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Pierre R. Fournie, Stephane D. Galiacy, Carine Froment, Emmanuelle Mouton-Barbosa, Angélique Erraud, Karima Chaoui, Laurence Desjardins, Bernard Monsarrat, Odile Burlet-Schiltz, Francois J. Malecaze; Deeper In The Human Cornea Proteome Using Nanolc-orbitrap Ms/ms: An Improvement For Future Studies On Cornea Homeostasis And Pathophysiology. Invest. Ophthalmol. Vis. Sci. 2012;53(14):4184.
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© ARVO (1962-2015); The Authors (2016-present)
To investigate human cornea proteome. The human cornea is composed of several layers interacting in a complex manner and possessing specific functions, like eye protection and optical clearness. Only few proteomic studies of mammalian cornea have been performed leading to the identification of less than 200 proteins in human corneas.
The present study explores the proteome of the intact normal human cornea using a shot-gun nanoLC-MS/MS strategy and an LTQ Orbitrap mass spectrometer.
A total of 2070 distinct corneal proteins were identified from five human cornea samples, which represents a 14-fold improvement in the number of proteins identified so far for human cornea. Network and gene ontology analyses were used to determine biological pathways specific of the human cornea. They allowed the identification of subnetworks of putative importance for corneal diseases, like a redox regulation and oxidative stress network constituted of aldehyde and alcohol dehydrogenases, most of them being described for the first time in human cornea.
This enlarged dataset of human corneal proteins represents a valuable reference library for further studies on cornea homeostasis and pathophysiology.
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