scholarly journals Protease Inhibitor-Dependent Inhibition of Light-Induced Stomatal Opening

2021 ◽  
Vol 12 ◽  
Author(s):  
Tenghua Wang ◽  
Wenxiu Ye ◽  
Yin Wang ◽  
Maoxing Zhang ◽  
Yusuke Aihara ◽  
...  
Keyword(s):  
Matrix Metalloproteinase ◽  
Protease Inhibitor ◽  
Signaling Pathway ◽  
Stomatal Closure ◽  
Screening Method ◽  
Stomatal Opening ◽  
Matrix Metalloproteinase 2 ◽  
Aba Signaling ◽  
Bioinformatics Analyses ◽  
Chemical Screening

Stomata in the epidermis of plants play essential roles in the regulation of photosynthesis and transpiration. Stomata open in response to blue light (BL) by phosphorylation-dependent activation of the plasma membrane (PM) H+-ATPase in guard cells. Under water stress, the plant hormone abscisic acid (ABA) promotes stomatal closure via the ABA-signaling pathway to reduce water loss. We established a chemical screening method to identify compounds that affect stomatal movements in Commelina benghalensis. We performed chemical screening using a protease inhibitor (PI) library of 130 inhibitors to identify inhibitors of stomatal movement. We discovered 17 PIs that inhibited light-induced stomatal opening by more than 50%. Further analysis of the top three inhibitors (PI1, PI2, and PI3; inhibitors of ubiquitin-specific protease 1, membrane type-1 matrix metalloproteinase, and matrix metalloproteinase-2, respectively) revealed that these inhibitors suppressed BL-induced phosphorylation of the PM H+-ATPase but had no effect on the activity of phototropins or ABA-dependent responses. The results suggest that these PIs suppress BL-induced stomatal opening at least in part by inhibiting PM H+-ATPase activity but not the ABA-signaling pathway. The targets of PI1, PI2, and PI3 were predicted by bioinformatics analyses, which provided insight into factors involved in BL-induced stomatal opening.

scholarly journals Euodia pasteuriana Methanol Extract Exerts Anti-Inflammatory Effects by Targeting TAK1 in the AP-1 Signaling Pathway

Molecules ◽  
2020 ◽  
Vol 25 (23) ◽  
pp. 5760
Author(s):  
Jianmei Zhang ◽  
Mi-Yeon Kim ◽  
Jae Youl Cho
Keyword(s):  
Matrix Metalloproteinase ◽  
Signaling Pathway ◽  
Transforming Growth Factor ◽  
Methanol Extract ◽  
Matrix Metalloproteinase 2 ◽  
Transcriptional Level ◽  
Nuclear Fraction ◽  
Polycytidylic Acid ◽  
Matrix Metalloproteinase 1 ◽  
Anti Inflammatory

Euodia pasteuriana A. Chev. ex Guillaumin, also known as Melicope accedens (Blume) T.G. Hartley, is a herbal medicinal plant native to Vietnam. Although Euodia pasteuriana is used as a traditional medicine to treat a variety of inflammatory diseases, the pharmacological mechanisms related to this plant are unclear. This study aimed to investigate the anti-inflammatory effects of a methanol extract of Euodia pasteuriana leaves (Ep-ME) on the production of inflammatory mediators, the mRNA expression of proinflammatory genes, and inflammatory signaling activities in macrophage cell lines. The results showed that Ep-ME strongly suppressed the release of nitric oxide (NO) in RAW264.7 cells induced with lipopolysaccharide (LPS), pam3CysSerLys4 (Pam3CSK), and polyinosinic-polycytidylic acid (poly I:C) without cytotoxicity. A reverse transcription-polymerase chain reaction further confirmed that Ep-ME suppressed the expression of interleukin 6 (IL-6), matrix metalloproteinase-1 (MMP1), matrix metalloproteinase-2 (MMP2), matrix metalloproteinase-3 (MMP3), tumor necrosis factor-α (TNF-α), and matrix metalloproteinase-9 (MMP9) at the transcriptional level and reduced the luciferase activities of activator protein 1 (AP-1) reporter promoters. In addition, immunoblotting analyses of the whole lysate and nuclear fraction, as well as overexpression assays demonstrated that Ep-ME decreased the translocation of c-Jun and suppressed the activation of transforming growth factor beta-activated kinase 1 (TAK1) in the AP-1 signaling pathways. These results imply that Ep-ME could be developed as an anti-inflammatory agent that targets TAK1 in the AP-1 signaling pathway.

