Role of Phospholipid Metabolites in the Cell Cycle Delay Caused by Epidermal Growth Factor at the Transition from G2-Phase to Mitosis in A431 Cells

1993 ◽  
pp. 537-540
Author(s):  
M. Kaszkin ◽  
V. Kinzel
Keyword(s):  
Cell Cycle ◽  
Growth Factor ◽  
Epidermal Growth Factor ◽  
A431 Cells ◽  
Cell Cycle Delay ◽  
Epidermal Growth ◽  
G2 Phase

scholarly journals LINC00037 Inhibits Proliferation of Renal Cell Carcinoma Cells in an Epidermal Growth Factor Receptor-Dependent Way

2018 ◽  
Vol 45 (2) ◽  
pp. 523-536 ◽  
Author(s):  
Xiaohui Gong ◽  
Xianjin Du ◽  
Yong Xu ◽  
Wenze Zheng
Keyword(s):  
Cell Cycle ◽  
Renal Cell Carcinoma ◽  
Cell Proliferation ◽  
Epidermal Growth Factor Receptor ◽  
Growth Factor ◽  
Epidermal Growth Factor ◽  
Growth Factor Receptor ◽  
Epidermal Growth

Background/Aims: LINC00037 has previously been reported to be up-regulated in clear cell renal cell carcinoma (ccRCC), however, the underlying mechanism remained unknown. In this study, we designed to investigate the functional role of LINC00037 in ccRCC Methods: LINC00037 knockdown and re-expressing 786-O and A498 cells were established. CCK8 assay and EdU assay were performed to evaluate the proliferation rates of ccRCC cells. Flow cytometry assay was performed to detect the cell apoptosis and cell cycle. Subcutaneous injection xenotransplantation mouse model was used to observe the role of LINC00037 in tumor growth in vivo. Mass spectrometry (MS) was performed to find the interacting partner of LINC00037 and RNA immunoprecipitation (RIP) was carried out to validate their interaction. Results: We found that knockdown of LINC00037 resulted in inhibited cell proliferation with activated apoptosis and cell cycle arrest in vitro. Over-expression of LINC00037 in LINC00037 knockdown cells restored and enhanced cell proliferation. In vivo mouse model indicated reduced tumor progression by LINC00037 depletion and promoted tumor progression by LINC00037 overexpression. LINC00037 could bind to epidermal growth factor receptor (EGFR) and increase the protein level of EGFR. Conclusion: LINC00037 could inhibit proliferation of ccRCC in an epidermal growth factor receptor-dependent way.

scholarly journals Rapid uptake of tyrphostin into A431 human epidermoid cells is followed by delayed inhibition of epidermal growth factor (EGF)-stimulated EGF receptor tyrosine kinase activity.

1991 ◽  
Vol 11 (5) ◽  
pp. 2697-2703 ◽  
Author(s):  
C A Faaland ◽  
F H Mermelstein ◽  
J Hayashi ◽  
J D Laskin
Keyword(s):  
Cell Cycle ◽  
Growth Factor ◽  
Epidermal Growth Factor ◽  
Tyrosine Kinase ◽  
Receptor Tyrosine Kinase ◽  
Kinase Activity ◽  
Egf Receptor ◽  
Tyrosine Kinase Activity ◽  
A431 Cells ◽  
Epidermal Growth

Treatment of A431 human epidermoid cells with epidermal growth factor (EGF; 20 nM) results in decreased proliferation. This is associated with blockage of the cells in the S and/or G2 phases of the cell cycle. We found that tyrphostin, a putative tyrosine kinase inhibitor, in the range of 50 to 100 microM, partially reversed the growth-inhibitory and cell cycle changes induced by EGF. By using high-pressure liquid chromatography with electrochemical detection, we found that tyrphostin was readily incorporated into A431 cells, reaching maximal levels within 1 h. Although tyrphostin (50 to 100 microM) had no effect on high-affinity binding of EGF to its receptor in A431 cells for up to 24 h, the compound partially inhibited EGF-stimulated EGF receptor tyrosine kinase activity. However, this effect was evident only after prolonged treatment of the cells (4 to 24 h) with the drug. When the peak intracellular concentration of tyrphostin occurred (1 h), no inhibition of tyrosine kinase activity was observed. After both 1 and 24 h, tyrphostin was a less effective inhibitor of tyrosine kinase activity than the potent tumor promoter 12-O-tetradecanoyl phorbol-13-acetate, which almost completely blocked EGF receptor autophosphorylation. On the basis of our data, we hypothesize that tyrphostin is not a competitive inhibitor of the EGF receptor tyrosine kinase in intact cells and that it functions by an indirect mechanism.

