scholarly journals Suppression of Cholangiocarcinoma Cell Growth and Proliferation by Atractylodes lancea (Thunb) DC. through ERK-Signaling Cascade

2021 ◽  
Vol 22 (11) ◽  
pp. 3633-3640
Author(s):  
Pongsakorn Martviset ◽  
Luxsana Panrit ◽  
Pathanin Chantree ◽  
Phunuch Muhamad ◽  
Kesara Na-Bangchang
Keyword(s):  
Cell Growth ◽  
Erk Signaling ◽  
Signaling Cascade ◽  
Atractylodes Lancea ◽  
Cholangiocarcinoma Cell ◽  
Cell Growth And Proliferation

scholarly journals PAS kinase is activated by direct SNF1-dependent phosphorylation and mediates inhibition of TORC1 through the phosphorylation and activation of Pbp1

2015 ◽  
Vol 26 (3) ◽  
pp. 569-582 ◽  
Author(s):  
Desiree DeMille ◽  
Bryan D. Badal ◽  
J. Brady Evans ◽  
Andrew D. Mathis ◽  
Joseph F. Anderson ◽  
...  
Keyword(s):  
Cell Growth ◽  
Binding Protein ◽  
Carbon Sources ◽  
Signaling Cascade ◽  
Nutrient Depletion ◽  
Pas Kinase ◽  
Necessary And Sufficient ◽  
Cell Growth And Proliferation

We describe the interplay between three sensory protein kinases in yeast: AMP-regulated kinase (AMPK, or SNF1 in yeast), PAS kinase 1 (Psk1 in yeast), and the target of rapamycin complex 1 (TORC1). This signaling cascade occurs through the SNF1-dependent phosphorylation and activation of Psk1, which phosphorylates and activates poly(A)- binding protein binding protein 1 (Pbp1), which then inhibits TORC1 through sequestration at stress granules. The SNF1-dependent phosphorylation of Psk1 appears to be direct, in that Snf1 is necessary and sufficient for Psk1 activation by alternate carbon sources, is required for altered Psk1 protein mobility, is able to phosphorylate Psk1 in vitro, and binds Psk1 via its substrate-targeting subunit Gal83. Evidence for the direct phosphorylation and activation of Pbp1 by Psk1 is also provided by in vitro and in vivo kinase assays, including the reduction of Pbp1 localization at distinct cytoplasmic foci and subsequent rescue of TORC1 inhibition in PAS kinase–deficient yeast. In support of this signaling cascade, Snf1-deficient cells display increased TORC1 activity, whereas cells containing hyperactive Snf1 display a PAS kinase–dependent decrease in TORC1 activity. This interplay between yeast SNF1, Psk1, and TORC1 allows for proper glucose allocation during nutrient depletion, reducing cell growth and proliferation when energy is low.

scholarly journals Enhanced Myc Expression in Silkworm Silk Gland Promotes DNA Replication and Silk Production

Insects ◽  
2021 ◽  
Vol 12 (4) ◽  
pp. 361
Author(s):  
Wenliang Qian ◽  
Yan Yang ◽  
Zheng Li ◽  
Yuting Wu ◽  
Xuechuan He ◽  
...  
Keyword(s):  
Dna Replication ◽  
Cell Growth ◽  
Silk Gland ◽  
Biological Functions ◽  
Gland Cells ◽  
Silk Production ◽  
Myc Gene ◽  
Cell Growth And Proliferation ◽  
Silkworm Silk ◽  
Posterior Silk Gland

Silkworm is an economically important insect that synthetizes silk proteins for silk production in silk gland, and silk gland cells undergo endoreplication during larval period. Transcription factor Myc is essential for cell growth and proliferation. Although silkworm Myc gene has been identified previously, its biological functions in silkworm silk gland are still largely unknown. In this study, we examined whether enhanced Myc expression in silk gland could facilitate cell growth and silk production. Based on a transgenic approach, Myc was driven by the promoter of the fibroin heavy chain (FibH) gene to be successfully overexpressed in posterior silk gland. Enhanced Myc expression in the PSG elevated FibH expression by about 20% compared to the control, and also increased the weight and shell rate of the cocoon shell. Further investigation confirmed that Myc overexpression increased nucleus size and DNA content of the PSG cells by promoting the transcription of the genes involved in DNA replication. Therefore, we conclude that enhanced Myc expression promotes DNA replication and silk protein expression in endoreplicating silk gland cells, which subsequently raises silk yield.

microRNA 21-mediated suppression of sprouty1 by Pokemon affects liver cancer cell growth and proliferation

2013 ◽  
Vol 114 (7) ◽  
pp. 1625-1633 ◽  
Author(s):  
Xiu-Li Jin ◽  
Qin-Sheng Sun ◽  
Feng Liu ◽  
Hong-Wei Yang ◽  
Min Liu ◽  
...  
Keyword(s):  
Cell Growth ◽  
Liver Cancer ◽  
Cancer Cell ◽  
Liver Cancer Cell ◽  
Cancer Cell Growth ◽  
Cell Growth And Proliferation

scholarly journals Probiotic-Derived Polyphosphate Accelerates Intestinal Epithelia Wound Healing through Inducing Platelet-Derived Mediators

