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Scientific Research Publishing, Natural Science, 08(05), p. 919-924, 2013

DOI: 10.4236/ns.2013.58111

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New proteins and protein species identified in human umbilical vein endothelial cells by Fourier transform ion cyclotron resonance-mass spectrometry

This paper is made freely available by the publisher.
This paper is made freely available by the publisher.

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Abstract

For many years, HUVEC.com1 public database provides biological data relative to the proteome of human umbilical vein endothelial cells (HU-VECs), which are the most used human endothelial cell model in vascular biology. The proteins were identified using two-dimensional gel electrophoresis (2-DGE) for protein separation coupled with Matrix Assisted Laser Desorption-Ionization Mass Spectrometry (MALDI-TOF-MS) for identification. We present here an important update of HUVEC.com with 521 protein identifications as determined using Fourier transformed ion cyclotron resonance-mass spectrometry (FTICR-MS) applied to an unstained 2-DGE gel cut in 221 squared pieces; each identified protein being accompanied by a semi-quantitative three dimensional visualization is called “score imaging”. The squared analyzed gel and the alphabetical list of identified proteins, linked with their corresponding three-dimensional score imaging, are available at www.huvec.com . This original approach led to the establishment of the most protein-rich and informative database for HUVECs, as well as to the identification of some protein species, in particular with phosphorylation.