10.1021/pr901113z.s002
Stephanie Kaspar
Stephanie
Kaspar
Andrea Matros
Andrea
Matros
Hans-Peter Mock
Hans-Peter
Mock
Proteome and Flavonoid Analysis Reveals Distinct Responses of Epidermal Tissue and Whole Leaves upon UV−B Radiation of Barley (<i>Hordeum vulgare</i> L.) Seedlings
American Chemical Society
2010
barley seedling leaf epidermis
Whole Leaves
flavonoid molecule
Flavonoid Analysis
gel electrophoresis
oxidative stress
metabolism proteins
UV
flavonoid content
Flavonoid analysis
Distinct Responses
mesophyll tissue
epidermis tissue
DE
Epidermal Tissue
expression pattern
protein expression
2010-05-07 00:00:00
Journal contribution
https://acs.figshare.com/articles/journal_contribution/Proteome_and_Flavonoid_Analysis_Reveals_Distinct_Responses_of_Epidermal_Tissue_and_Whole_Leaves_upon_UV_B_Radiation_of_Barley_i_Hordeum_vulgare_i_L_Seedlings/2771722
We describe here the effect of UV−B irradiation on the proteome and flavonoid content of the barley seedling leaf epidermis and mesophyll. Flavonoid analysis was performed using UPLC-PDA/-MS. The major flavonoid molecule responding to UV−B radiation was saponarin, and this accumulated in the epidermis, but not in the mesophyll. Changes in protein expression were determined using two-dimensional gel electrophoresis (2-DE) and identified 11 responsive proteins (seven up-regulated and two down-regulated in the epidermis; and one up- and one down-regulated in the mesophyll). A label-free LC-MS/MS<sup>E</sup> approach was applied for a subset of samples consisting of epidermis tissue and was able to detect a further 15 (11 up-regulated and four down-regulated) proteins. Most of the proteins with changed expression pattern after UV−B treatment were involved in initial responses characteristic for oxidative stress. Others were primary metabolism proteins involved in the supply of precursors for secondary metabolites. A separate analysis of epidermis and mesophyll tissue is important to give a spatially resolved picture of the response to UV−B treatment. The label-free LC-MS/MS<sup>E</sup> approach is complementary to the more conventional two-dimensional gel electrophoresis, as there was no overlap between the spectra of proteins identified by the two techniques.