TY  - JOUR
A1  - Rasouli, Fatemeh
A1  - Kiani-Pouya, Ali
A1  - Li, Leiting
A1  - Zhang, Heng
A1  - Chen, Zhonghua
A1  - Hedrich, Rainer
A1  - Wilson, Richard
A1  - Shabala, Sergey
T1  - Sugar beet (Beta vulgaris) guard cells responses to salinity stress: a proteomic analysis
JF  - International Journal of Molecular Sciences
N2  - Soil salinity is a major environmental constraint affecting crop growth and threatening global food security. Plants adapt to salinity by optimizing the performance of stomata. Stomata are formed by two guard cells (GCs) that are morphologically and functionally distinct from the other leaf cells. These microscopic sphincters inserted into the wax-covered epidermis of the shoot balance CO\(_2\) intake for photosynthetic carbon gain and concomitant water loss. In order to better understand the molecular mechanisms underlying stomatal function under saline conditions, we used proteomics approach to study isolated GCs from the salt-tolerant sugar beet species. Of the 2088 proteins identified in sugar beet GCs, 82 were differentially regulated by salt treatment. According to bioinformatics analysis (GO enrichment analysis and protein classification), these proteins were involved in lipid metabolism, cell wall modification, ATP biosynthesis, and signaling. Among the significant differentially abundant proteins, several proteins classified as “stress proteins” were upregulated, including non-specific lipid transfer protein, chaperone proteins, heat shock proteins, inorganic pyrophosphatase 2, responsible for energized vacuole membrane for ion transportation. Moreover, several antioxidant enzymes (peroxide, superoxidase dismutase) were highly upregulated. Furthermore, cell wall proteins detected in GCs provided some evidence that GC walls were more flexible in response to salt stress. Proteins such as L-ascorbate oxidase that were constitutively high under both control and high salinity conditions may contribute to the ability of sugar beet GCs to adapt to salinity by mitigating salinity-induced oxidative stress.
KW  - guard cells
KW  - stomata
KW  - sugar beet
KW  - salt stress
KW  - proteomic
Y1  - 2020
U6  - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:bvb:20-opus-285765
SN  - 1422-0067
VL  - 21
IS  - 7
ER  - 
TY  - JOUR
A1  - Jarausch, Johannes
A1  - Neuenroth, Lisa
A1  - Andag, Reiner
A1  - Leha, Andreas
A1  - Fischer, Andreas
A1  - Asif, Abdul R.
A1  - Lenz, Christof
A1  - Eidizadeh, Abass
T1  - Influence of shear stress, inflammation and BRD4 inhibition on human endothelial cells: a holistic proteomic approach
JF  - Cells
N2  - Atherosclerosis is an important risk factor in the development of cardiovascular diseases. In addition to increased plasma lipid concentrations, irregular/oscillatory shear stress and inflammatory processes trigger atherosclerosis. Inhibitors of the transcription modulatory bromo- and extra-terminal domain (BET) protein family (BETi) could offer a possible therapeutic approach due to their epigenetic mechanism and anti-inflammatory properties. In this study, the influence of laminar shear stress, inflammation and BETi treatment on human endothelial cells was investigated using global protein expression profiling by ion mobility separation-enhanced data independent acquisition mass spectrometry (IMS-DIA-MS). For this purpose, primary human umbilical cord derived vascular endothelial cells were treated with TNFα to mimic inflammation and exposed to laminar shear stress in the presence or absence of the BRD4 inhibitor JQ1. IMS-DIA-MS detected over 4037 proteins expressed in endothelial cells. Inflammation, shear stress and BETi led to pronounced changes in protein expression patterns with JQ1 having the greatest effect. To our knowledge, this is the first proteomics study on primary endothelial cells, which provides an extensive database for the effects of shear stress, inflammation and BETi on the endothelial proteome.
KW  - HUVEC
KW  - shear stress
KW  - endothelial
KW  - proteomic
KW  - BRD4
KW  - JQ1
KW  - DIA-MS
KW  - BET Inhibitor
KW  - atherosclerosis
Y1  - 2022
U6  - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:bvb:20-opus-289872
SN  - 2073-4409
VL  - 11
IS  - 19
ER  -