TRIM65 Promotes Invasion of Endometrial Stromal Cells by Activating ERK1/2/C-myc Signaling via Ubiquitination of DUSP6

2020 ◽  
Author(s):  
Ying-Ting Wu ◽  
Si-Yu Ma ◽  
Wen-Qin Sun ◽  
Wei-Wei Shen ◽  
Hui-Ting Zhu ◽  
...  
Keyword(s):  
Cell Proliferation ◽  
Matrix Metalloproteinase ◽  
Signaling Pathway ◽  
Matrix Metalloproteinase 2 ◽  
Mice Model ◽  
Integrin Β1 ◽  
Normal Endometrium ◽  
Endometrial Stromal Cells ◽  
Benign Gynecological Disease ◽  
Proliferation And Invasion

Abstract Background Endometriosis (EM) is a benign gynecological disease that shares some characteristics with malignancy, such as proliferation and invasion. So far, the pathogenesis of EM is still unclear. In this study, we investigated whether TRIM65 can play a role in the development of EM. Methods TRIM65 expression levels in eutopic, ectopic, and normal endometrium were detected by quantitative real-time PCR and Western blot. Cell proliferation and invasion of primary endometrial stromal (EMS) cells were detected by CCK-8 and Transwell analysis. The interaction between TRIM65 and DUSP6 or C-myc was measured by coimmunoprecipitation, ubiquitylation, dual luciferase, and chromatin immunoprecipitation analysis. Results We found that TRIM65 was identified as an up-regulated gene in ectopic endometrial tissues and EMS cells compared with control groups without EM. TRIM65 expression was positively correlated with the levels of p-ERK1/2, C-myc, matrix metalloproteinase-2, and integrin β1 in ectopic endometrial tissues in patients and mice. TRIM65 promoted the cell proliferation and invasion of EMS cells via the ERK1/2/C-myc pathway through ubiquitination of DUSP6. C-myc promoted TRIM65 expression through inducing TRIM65 promoter activity. Additionally, the increased expression of TRIM65, C-myc, matrix metalloproteinase-2, integrin β1, and p-ERK1/2 and the decreased expression of DUSP6 in ectopic endometrial tissues were significantly suppressed by inhibition of ERK1/2 signaling pathway in ectopic endometrial tissues in experimental mice model. Conclusion In conclusion, TRIM65 promotes invasion of ectopic EMS cells by activating a feedback loop with the ERK1/2/C-myc signaling pathway and may be a potential therapeutic target for EM.

scholarly journals Novel regulation of transpiration by sugar signals within guard cells

2012 ◽  
Author(s):  
David Granot ◽  
Sarah M. Assmann
Keyword(s):  
Abscisic Acid ◽  
Signaling Pathway ◽  
Water Loss ◽  
Stomatal Closure ◽  
Guard Cells ◽  
Feedback Mechanism ◽  
Limiting Factor ◽  
Aba Signaling ◽  
Sugar Sensing ◽  
New Discovery

Water is the major limiting factor in agriculture and stomata, composed of two guard cells and the pore they circumscribe, are the chief gates controlling plants’ water loss. The prevailing century old paradigm was that sugars act as an osmoticum in guard cells, contributing to the opening of the stomata. In contrast, we discovered that sugars close stomata and the closure is mediated by the sugar-sensing enzyme hexokinase (HXK) that triggers the abscisic acid (ABA)-signaling pathway within the guard cells. This new discovery suggests a sugar-sensing mechanism within guard cells that controls stomatal closure, and supports the existence of a stomatal feedback mechanism that coordinates photosynthesis with transpiration.

