PROSTAGLANDIN MEDIATES DOWN-REGULATION OF PHENOLOXIDASE ACTIVATION OFSpodoptera exiguaVIA PLASMATOCYTE-SPREADING PEPTIDE-BINDING PROTEIN

2014 ◽  
Vol 85 (4) ◽  
pp. 234-247 ◽  
Author(s):  
Jiyeong Park ◽  
Yonggyun Kim
Keyword(s):  
Binding Protein ◽  
Peptide Binding ◽  
Down Regulation

Escherichia coli Peptide Binding Protein OppA Has a Preference for Positively Charged Peptides

2011 ◽  
Vol 414 (1) ◽  
pp. 75-85 ◽  
Author(s):  
M.M. Klepsch ◽  
M. Kovermann ◽  
C. Löw ◽  
J. Balbach ◽  
H.P. Permentier ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Binding Protein ◽  
Peptide Binding ◽  
Charged Peptides ◽  
Positively Charged

CHMP2B regulates TDP-43 phosphorylation and cytotoxicity independent of autophagy via CK1

2021 ◽  
Vol 221 (1) ◽  
Author(s):  
Xue Deng ◽  
Xing Sun ◽  
Wenkai Yue ◽  
Yongjia Duan ◽  
Rirong Hu ◽  
...  
Keyword(s):  
Mammalian Cells ◽  
Rna Binding ◽  
Binding Protein ◽  
Rna Binding Protein ◽  
Down Regulation ◽  
Protein Levels ◽  
Modifying Effect

The ESCRT protein CHMP2B and the RNA-binding protein TDP-43 are both associated with ALS and FTD. The pathogenicity of CHMP2B has mainly been considered a consequence of autophagy–endolysosomal dysfunction, whereas protein inclusions containing phosphorylated TDP-43 are a pathological hallmark of ALS and FTD. Intriguingly, TDP-43 pathology has not been associated with the FTD-causing CHMP2BIntron5 mutation. In this study, we identify CHMP2B as a modifier of TDP-43–mediated neurodegeneration in a Drosophila screen. Down-regulation of CHMP2B reduces TDP-43 phosphorylation and toxicity in flies and mammalian cells. Surprisingly, although CHMP2BIntron5 causes dramatic autophagy dysfunction, disturbance of autophagy does not alter TDP-43 phosphorylation levels. Instead, we find that inhibition of CK1, but not TTBK1/2 (all of which are kinases phosphorylating TDP-43), abolishes the modifying effect of CHMP2B on TDP-43 phosphorylation. Finally, we uncover that CHMP2B modulates CK1 protein levels by negatively regulating ubiquitination and the proteasome-mediated turnover of CK1. Together, our findings propose an autophagy-independent role and mechanism of CHMP2B in regulating CK1 abundance and TDP-43 phosphorylation.

Peptide Binding in OppA, the Crystal Structures of the Periplasmic Oligopeptide Binding Protein in the Unliganded Form and in Complex with Lysyllysine†,‡

Biochemistry ◽  
1997 ◽  
Vol 36 (32) ◽  
pp. 9747-9758 ◽  
Author(s):  
Sara H. Sleigh ◽  
Jeremy R. H. Tame ◽  
Eleanor J. Dodson ◽  
Anthony J. Wilkinson
Keyword(s):  
Crystal Structures ◽  
Binding Protein ◽  
Peptide Binding

scholarly journals Cellular retinol binding protein 1 transfection reduces proliferation and AKT-related gene expression in H460 non-small lung cancer cells

2020 ◽  
Vol 47 (9) ◽  
pp. 6879-6886
Author(s):  
Amedeo Ferlosio ◽  
Elena Doldo ◽  
Sara Agostinelli ◽  
Gaetana Costanza ◽  
Federica Centofanti ◽  
...  
Keyword(s):  
Gene Expression ◽  
Lung Cancer ◽  
Binding Protein ◽  
Retinol Binding Protein ◽  
Nsclc Cell Line ◽  
Related Gene ◽  
Down Regulation ◽  
Mammalian Expression ◽  
H460 Cells ◽  
Cellular Retinol Binding Protein