Role of epidermal growth factor-stimulated protein kinase in control of proliferation of A431 cells

1982 ◽  
Vol 19 (3) ◽  
pp. 249-257 ◽  
Author(s):  
Gordon N. Gill ◽  
Janice E. Buss ◽  
Cheri S. Lazar ◽  
Aliza Lifshitz ◽  
Jonathan A. Cooper
Keyword(s):  
Growth Factor ◽  
Protein Kinase ◽  
Epidermal Growth Factor ◽  
A431 Cells ◽  
Epidermal Growth

Rapid uptake of tyrphostin into A431 human epidermoid cells is followed by delayed inhibition of epidermal growth factor (EGF)-stimulated EGF receptor tyrosine kinase activity

1991 ◽  
Vol 11 (5) ◽  
pp. 2697-2703
Author(s):  
C A Faaland ◽  
F H Mermelstein ◽  
J Hayashi ◽  
J D Laskin
Keyword(s):  
Cell Cycle ◽  
Growth Factor ◽  
Epidermal Growth Factor ◽  
Tyrosine Kinase ◽  
Receptor Tyrosine Kinase ◽  
Kinase Activity ◽  
Egf Receptor ◽  
Tyrosine Kinase Activity ◽  
A431 Cells ◽  
Epidermal Growth

Treatment of A431 human epidermoid cells with epidermal growth factor (EGF; 20 nM) results in decreased proliferation. This is associated with blockage of the cells in the S and/or G2 phases of the cell cycle. We found that tyrphostin, a putative tyrosine kinase inhibitor, in the range of 50 to 100 microM, partially reversed the growth-inhibitory and cell cycle changes induced by EGF. By using high-pressure liquid chromatography with electrochemical detection, we found that tyrphostin was readily incorporated into A431 cells, reaching maximal levels within 1 h. Although tyrphostin (50 to 100 microM) had no effect on high-affinity binding of EGF to its receptor in A431 cells for up to 24 h, the compound partially inhibited EGF-stimulated EGF receptor tyrosine kinase activity. However, this effect was evident only after prolonged treatment of the cells (4 to 24 h) with the drug. When the peak intracellular concentration of tyrphostin occurred (1 h), no inhibition of tyrosine kinase activity was observed. After both 1 and 24 h, tyrphostin was a less effective inhibitor of tyrosine kinase activity than the potent tumor promoter 12-O-tetradecanoyl phorbol-13-acetate, which almost completely blocked EGF receptor autophosphorylation. On the basis of our data, we hypothesize that tyrphostin is not a competitive inhibitor of the EGF receptor tyrosine kinase in intact cells and that it functions by an indirect mechanism.

scholarly journals Role of Cell Cycle in Epidermal Growth Factor Receptor Inhibitor-Mediated Radiosensitization

2009 ◽  
Vol 69 (12) ◽  
pp. 5108-5114 ◽  
Author(s):  
Aarif Ahsan ◽  
Susan M. Hiniker ◽  
Mary A. Davis ◽  
Theodore S. Lawrence ◽  
Mukesh K. Nyati
Keyword(s):  
Cell Cycle ◽  
Epidermal Growth Factor Receptor ◽  
Growth Factor ◽  
Epidermal Growth Factor ◽  
Growth Factor Receptor ◽  
Epidermal Growth ◽  
Receptor Inhibitor

The role of microfilaments in the capping of epidermal growth factor receptor in A431 cells

1991 ◽  
Vol 194 (1) ◽  
pp. 48-55 ◽  
Author(s):  
I.A. Khrebtukova ◽  
K. Kwiatkowska ◽  
D.A. Gudkova ◽  
A.B. Sorokin ◽  
G.P. Pinaev
Keyword(s):  
Epidermal Growth Factor Receptor ◽  
Growth Factor ◽  
Epidermal Growth Factor ◽  
Growth Factor Receptor ◽  
A431 Cells ◽  
Epidermal Growth

The Role of the Epidermal Growth Factor (EGF) Receptors (ErbBs) in Mouse Preantral Follicle Development

2016 ◽  
Author(s):  
Kacie Thomson ◽  
Victoria Atess ◽  
Mhairi Laird ◽  
Stephen Franks ◽  
Kate Hardy
Keyword(s):  
Growth Factor ◽  
Epidermal Growth Factor ◽  
Follicle Development ◽  
Egf Receptors ◽  
Preantral Follicle ◽  
Epidermal Growth
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