scholarly journals Histone deacetylase (Rpd3) regulates Drosophila early brain development via regulation of Tailless

Open Biology ◽  
2020 ◽  
Vol 10 (9) ◽  
pp. 200029
Author(s):  
Paromita Das ◽  
Manika Pal Bhadra
Keyword(s):  
Brain Development ◽  
Histone Deacetylase ◽  
Growth Factor Receptor ◽  
Larval Brain ◽  
Egfr Expression ◽  
Neural Cell Adhesion ◽  
Epidermal Growth ◽  
Embryonic Segmentation ◽  
Fine Tune

Tailless is a committed transcriptional repressor and principal regulator of the brain and eye development in Drosophila . Rpd3, the histone deacetylase, is an established repressor that interacts with co-repressors like Sin3a, Prospero, Brakeless and Atrophin. This study aims at deciphering the role of Rpd3 in embryonic segmentation and larval brain development in Drosophila . It delineates the mechanism of Tailless regulation by Rpd3 , along with its interacting partners. There was a significant reduction in Tailless in Rpd3 heteroallelic mutant embryos, substantiating that Rpd3 is indispensable for the normal Tailless expression. The expression of the primary readout, Tailless was correlative to the expression of the neural cell adhesion molecule homologue, Fascilin2 (Fas2). Rpd3 also aids in the proper development of the mushroom body. Both Tailless and Fas2 expression are reported to be antagonistic to the epidermal growth factor receptor (EGFR) expression. The decrease in Tailless and Fas2 expression highlights that EGFR is upregulated in the larval mutants, hindering brain development. This study outlines the axis comprising Rpd3, dEGFR, Tailless and Fas2, which interact to fine-tune the early segmentation and larval brain development. Therefore, Rpd3 along with Tailless has immense significance in early embryogenesis and development of the larval brain.

scholarly journals Epidermal growth factor receptor expression and signaling are essential in glutamine's cytoprotective mechanism in heat-stressed intestinal epithelial-6 cells

2013 ◽  
Vol 304 (5) ◽  
pp. G543-G552 ◽  
Author(s):  
Stefanie Niederlechner ◽  
Christine Baird ◽  
Benjamin Petrie ◽  
Erhard Wischmeyer ◽  
Paul E. Wischmeyer
Keyword(s):  
Small Interfering Rna ◽  
Growth Factor Receptor ◽  
Intestinal Epithelial ◽  
Egfr Signaling ◽  
Cellular Protection ◽  
Akt Phosphorylation ◽  
Egfr Expression ◽  
Epidermal Growth ◽  
Interfering Rna

Epidermal growth factor receptor (EGFR) expression and signaling can induce cellular protection after intestinal inflammation. l-Glutamine (GLN) is known to prevent apoptosis after intestinal injury by activating MAPK and phosphatidylinositol 3-kinase (PI3-K)/Akt pathways. However, the role of EGFR expression and signaling in GLN-mediated cellular protection in intestinal epithelial-6 (IEC-6) cells after heat stress (HS) is unknown. To address the role of EGFR in GLN-mediated protection, IEC-6 cells were treated with GLN in the presence or absence of EGFR small interfering RNA, the EGFR tyrosine kinase inhibitor AG1478, the ERK1/2 inhibitor PD98059, the p38MAPK inhibitor SB203580, or the PI3-K/Akt inhibitor LY294002 under basal and HS conditions. GLN-mediated cell survival was measured using 3-(4,5-dimethylthiazol-2-yl)-5-(3-carboxymethoxyphenyl)-2-(4-sulfophenyl)-2H-tetrazolium assay. Phosphorylated and/or total levels of EGFR, cleaved caspase-3, poly(ADP-ribose) polymerase-1, ERK1/2, p38MAPK, and Akt were assessed by Western blotting. We showed that HS induced a decrease in total, cytoplasmic, and nuclear EGFR levels in IEC-6 cells, which was prevented by GLN supplementation, leading to attenuated apoptosis via EGFR small interfering RNA. Furthermore, the protective effect of GLN was lessened by AG1478, PD98059, and LY294002 but was not affected by SB203580. AG1478 attenuated GLN-mediated increases in ERK1/2 and decreases in p38MAPK phosphorylation. However, AG1478 had no effect on GLN-mediated augmentations in Akt phosphorylation. In summary, EGFR expression was important in the protective mechanism of GLN, as well as GLN-mediated activation of EGFR tyrosine kinase activity. GLN-mediated EGFR signaling activated ERK1/2 and decreased p38MAPK signaling. However, GLN-mediated Akt phosphorylation after HS seems to be independent of EGFR signaling.

scholarly journals Bi-Functional Radiotheranostics of 188Re-Liposome-Fcy-hEGF for Radio- and Chemo-Therapy of EGFR-Overexpressing Cancer Cells

2021 ◽  
Vol 22 (4) ◽  
pp. 1902 ◽  
Author(s):  
Yi-Shu Huang ◽  
Wei-Chuan Hsu ◽  
Chien-Hong Lin ◽  
Sheng-Nan Lo ◽  
Chu-Nian Cheng ◽  
...  
Keyword(s):  
Fusion Protein ◽  
Cancer Cells ◽  
Tumor Cells ◽  
Cytotoxic Effect ◽  
Cytosine Deaminase ◽  
Growth Factor Receptor ◽  
Size Exclusion ◽  
Specific Therapy ◽  
Egfr Expression ◽  
Epidermal Growth

Epidermal growth factor receptor (EGFR) specific therapeutics is of great importance in cancer treatment. Fcy-hEGF fusion protein, composed of yeast cytosine deaminase (Fcy) and human EGF (hEGF), is capable of binding to EGFR and enzymatically convert 5-fluorocytosine (5-FC) to 1000-fold toxic 5-fluorocuracil (5-FU), thereby inhibiting the growth of EGFR-expressing tumor cells. To develop EGFR-specific therapy, 188Re-liposome-Fcy-hEGF was constructed by insertion of Fcy-hEGF fusion protein onto the surface of liposomes encapsulating of 188Re. Western blotting, MALDI-TOF, column size exclusion and flow cytometry were used to confirm the conjugation and bio-activity of 188Re-liposome-Fcy-hEGF. Cell lines with EGFR expression were subjected to treat with 188Re-liposome-Fcy-hEGF/5-FC in the presence of 5-FC. The 188Re-liposome-Fcy-hEGF/5-FC revealed a better cytotoxic effect for cancer cells than the treatment of liposome-Fcy-hEGF/5-FC or 188Re-liposome-Fcy-hEGF alone. The therapeutics has radio- and chemo-toxicity simultaneously and specifically target to EGFR-expression tumor cells, thereby achieving synergistic anticancer activity.

scholarly journals Role of epidermal growth factor receptor degradation in gemcitabine-mediated cytotoxicity

Oncogene ◽  
2006 ◽  
Vol 26 (23) ◽  
pp. 3431-3439 ◽  
Author(s):  
F Y Feng ◽  
S Varambally ◽  
S A Tomlins ◽  
P Y Chun ◽  
C A Lopez ◽  
...  
Keyword(s):  
Epidermal Growth Factor Receptor ◽  
Growth Factor ◽  
Epidermal Growth Factor ◽  
Growth Factor Receptor ◽  
Epidermal Growth
Sign in / Sign up

Export Citation Format

Share Document