Abstract In recent years, new treatments with novel action mechanisms have been explored for advanced non-small cell lung cancer (NSCLC). Retinoids promote cancer cell differentiation and death and their trafficking and action is mediated from specific cytoplasmic and nuclear receptors, respectively. The purpose of this study was to investigate the effect of Cellular retinol binding protein-1 (CRBP-1) transfection in H460 human NSCLC cell line, normally not expressing CRBP-1. H460 cells were transfected by using a vector pTargeT Mammalian expression system carrying the whole sequence of CRBP-1 gene. For proliferation and apoptosis studies, cells were treated with different concentrations of all-trans Retinoic Acid (atRA) and retinol. AKT-related gene expression was analyzed by using western blot and Signosis array and results analysed by one-way analysis of variance (ANOVA) or by t-student test. CRBP-1+ showed reduced proliferation and viability in basal condition and after atRA treatment when compared to empty-transfected H460 cells. Reduced proliferation in CRBP-1+ H460 cells associated to the down-regulation of pAKT/pERK/pEGFR-related genes. In particular, gene array documented the down-regulation of AKT and Stat-3-related genes, including M-Tor, Akt1, Akt2, Akt3, Foxo1, p27, Jun. Restoration of CRBP-1 expression in H460 cells reduced proliferation and viability in both basal condition and after atRA treatment, likely by down-regulating AKT-related gene level. Further studies are needed to better clarify how those CRBP-1-related intracellular pathways contribute to counteract NSCLC progression in order to suggest a potential tool to improve efficacy of retinoid anti lung cancer adjuvant therapy.

Human α2-Macroglobulin Is an Osteogenic Growth Peptide-Binding Protein

Biochemistry ◽  
1997 ◽  
Vol 36 (48) ◽  
pp. 14883-14888 ◽  
Author(s):  
Hanna Gavish ◽  
Itai Bab ◽  
Alexander Tartakovsky ◽  
Michael Chorev ◽  
Nora Mansur ◽  
...  
Keyword(s):  
Binding Protein ◽  
Peptide Binding ◽  
Α2 Macroglobulin

scholarly journals hZIP1 zinc transporter down-regulation in prostate cancer involves the overexpression of ras responsive element binding protein-1 (RREB-1)

The Prostate ◽  
2011 ◽  
Vol 71 (14) ◽  
pp. 1518-1524 ◽  
Author(s):  
Jing Zou ◽  
Beatrice C. Milon ◽  
Mohamed M. Desouki ◽  
Leslie C. Costello ◽  
Renty B. Franklin
Keyword(s):  
Prostate Cancer ◽  
Binding Protein ◽  
Zinc Transporter ◽  
Down Regulation ◽  
Element Binding Protein ◽  
Responsive Element

scholarly journals Interaction Between IGF Binding Protein-3 and TGFβ in the Regulation of Adipocyte Differentiation

Endocrinology ◽  
2012 ◽  
Vol 153 (10) ◽  
pp. 4799-4807 ◽  
Author(s):  
Hasanthi C. de Silva ◽  
Sue M. Firth ◽  
Stephen M. Twigg ◽  
Robert C. Baxter
Keyword(s):  
Binding Protein ◽  
Adipogenic Differentiation ◽  
Cell Types ◽  
Inhibitory Effect ◽  
Down Regulation ◽  
Smad2 Phosphorylation ◽  
Igf Binding ◽  
Igf Binding Protein ◽  
Interfering Rna ◽  
Igfbp 3

Abstract The development of white adipose tissue involves both the hypertrophy of existing adipocytes and the proliferation and differentiation of preadipocytes. Adipogenic differentiation is inhibited by TGFβ signaling through Smad2/3, and IGF binding protein-3 (IGFBP-3) is also known to activate Smad2/3 signaling in some cell types. We previously reported that exogenous or overexpressed IGFBP-3 inhibits adipogenesis in 3T3-L1 cells, but the role of endogenous IGFBP-3 in this process, and its possible interaction with TGFβ, is not known. During 10-d adipogenic differentiation initiated by insulin, dexamethasone, and 3-isobutyl-1-methylxanthine, 3T3-L1 cells expressed increasing levels of IGFBP-3 and TGFβ1, secreting over 1000 pg/ml of both proteins. Exogenous recombinant human IGFBP-3 paralleled TGFβ1 in stimulating Smad2 phosphorylation in 3T3-L1 preadipocytes, but no additive effect was observed for the two agents. In contrast, knockdown of endogenous IGFBP-3 by small interfering RNA (siRNA) significantly impaired Smad2 activation by 0.25 ng/ml TGFβ1. Transient expression of human IGFBP-3 significantly inhibited the induction of adipogenic markers adiponectin and resistin, and the appearance of lipid droplets, but down-regulation of endogenous IGFBP-3 by siRNA had little effect on the expression of either marker during the 10-d differentiation, compared with nonsilencing control siRNA. However, down-regulation of endogenous IGFBP-3 using two different siRNA significantly reversed the inhibitory effect of TGFβ1 on both adiponectin and resistin induction. We conclude that IGFBP-3 activates inhibitory Smad signaling in 3T3-L1 cells and that endogenous IGFBP-3 modulates their adipogenic differentiation by regulating cell sensitivity towards the inhibitory effect of TGFβ.

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