Oncogene Products as Receptors

1987 ◽  
pp. 59-67
Author(s):  
Erica M. S. Sibinga ◽  
Gail R. Massey ◽  
Mark I. Greene
Keyword(s):  
Oncogene Products

Characterization of YY1 OPB Peptide for its Anticancer Activity

2019 ◽  
Vol 19 (6) ◽  
pp. 504-511 ◽  
Author(s):  
Yige Qi ◽  
Ting Yan ◽  
Lu Chen ◽  
Qiang Zhang ◽  
Weishu Wang ◽  
...  
Keyword(s):  
Breast Cancer ◽  
Amino Acids ◽  
Cell Proliferation ◽  
Cancer Cell ◽  
Breast Cancer Cell ◽  
Expression Vectors ◽  
Cancer Cell Proliferation ◽  
Breast Cancer Cell Proliferation ◽  
Oncogene Products ◽  
And Migration

Background:The oncoprotein binding (OPB) domain of Yin Yang 1 (YY1) consists of 26 amino acids between G201 and S226, and is involved in YY1 interaction with multiple oncogene products, including MDM2, AKT, EZH2 and E1A. Through the OPB domain, YY1 promotes the oncogenic or proliferative regulation of these oncoproteins in cancer cells. We previously demonstrated that a peptide with the OPB sequence blocked YY1-AKT interaction and inhibited breast cancer cell proliferation.Objective:In the current study, we characterized the OPB domain and determined a minimal region for peptide design to suppress cancer cellMethods:Using alanine-scan method, we identified that the amino acids at OPB C-terminal are essential to YY1 binding to AKT. Further studies suggested that serine and threonine residues, but not lysines, in OPB play a key role in YY1-AKT interaction. We generated GFP fusion expression vectors to express OPB peptides with serially deleted N-terminal and found that OPB1 (i.e. G201-S226) is cytoplasmic, but OPB2 (i.e. E206-S226), OPB3 (i.e. E206-S226) and control peptide were both nuclear and cytoplasmic.Results:Both OPB1 and 2 inhibited breast cancer cell proliferation and migration, but OPB3 exhibited similar effects to control. OPB1 and 2 caused cell cycle arrest at G1 phase, increased p53 and p21 expression, and reduced AKT(S473) phosphorylation in MCF-7 cells, but not in MDA-MB-231 cells.Conclusion:: Overall, the serines and threonines of OPB are essential to YY1 binding to oncoproteins, and OPB peptide can be minimized to E206-S226 that maintain inhibitory activity to YY1- promoted cell proliferation.

Regulation by thyroid status of c-myc, c-fos and H-ras mRNAs in the rat myocardium

1991 ◽  
Vol 130 (2) ◽  
pp. 239-244 ◽  
Author(s):  
N. K. Green ◽  
M. D. Gammage ◽  
J. A. Franklyn ◽  
M. C. Sheppard
Keyword(s):  
Protein Synthesis ◽  
Thyroid Hormones ◽  
Contractile Protein ◽  
Rat Myocardium ◽  
Direct Effects ◽  
Thyroid Status ◽  
Critical Signal ◽  
Ras Genes ◽  
Intracellular Signals ◽  
Oncogene Products

ABSTRACT Effects of thyroid status on expression of a variety of myocardial genes, such as those encoding contractile proteins, have been reported, as well as interactions between thyroid hormones and developmental and haemodynamic regulation of contractile protein synthesis. In addition, it is clear that developmental and haemodynamic factors regulate expression of specific proto-oncogenes, including c-myc, c-fos and H-ras, in the myocardium but the effect of thyroid status on such proto-oncogene products, which are proposed to play a critical signal-transducing role in the heart, has been previously unexplored. In order to determine whether changes in thyroid status are associated with changes in expression of these putative intracellular signals, we examined the effect of hypothyroidism and tri-iodothyronine (T3) treatment on myocardial levels of c-myc, c-fos and H-ras mRNAs in the rat. The induction of hypothyroidism was associated with a marked increase in myocardial c-myc, c-fos and H-ras mRNAs, changes reversed by 72 h of T3 replacement. Administration of T3 to euthyroid rats had no significant effect on myocardial c-myc or c-fos mRNAs, but inhibition of H-ras mRNA by T3 was evident. These observations demonstrating influences of thyroid status on expression of specific proto-oncogenes suggest that thyroid hormones, as well as exerting direct effects on expression of functionally important myocardial genes, also interact with the cellular transduction pathways mediated by the products of the c-myc, c-fos and H-ras genes. Journal of Endocrinology (1991) 130, 239–244

Differential response to retinoic acid of Syrian hamster embryo fibroblasts expressing v-src or v-Ha-ras oncogenes

1986 ◽  
Vol 6 (10) ◽  
pp. 3341-3348
Author(s):  
A M Jetten ◽  
J C Barrett ◽  
T M Gilmer
Keyword(s):  
Retinoic Acid ◽  
Tumor Cell ◽  
Cell Lines ◽  
Ornithine Decarboxylase ◽  
Syrian Hamster ◽  
Soft Agar ◽  
Protein Kinase Activity ◽  
Decarboxylase Activity ◽  
Oncogene Products ◽  
Transformed Cell Lines

