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Yanofsky, C.M., Bell, A.W., Lesimple, S., Morales, F., Lam, T.T., Blakney, G.T., Marshall, A.G., Carillo, B., Lekpor K., Boismenu, D. and Kearney, R.E. (2005) Mul ticomponent internal recalibration of an LC-FTICR-MS analysis employing a partially characterized complex peptide mixture: Systematic and random errors. Analyti cal Chemistry, 77, 7246-7254. doi:10.1021/ac050640q

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

  AUTHORS: Bruno Baudin, Arnaud Bruneel, Pascal Pernet, Michel Vaubourdolle, Iman Haddad, Paulo Marcelo, Jean Rossier, Joëlle Vinh

  KEYWORDS: Database; 2-DGE; Endothelium;HUVEC; FTICR; Tubulins

  JOURNAL NAME: Natural Science, Vol.5 No.8, August 7, 2013

  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.