2021 ◽  
Vol 2021 ◽  
pp. 1-14
Author(s):  
Shotaro Isozaki ◽  
Hiroaki Konishi ◽  
Mikihiro Fujiya ◽  
Hiroki Tanaka ◽  
Yuki Murakami ◽  
...  
Keyword(s):  
Wound Healing ◽  
Cell Growth ◽  
Epithelial Cell ◽  
Intestinal Inflammation ◽  
Light Transmission ◽  
Platelet Rich Plasma ◽  
Mitogen Activated Protein Kinase ◽  
Erk Signaling ◽  
Intestinal Barrier Function ◽  
Ki 67

Inflammatory bowel disease (IBD), such as ulcerative colitis (UC) and Crohn’s disease (CD), is an intractable intestinal inflammation associated with the disruption of the intestinal mucosa. We previously demonstrated that Lactobacillus brevis-derived long-chain polyphosphate (poly P) improved the intestinal barrier function by the upregulation of cell adhesion and relieved intestinal inflammation, thereby exerting a curing effect on colitis in vitro, in vivo, and in an investigator-initiated clinical study of UC. However, how poly P improves mucosal defects induced by intestinal inflammation has not been elucidated. In this study, we detected the accumulation of platelets in inflamed tissues induced by poly P in a dextran sulfate sodium- (DSS-) induced colitis mouse model. A light transmission aggregometry analysis and scanning electron microscopy showed that poly P promoted the platelet aggregation. An SRB assay and ki-67 staining showed that the supernatant of poly P-treated platelet-rich plasma (PRP) increased intestinal epithelial cell growth. A wound healing assay showed that the supernatant of poly P-treated PRP, but not poly P itself, accelerated wound healing. A Western blotting analysis indicated that mitogen-activated protein kinase activation was induced by the supernatant of poly P-treated human PRP in the epithelial cells and its wound healing effect was significantly decreased by the inhibition of ERK signaling. These data suggested that platelet-derived mediators induced by poly P improved intestinal inflammation through the promotion of epithelial cell growth by the activation of the ERK signaling pathway. The mechanism is a novel host-microbe interaction through mammalian platelet-derived mediators induced by bacterial molecules.

scholarly journals The mechanism of full activation of tumor suppressor PTEN at the phosphatidylinositol-enriched membrane

2021 ◽  
Author(s):  
Hyunbum Jang ◽  
Iris Nira Smith ◽  
Charis Eng ◽  
Ruth Nussinov
Keyword(s):  
Drug Discovery ◽  
Cell Growth ◽  
Tumor Suppressor ◽  
Full Length ◽  
Detailed Mechanism ◽  
Explicit Solvent ◽  
Signaling Lipids ◽  
Cell Growth And Proliferation ◽  
First Time ◽  
Full Activation

AbstractTumor suppressor PTEN dephosphorylates signaling lipid PIP3 produced by PI3Ks. Abundant PIP3 promotes cell growth and proliferation. PTEN is the second most highly mutated protein in cancer and is drugless. The detailed mechanism at the membrane of this pivotal phosphatase is unknown hindering understanding and drug discovery. Here for the first time, exploiting explicit solvent simulations, we tracked full-length PTEN trafficking from the cytosol to the membrane, its interaction with membranes composed of zwitterionic phosphatidylcholine and anionic phosphatidylserine and phosphatidylinositol, including signaling lipids PIP2 and PIP3, and moving away from the zwitterionic and getting absorbed onto the anionic membrane that harbors the PIP3. PIP3 then allosterically unfolds the N-terminal PIP2 binding domain, translocating it to the membrane where its polybasic motif interacts with PIP2, localizing on microdomains enriched in signaling lipids, as PI3K does. Finally, we determined PTEN catalytic action at the membrane, all in line with available experimental observations.

scholarly journals RAS Function in cancer cells: translating membrane biology and biochemistry into new therapeutics

2020 ◽  
Vol 477 (15) ◽  
pp. 2893-2919
Author(s):  
Walaa E. Kattan ◽  
John F. Hancock
Keyword(s):  
Plasma Membrane ◽  
Cell Growth ◽  
Cancer Cells ◽  
Special Focus ◽  
Ras Proteins ◽  
Membrane Interactions ◽  
Multiple Methods ◽  
Membrane Biology ◽  
The Past ◽  
Cell Growth And Proliferation

The three human RAS proteins are mutated and constitutively activated in ∼20% of cancers leading to cell growth and proliferation. For the past three decades, many attempts have been made to inhibit these proteins with little success. Recently; however, multiple methods have emerged to inhibit KRAS, the most prevalently mutated isoform. These methods and the underlying biology will be discussed in this review with a special focus on KRAS-plasma membrane interactions.

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