Browse
Submit Data
Databases
API
Help

Dataset Information

21 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Production of reactive oxygen species by PuRBOHF is critical for stone cell development in pear fruit.

ABSTRACT: The production of reactive oxygen species (ROS) by NADPH oxidase, which is also referred to as respiratory burst oxidase homolog (RBOH), affects several processes in plants. However, the role of RBOHs in cell wall lignification is not well understood. In this study, we show that PuRBOHF, an RBOH isoform, plays an important role in secondary wall formation in pear stone cells. ROS were closely associated with lignin deposition and stone cell formation according to microscopy data. In addition, according to the results of an in situ hybridization analysis, the stage-specific expression of PuRBOHF was higher in stone cells than in cells of other flesh tissues. Inhibitors of RBOH activity suppressed ROS accumulation and stone cell lignification in pear fruit. Moreover, transient overexpression of PuRBOHF caused significant changes in the amount of ROS and lignin that accumulated in pear fruit and flesh calli. We further showed that PuMYB169 regulates PuRBOHF expression, while PuRBOHF-derived ROS induces the transcription of PuPOD2 and PuLAC2. The findings of this study indicate that PuRBOHF-mediated ROS production, which is regulated by a lignin-related transcriptional network, is essential for monolignol polymerization and stone cell formation in pear fruit.

SUBMITTER: Wang X

PROVIDER: S-EPMC8633289 | biostudies-literature |

REPOSITORIES: biostudies-literature

ACCESS DATA

Json Xml

Similar Datasets

PbrmiR397a regulates lignification during stone cell development in pear fruit.

Project description:Lignified stone cells substantially reduce fruit quality. Therefore, it is desirable to inhibit stone cell development using genetic technologies. However, the molecular mechanisms regulating lignification are poorly understood in fruit stone cells. In this study, we have shown that microRNA (miR) miR397a regulates fruit cell lignification by inhibiting laccase (LAC) genes that encode key lignin biosynthesis enzymes. Transient overexpression of PbrmiR397a, which is the miR397a of Chinese pear (Pyrus bretschneideri), and simultaneous silencing of three LAC genes reduced the lignin content and stone cell number in pear fruit. A single nucleotide polymorphism (SNP) identified in the promoter of the PbrmiR397a gene was found to associate with low levels of fruit lignin, after analysis of the genome sequences of sixty pear varieties. This SNP created a TCA element that responded to salicylic acid to induce gene expression as confirmed using a cell-based assay system. Furthermore, stable overexpression of PbrmiR397a in transgenic tobacco plants reduced the expression of target LAC genes and decreased the content of lignin but did not change the ratio of syringyl- and guaiacyl-lignin monomers. Consistent with reduction in lignin content, the transgenic plants showed fewer numbers of vessel elements and thinner secondary walls in the remaining elements compared to wild-type control plants. This study has advanced our understanding of the regulation of lignin biosynthesis and provided useful molecular genetic information for improving pear fruit quality.

| S-EPMC6330545 | biostudies-literature

PbCSE1 promotes lignification during stone cell development in pear (Pyrus bretschneideri) fruit.

Project description:Pear [Pyrus bretschneideri cv. Dangshan Su] fruit quality is not always satisfactory owing to the presence of stone cells, and lignin is the main component of stone cells in pear fruits. Caffeoyl shikimate esterase (CSE) is a key enzyme in the lignin biosynthesis. Although CSE-like genes have been isolated from a variety of plant species, their orthologs are not characterized in pear. In this study, the CSE gene family (PbCSE) from P. bretschneideri was identified. According to the physiological data and quantitative RT-PCR (qRT-PCR), PbCSE1 was associated with lignin deposition and stone cell formation. The overexpression of PbCSE1 increased the lignin content in pear fruits. Relative to wild-type (WT) Arabidopsis, the overexpression of PbCSE1 delayed growth, increased the lignin deposition and lignin content in stems. Simultaneously, the expression of lignin biosynthetic genes were also increased in pear fruits and Arabidopsis. These results demonstrated that PbCSE1 plays an important role in cell lignification and will provide a potential molecular strategy to improve the quality of pear fruits.

| S-EPMC8093294 | biostudies-literature

PbMC1a/1b regulates lignification during stone cell development in pear (Pyrus bretschneideri) fruit.