Selective processing of a follicular matrix metalloproteinase-2 isoform by human oviducal fluid

2003 ◽  
Vol 15 (3) ◽  
pp. 141 ◽  
Author(s):  
Jisoo Kim ◽  
Jiyoung Kim ◽  
Haekwon Kim ◽  
Seung-Jae Lee ◽  
Yong Dal Yoon ◽  
...  
Keyword(s):  
Matrix Metalloproteinase ◽  
Protease Inhibitor ◽  
Incubation Period ◽  
Follicular Fluid ◽  
Matrix Metalloproteinase 2 ◽  
Concomitant Increase ◽  
Human Follicular Fluid ◽  
Gelatinase Activity ◽  
Selective Processing

The present study demonstrates that a unique isoform of matrix metalloproteinase (MMP)-2 present in human follicular fluid (FF) can be processed selectively by human oviducal fluid (OF). A gelatin zymogram of untreated FF showed distinct 88-, 84- and 62-kDa gelatinases. Treatment of FF with EDTA resulted in the appearance of 110-kDa gelatinase (GA110). Most gelatinases, except for the 88- and 84-kDa gelatinases, were abolished by pretreatment with EDTA or phenanthroline, but not by pretreatment with a serine/threonine protease inhibitor. When EDTA-pretreated FF was mixed with OF, the GA110 of the FF was specifically reduced. The reduction in GA110 was dependent upon the amount of OF protein and the incubation period after mixing. Treatment of FF with aminophenylmercuric acetate reduced GA110 activity, but this reduction was accompanied by a concomitant increase of 62-kDa gelatinase activity. Anti-human MMP-2 antibody strongly reacted with both GA110 and 62-kDa gelatinases of FF, but only GA110 immunoreactivity was abolished when FF was mixed with OF. The results suggest that the GA110 of FF is an MMP-2 isoform that can be processed selectively by OF.

scholarly journals MnTE-2-PyP Attenuates TGF-β-Induced Epithelial-Mesenchymal Transition of Colorectal Cancer Cells by Inhibiting the Smad2/3 Signaling Pathway

2019 ◽  
Vol 2019 ◽  
pp. 1-11 ◽  
Author(s):  
Yu Yang ◽  
Pei Zhang ◽  
Ruicheng Yan ◽  
Qi Wang ◽  
Erhu Fang ◽  
...  
Keyword(s):  
Colorectal Cancer ◽  
Matrix Metalloproteinase ◽  
Cancer Cells ◽  
Signaling Pathway ◽  
Cancer Progression ◽  
Epithelial Mesenchymal Transition ◽  
Matrix Metalloproteinase 2 ◽  
Mesenchymal Transition ◽  
Colorectal Cancer Cells ◽  
Colorectal Cancer Progression

Background. As a key step in enhancing cancer cell invasion and metastasis, epithelial-mesenchymal transition (EMT) plays an important role in colorectal cancer progression. EMT is triggered by a variety of signaling pathways, among which the transforming growth factor β (TGF-β) signaling pathway has been implicated as a primary inducer. Accumulating evidence demonstrates that MnTE-2-PyP (chemical name: manganese(III) meso-tetrakis-(N-ethylpyridinium-2-yl), a superoxide dismutase (SOD) mimetic, inhibits TGF-β signaling; however, its ability to inhibit TGF-β-induced EMT in colorectal cancer has not yet been explored. Methods. To verify our hypothesis that MnTE-2-PyP attenuates TGF-β-induced EMT, human colorectal cancer cells were treated with TGF-β in the presence or absence of MnTE-2-PyP. Cells were analyzed by several techniques including western blotting, real-time quantitative PCR, transwell assay, and wound healing assay. Results. MnTE-2-PyP reverses cell phenotypes induced by TGF-β in colon cancer cells. MnTE-2-PyP treatment significantly reduced the expression of mesenchymal markers but maintained epithelial marker expression. Mechanistically, MnTE-2-PyP suppressed the phosphorylated Smad2/3 protein levels induced by TGF-β in SW480 cells, but MnTE-2-PyP failed to suppress TGF-β-induced Slug and Snail expression in colorectal cells. Furthermore, MnTE-2-PyP effectively suppressed TGF-β-mediated cell migration and invasion and the expression of matrix metalloproteinase 2 (MMP-2) and matrix metalloproteinase 9 (MMP-9) in colorectal cells. Conclusion. Taken together, we provide an in-depth mechanism by which MnTE-2-PyP inhibits colorectal cancer progression, supporting an important role for MnTE-2-PyP as an effective and innovative antitumor agent to enhance treatment outcomes in colorectal cancer.

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