach. By comparing proteomic changes in primary human endothelial cells morphogenesis on matrigel to general adhesion mechanisms in cells spreading on culture dish, we pinpoint pathways and proteins modulated by endothelial cells. The cell-extracellular matrix adhesion proteome depends on the adhesion substrate, and a detailed proteomic profile of the extracellular matrix secreted by endothelial cells identified CLEC14A as a matrix component, which binds to MMRN2. We verify deregulated levels of these proteins during tumor angiogenesis in models of multistage carcinogenesis. This is the most in depth quantitative proteomic study of endothelial cell morphogenesis, which shows the potential of applying high accuracy quantitative proteomics to in vitro models of vessel growth to shed new light on mechanisms that accompany pathological angiogenesis. The mass spectrometry proteomics data have been deposited to the ProteomeXchange Consortium with the data set identifier PXD000359.

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Language(s): eng - English
 Dates: 2013-12
 Publication Status: Published in print
 Pages: 13
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: ISI: 000329993600014
DOI: 10.1074/mcp.M113.031344
 Degree: -

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Title: MOLECULAR & CELLULAR PROTEOMICS
Source Genre: Journal
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Publ. Info: 9650 ROCKVILLE PIKE, BETHESDA, MD 20814-3996 USA : AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
Pages: - Volume / Issue: 12 (12) Sequence Number: - Start / End Page: 3599 - 3611 Identifier: ISSN: 1535-9476