Project description:Programmed cell death (PCD) and secondary cell wall (SCW) thickening in pear fruit are accompanied by the deposition of cellulose and lignin to form stone cells. Metacaspase is an important protease for development, tissue renewal and PCD. The understanding of the molecular mechanism whereby pear (Pyrus) metacaspase promotes PCD and cell wall lignification is still limited. In this study, the Metacaspases gene family (PbMCs) from P. bretschneideri was identified. PbMC1a/1b was associated with lignin deposition and stone cell formation by physiological data, semiquantitative real-time polymerase chain reaction (RT-PCR) and quantitative RT-PCR (qRT-PCR). Relative to wild-type (WT) Arabidopsis, the overexpression of PbMC1a/1b increased lignin deposition and delayed growth, thickened the cell walls of vessels, xylary fibers and interfascicular fibers, and increased the expression of lignin biosynthetic genes. Yeast two-hybrid (Y2H), bimolecular fluorescence complementation (BiFC) and GST pull-down assays indicated that the PbMC1a/1b protein physically interacted with PbRD21. Simultaneously, the transient expression of PbMC1a/1b and PbRD21 led to significant changes in the expression of genes and lignin contents in pear fruits and flesh calli. These results indicate that PbMC1a/1b plays an important role in cell wall lignification, possibly by interacting with PbRD21 to increase the mRNA levels of some lignin synthesis-associated genes and promote the formation of stone cells in pear fruit.

| S-EPMC7193627 | biostudies-literature

The Peptide PbrPSK2 From Phytosulfokine Family Induces Reactive Oxygen Species (ROS) Production to Regulate Pear Pollen Tube Growth.

Project description:Phytosulfokines (PSKs) are plant peptide growth factors that participate in multiple biological processes, including cell elongation and immune signaling. However, little is known about PSKs in Rosaceae species. Here, we identified 10 PSK genes in pear (Pyrus bretschneideri), 11 in apple (Malus × domestica), four in peach (Prunus persica), six in strawberry (Fragaria vesca), and five in Chinese plum (Prunus mume). In addition, we undertook comparative analysis of the PSK gene family in pear and the four other species. Evolutionary analysis indicated that whole genome duplication events (WGD) may have contributed to the expansion of the PSK gene family in Rosaceae. Transcriptomes, reverse transcription-PCR and quantitative real-time-PCR analyses were undertaken to demonstrate that PbrPSK2 is highly expressed in pear pollen. In addition, by adding purified E. coli-expressed PbrPSK2 to pollen and using an antisense oligonucleotide approach, we showed that PbrPSK2 can promote pear pollen tube elongation in a dose-dependent manner. Furthermore, PbrPSK2 was found to mediate the production of reactive oxygen species to regulate pear pollen tube growth.

| S-EPMC7734187 | biostudies-literature

CsWRKY25 Improves Resistance of Citrus Fruit to Penicillium digitatum via Modulating Reactive Oxygen Species Production.

Project description:WRKY transcription factors (TFs) play crucial roles in the regulation of biotic stress. Citrus is the most productive fruit in the world. It is of great value to investigate the regulatory molecular mechanism of WRKYs in improving disease resistance. In this research, the transcription level of CsWRKY25 was upregulated in P. digitatum infected citrus peel, and CsWRKY25 activated the expression of three target genes (RbohB, RbohD, and PR10). Besides, the Agrobacterium-mediated transient overexpression of CsWRKY25 has also been shown to enhance resistance to P. digitatum in citrus, and caused the accumulation of hydrogen peroxide and lignin. The accumulation of ROS also activated the antioxidant system, the catalase (CAT), peroxidase (POD), and cinnamyl alcohol dehydrogenase (CAD) genes were significant upregulated, leading to activation of antioxidant enzymes. In addition, the up-regulated expression of MPK5 and MPK6 genes suggested that the regulatory role of CsWRKY25 might be related to the phosphorylation process. In conclusion, CsWRKY25 could enhance the resistance to P. digitatum via modulating ROS production and PR genes in citrus peel.

| S-EPMC8784754 | biostudies-literature

Autophagy proteins control goblet cell function by potentiating reactive oxygen species production.

