April 2014
Volume 55, Issue 13
ARVO Annual Meeting Abstract  |   April 2014
Label free LC-MS/MS quantitative analysis of aqueous humor proteome from keratoconus and myopic controls patients
Author Affiliations & Notes
  • Arantxa Acera
    Research, Bioftalmik, Derio, Spain
  • Javier Soria
    Research, Bioftalmik, Derio, Spain
  • Alberto Villarrubia
    Instituto La Arruzafa, Cordoba, Spain
  • Felix Elortza
    Proteomics Platform, CIC bioGUNE, Derio, Spain
  • Mikel Azkargorta
    Proteomics Platform, CIC bioGUNE, Derio, Spain
  • Juan Alvarez de Toledo
    Instituto Barraquer, Barcelona, Spain
  • Ignacio Rodriguez-Agirretxe
    Instituto Clinico Quirurgico de Oftalmologia, Bilbao, Spain
  • Jesus Merayo-Lloves
    Instituto Oftalmologico Fernandez Vega and University of Oviedo, Oviedo, Spain
  • Tatiana Maria Suarez-Cortes
    Research, Bioftalmik, Derio, Spain
  • Footnotes
    Commercial Relationships Arantxa Acera, None; Javier Soria, None; Alberto Villarrubia, None; Felix Elortza, None; Mikel Azkargorta, None; Juan Alvarez de Toledo, None; Ignacio Rodriguez-Agirretxe, None; Jesus Merayo-Lloves, None; Tatiana Suarez-Cortes, None
  • Footnotes
    Support None
Investigative Ophthalmology & Visual Science April 2014, Vol.55, 4218. doi:
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      Arantxa Acera, Javier Soria, Alberto Villarrubia, Felix Elortza, Mikel Azkargorta, Juan Alvarez de Toledo, Ignacio Rodriguez-Agirretxe, Jesus Merayo-Lloves, Tatiana Maria Suarez-Cortes, Keratoconus CeyeC group; Label free LC-MS/MS quantitative analysis of aqueous humor proteome from keratoconus and myopic controls patients. Invest. Ophthalmol. Vis. Sci. 2014;55(13):4218.

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      © ARVO (1962-2015); The Authors (2016-present)

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Purpose: The etiology and the factors governing keratoconus (KC) progression remain to be elucidated. It has been reported to arise as a consequence of biochemical alterations in the cornea. It is known that the expression profile for some proteins in the aqueous humor (hAH) changes in some diseases. Our purpose was to identify the possible implication of hAH in the development of KC disease based on hAH protein expression differences among patients with KC and control subjects by a high-throughput mass spectrometry approach.

Methods: Aqueous humor samples were acquired from 5 patients with keratoconus and 5 myopic control subjects. Spectral counting mass spectrometry analysis was performed to determine the relative amounts of hAH proteins in keratokonus and controls patients.

Results: All patients included in the study presented severe keratoconus (K2>52D), and slit lamp examination revealed microfolds in Descemets membrane without clinical signs of hydrops. As a result of mass spectrometry analysis a total of 242 distinct proteins were significantly identified. Eleven proteins exhibited inter-group significant protein expression differences, seven of which were overexpressed whereas four exhibited decreased expression levels. Gene ontology analyses revealed that deregulated proteins are implicated in biological processes such as regulation of proteolysis, response to hypoxia, response to hydrogen peroxide and regulation of collagen biosynthesis, among others.

Conclusions: The protein expression profile in hAH from KC patients varies from that of myopic control subjects evidencing the implication, direct or indirect, of hAH in keratoconus disease. In consequence, this study demonstrates that in-deep analysis of hAH proteome will lead to a greater understanding of the pathophysiology of keratoconus disease.

Keywords: 663 proteomics • 574 keratoconus • 427 aqueous  

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