In order to understand the molecular basis of salt stress response, a proteomic approach, employing two-dimensional electrophoresis and matrix-assisted laser desorption/ionization time of flight mass spectrometry (MALDI-TOF MS), was used to identify proteins affected by salinity in wheat (Triticum durum 'Ofanto'). Identification of proteins, whose levels were altered, was performed by comparing protein patterns of salt-treated and control plants. A set of control plants was grown without NaCl addition under the same conditions as the salt-treated plants. Proteins were extracted from the leaves of untreated and NaCl-treated plants, and resolved using 24-cm immobilized pH gradient strips with a pH 4-7 linear gradient in the first dimension and a 12.5% sodium dodecyl sulphate polyacrylamide gel electrophoresis in the second dimension; the gels were stained with Coomassie and image analysis was performed. Quantitative evaluation, statistical analyses and MALDI-TOF MS characterization of the resolved spots in treated and untreated samples enabled us to identify 38 proteins whose levels were altered in response to salt stress. In particular, ten proteins were downregulated and 28 were upregulated. A possible role of these proteins in response to salinity is discussed. © 2008 Springer-Verlag.

Identification of changes in Triticum durum L. leaf proteome in response to salt stress by two-dimensional electrophoresis and MALDI-TOF mass spectrometry / Caruso, Giuseppe; Cavaliere, Chiara; Guarino, Chiara; Gubbiotti, Riccardo; Foglia, Patrizia; Lagana', Aldo. - In: ANALYTICAL AND BIOANALYTICAL CHEMISTRY. - ISSN 1618-2642. - STAMPA. - 391:1(2008), pp. 381-390. [10.1007/s00216-008-2008-x]

Identification of changes in Triticum durum L. leaf proteome in response to salt stress by two-dimensional electrophoresis and MALDI-TOF mass spectrometry

CARUSO, Giuseppe;CAVALIERE, CHIARA;GUARINO, CHIARA;GUBBIOTTI, RICCARDO;FOGLIA, Patrizia;LAGANA', Aldo
2008

Abstract

In order to understand the molecular basis of salt stress response, a proteomic approach, employing two-dimensional electrophoresis and matrix-assisted laser desorption/ionization time of flight mass spectrometry (MALDI-TOF MS), was used to identify proteins affected by salinity in wheat (Triticum durum 'Ofanto'). Identification of proteins, whose levels were altered, was performed by comparing protein patterns of salt-treated and control plants. A set of control plants was grown without NaCl addition under the same conditions as the salt-treated plants. Proteins were extracted from the leaves of untreated and NaCl-treated plants, and resolved using 24-cm immobilized pH gradient strips with a pH 4-7 linear gradient in the first dimension and a 12.5% sodium dodecyl sulphate polyacrylamide gel electrophoresis in the second dimension; the gels were stained with Coomassie and image analysis was performed. Quantitative evaluation, statistical analyses and MALDI-TOF MS characterization of the resolved spots in treated and untreated samples enabled us to identify 38 proteins whose levels were altered in response to salt stress. In particular, ten proteins were downregulated and 28 were upregulated. A possible role of these proteins in response to salinity is discussed. © 2008 Springer-Verlag.
2008
matrix-assisted laser desorption/ionization time of flight; proteomics; salt stress; triticum durum; two-dimensional electrophoresis; wheat
01 Pubblicazione su rivista::01a Articolo in rivista
Identification of changes in Triticum durum L. leaf proteome in response to salt stress by two-dimensional electrophoresis and MALDI-TOF mass spectrometry / Caruso, Giuseppe; Cavaliere, Chiara; Guarino, Chiara; Gubbiotti, Riccardo; Foglia, Patrizia; Lagana', Aldo. - In: ANALYTICAL AND BIOANALYTICAL CHEMISTRY. - ISSN 1618-2642. - STAMPA. - 391:1(2008), pp. 381-390. [10.1007/s00216-008-2008-x]
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11573/358710
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