Project description:Delivery of granule contents to epithelial surfaces by secretory cells is a critical physiologic process. In the intestine, goblet cells secrete mucus that is required for homeostasis. Autophagy proteins are required for secretion in some cases, though the mechanism and cell biological basis for this requirement remain unknown. We found that in colonic goblet cells, proteins involved in initiation and elongation of autophagosomes were required for efficient mucus secretion. The autophagy protein LC3 localized to intracellular multi-vesicular vacuoles that were consistent with a fusion of autophagosomes and endosomes. Using cultured intestinal epithelial cells, we found that NADPH oxidases localized to and enhanced the formation of these LC3-positive vacuoles. Both autophagy proteins and endosome formation were required for maximal production of reactive oxygen species (ROS) derived from NADPH oxidases. Importantly, generation of ROS was critical to control mucin granule accumulation in colonic goblet cells. Thus, autophagy proteins can control secretory function through ROS, which is in part generated by LC3-positive vacuole-associated NADPH oxidases. These findings provide a novel mechanism by which autophagy proteins can control secretion.

| S-EPMC3981139 | biostudies-literature

Endothelial cell-specific reactive oxygen species production increases susceptibility to aortic dissection.

Project description:BackgroundIncreased production of reactive oxygen species (ROS) throughout the vascular wall is a feature of cardiovascular disease states, but therapeutic strategies remain limited by our incomplete understanding of the role and contribution of specific vascular cell ROS to disease pathogenesis. To investigate the specific role of endothelial cell (EC) ROS in the development of structural vascular disease, we generated a mouse model of endothelium-specific Nox2 overexpression and tested the susceptibility to aortic dissection after angiotensin II (Ang II) infusion.Methods and resultsA specific increase in endothelial ROS production in Nox2 transgenic mice was sufficient to cause Ang II-mediated aortic dissection, which was never observed in wild-type mice. Nox2 transgenic aortas had increased endothelial ROS production, endothelial vascular cell adhesion molecule-1 expression, matrix metalloproteinase activity, and CD45(+) inflammatory cell infiltration. Conditioned media from Nox2 transgenic ECs induced greater Erk1/2 phosphorylation in vascular smooth muscle cells compared with wild-type controls through secreted cyclophilin A (CypA). Nox2 transgenic ECs (but not vascular smooth muscle cells) and aortas had greater secretion of CypA both at baseline and in response to Ang II stimulation. Knockdown of CypA in ECs abolished the increase in vascular smooth muscle cell Erk1/2 phosphorylation conferred by EC conditioned media, and preincubation with CypA augmented Ang II-induced vascular smooth muscle cell ROS production.ConclusionsThese findings demonstrate a pivotal role for EC-derived ROS in the determination of the susceptibility of the aortic wall to Ang II-mediated aortic dissection. ROS-dependent CypA secretion by ECs is an important signaling mechanism through which EC ROS regulate susceptibility of structural components of the aortic wall to aortic dissection.

| S-EPMC5357047 | biostudies-literature

RIP2 promotes FcγR-mediated reactive oxygen species production.

