Author(s)

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

Biochimie A, H?pital Saint-Antoine, P?le de Biologie Médicale et Pathologie, H?pitaux Universitaires de l’Est Parisien (AP-HP), Paris, France.
Biochimie A, H?pital Saint-Antoine, P?le de Biologie Médicale et Pathologie, H?pitaux Universitaires de l’Est Parisien (AP-HP), Paris, France;EA 4530, Université Paris-Sud, Chatenay-Malabry, France.
CNRS USR 3149, Spectrométrie de Masse Biologique et Protéomique, ESPCI-ParisTech, Paris, France.

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.

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

Baudin, B. , Bruneel, A. , Pernet, P. , Vaubourdolle, M. , Haddad, I. , Marcelo, P. , Rossier, J. and Vinh, J. (2013) New proteins and protein species identified in human umbilical vein endothelial cells by Fourier transform ion cyclotron resonance-mass spectrometry. Natural Science, 5, 919-924. doi: 10.4236/ns.2013.58111.