It has been shown that treatment of many but not all tumor cell lines with retinoids affects cell proliferation and expression of the transformed phenotype. To determine whether the response of the tumor cell to retinoids is influenced by specific oncogenes activated in the cell, we studied the action of these agents in the immortal, nontumorigenic Syrian hamster embryo cell lines DES-4 and 10W transfected with either v-Ha-ras or v-src oncogenes. In this paper we show that in transformed DES-4 cells expressing v-src, retinoic acid inhibited anchorage-independent growth, reduced saturation density, and inhibited the induction of ornithine decarboxylase by the phorbol ester 12-O-tetradecanoylphorbol-13-acetate. In contrast, retinoic acid enhances the expression of the transformed phenotype in DES-4-derived cells that express v-Ha-ras. In these cells retinoic acid increases the number and the average size of colonies formed in soft agar. Moreover, retinoic acid enhances ornithine decarboxylase activity and acts in a synergistic fashion with 12-O-tetradecanoylphorbol-13-acetate. These results indicate that oncogenes activated in cells can indeed influence the response of cells to retinoids. Retinoic acid does not appear to alter the levels of pp60src or p21ras proteins in these cells, suggesting that retinoic acid does not affect the synthesis of these oncogene products. Furthermore, retinoic acid does not affect the protein kinase activity of pp60src. Transformed cell lines derived from 10W cells responded differently, indicating that the presence of a specific oncogene is not the only factor determining the response to retinoids. Possible mechanisms by which retinoic acid may interfere with the expression of the oncogene products are discussed.

Expression of ret proto-oncogene products in the hypoganglionic segment of the small intestine of congenital aganglionosis rats

1995 ◽  
Vol 30 (5) ◽  
pp. 641-645 ◽  
Author(s):  
Yoshio Watanabe ◽  
Takahiro Ito ◽  
Toru Harada ◽  
Masahide Takahashi ◽  
Shigeru Kobayashi ◽  
...  
Keyword(s):  
Small Intestine ◽  
Oncogene Products

The role of oncogene products in neutrophil apoptosis

1994 ◽  
Vol 22 (3) ◽  
pp. 253S-253S ◽  
Author(s):  
SHARON HANNAH ◽  
THOMAS G. COTTER ◽  
ANDREW H. WYLLIE ◽  
CHRISTOPHER HASLETT
Keyword(s):  
Neutrophil Apoptosis ◽  
Oncogene Products

The viral Ki-ras gene must be expressed in the G2 phase if ts Kirsten sarcoma virus-infected NRK cells are to proliferate in serum-free medium

1987 ◽  
Vol 7 (1) ◽  
pp. 444-449
Author(s):  
J P Durkin ◽  
J F Whitfield
Keyword(s):  
S Phase ◽  
Temperature Sensitive ◽  
Serum Free Medium ◽  
Free Medium ◽  
Ras Gene ◽  
Serum Free ◽  
Quiescent Cells ◽  
Sarcoma Virus ◽  
G2 Phase ◽  
Oncogene Products

NRK cells infected with a temperature-sensitive Kirsten sarcoma virus (ts371 KSV) are transformed at 36 degrees C, but are untransformed at 41 degrees C which inactivates the abnormally thermolabile oncogenic p21Ki product of the viral Ki-ras gene. At 41 degrees C, tsKSV-infected NRK cells were arrested in G0/G1 when incubated in serum-free medium, but could then be stimulated to transit G1, replicate DNA, and divide by adding serum at 41 degrees C or dropping the temperature to a p21-activating 36 degrees C without adding serum. When quiescent cells at 41 degrees C were stimulated to transit G1 in serum-free medium by activating p21 at 36 degrees C and then shifted back to the p21-inactivating 41 degrees C in the mid-S phase, they continued replicating DNA but could not transit G2. Reactivating p21 in the G2-arrested cells by once again lowering the temperature to 36 degrees C stimulated a rapid entry into mitosis. By contrast, while serum-stimulated quiescent G0 cells at 41 degrees C replicate DNA and divide, serum did not induce G2-arrested cells to enter mitosis, indicating that serum growth factors may trigger events in the G1 phase that ultimately determine G2 transit. These observations made with the viral ras product suggest that cellular ras proto-oncogene products have a role in G2 transit of normal cells.

Oncogene Products

1995 ◽  
pp. 1304-1306
Author(s):  
Tony Milford Ward
Keyword(s):  
Oncogene Products

scholarly journals Oncogenic Signaling in Tumorigenesis and Applications of siRNA Nanotherapeutics in Breast Cancer

Cancers ◽  
2019 ◽  
Vol 11 (5) ◽  
pp. 632 ◽  
Author(s):  
Nur Izyani Kamaruzman ◽  
Noraini Abd Aziz ◽  
Chit Laa Poh ◽  
Ezharul Hoque Chowdhury
Keyword(s):  
Breast Cancer ◽  
Signaling Pathways ◽  
Targeted Delivery ◽  
Therapeutic Strategies ◽  
Signaling Cascades ◽  
Breast Tumorigenesis ◽  
Oncogenic Signaling ◽  
Complementary Sequence ◽  
Genetic Manipulations ◽  
Oncogene Products

Overexpression of oncogenes and cross-talks of the oncoproteins-regulated signaling cascades with other intracellular pathways in breast cancer could lead to massive abnormal signaling with the consequence of tumorigenesis. The ability to identify the genes having vital roles in cancer development would give a promising therapeutics strategy in combating the disease. Genetic manipulations through siRNAs targeting the complementary sequence of the oncogenic mRNA in breast cancer is one of the promising approaches that can be harnessed to develop more efficient treatments for breast cancer. In this review, we highlighted the effects of major signaling pathways stimulated by oncogene products on breast tumorigenesis and discussed the potential therapeutic strategies for targeted delivery of siRNAs with nanoparticles in suppressing the stimulated signaling pathways.

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