Project description:Receptor-interacting protein 2 (RIP2) is a kinase that mediates signaling downstream of the bacterial peptidoglycan sensors NOD1 and NOD2. Genetic loss or pharmaceutical inhibition of RIP2 has been shown to be beneficial in multiple inflammatory disease models with the effects largely attributed to reducing proinflammatory signaling downstream of peptidoglycan recognition. However, given the widespread expression of this kinase and its reported interactions with numerous other proteins, it is possible that RIP2 may also function in roles outside of peptidoglycan sensing. In this work, we show that RIP2 undergoes tyrosine phosphorylation and activation in response to engagement of the Fc γ receptor (FcγR). Using bone marrow-derived macrophages from WT and RIP2-KO mice, we show that loss of RIP2 leads to deficient FcγR signaling and reactive oxygen species (ROS) production upon FcγR cross-linking without affecting cytokine secretion, phagocytosis, or nitrate/nitrite production. The FcγR-induced ROS response was still dependent on NOD2, as macrophages deficient in this receptor showed similar defects. Mechanistically, we found that different members of the Src family kinases (SFKs) can promote RIP2 tyrosine phosphorylation and activation. Altogether, our findings suggest that RIP2 is functionally important in pathways outside of bacterial peptidoglycan sensing and that involvement in such pathways may depend on the actions of SFKs. These findings will have important implications for future therapies designed to target this kinase.

| S-EPMC6664193 | biostudies-literature

Indoxyl sulfate stimulates angiogenesis by regulating reactive oxygen species production via CYP1B1

Project description:Introduction: Indoxyl sulfate (IS) is an accumulated protein-bound uremic toxin found in patients with kidney disease. Although it is known that IS impairs the vascular endothelium, the precise underlying mechanism remains unclear. Methods: We performed RNA sequencing in human umbilical vein endothelial cells (HUVECs) that were treated with either IS or control medium. Gene enrichment analyses were performed based on differentially expressed genes. We further examined the main enriched biological processes at the functional level. Results: We identified 1,293 genes that were affected in IS-treated HUVECs when compared to control and gene enrichment analysis indicated altered vascular formation and cell metabolism. We observed decreased viability and increased cell senescence due to IS treatment at the functional level. Furthermore, we demonstrated that IS exposure of HUVECs promoted angiogenesis as shown by the increase in total tubule length in a 3D HUVECs/pericytes co-culture assay. We also observed an increase in ROS production in IS-treated endothelial cells. Notably, the pro-angiogenic response of IS and the increased ROS production were abolished when CYP1B1, one of the main target genes that was upregulated by IS, was silenced. Conclusion: IS promotes angiogenesis and CYP1B1 is an important factor in IS-activated angiogenic response.

2019-09-18 | GSE132410 | GEO

Reactive oxygen species oxidize STING and suppress interferon production.

Project description:Reactive oxygen species (ROS) are by-products of cellular respiration that can promote oxidative stress and damage cellular proteins and lipids. One canonical role of ROS is to defend the cell against invading bacterial and viral pathogens. Curiously, some viruses, including herpesviruses, thrive despite the induction of ROS, suggesting that ROS are beneficial for the virus. However, the underlying mechanisms remain unclear. Here, we found that ROS impaired interferon response during murine herpesvirus infection and that the inhibition occurred downstream of cytoplasmic DNA sensing. We further demonstrated that ROS suppressed the type I interferon response by oxidizing Cysteine 147 on murine stimulator of interferon genes (STING), an ER-associated protein that mediates interferon response after cytoplasmic DNA sensing. This inhibited STING polymerization and activation of downstream signaling events. These data indicate that redox regulation of Cysteine 147 of mouse STING, which is equivalent to Cysteine 148 of human STING, controls interferon production. Together, our findings reveal that ROS orchestrates anti-viral immune responses, which can be exploited by viruses to evade cellular defenses.

| S-EPMC7473769 | biostudies-literature

OmicsDI is part of the ELIXIR infrastructure

OmicsDI is an Elixir interoperability service. Learn more ›

OmicsDI Databases

PRIDE
PeptideAtlas
MassIVE
JPOST Repository
Physiome Model Repository

EGA
EVA
ENA
LINCS
PAXDB
Cell Collective

MetaboLights
Metabolomics Workbench
MetabolomeExpress
GNPS
BioModels
FAIRDOMHub

ArrayExpress
dbGaP
ExpressionAtlas
GEO
NODE

Information

Databases
Help
API
Contact us
Code on GitHub
Terms of use
Submit Data