scholarly journals Activation of chromosomal vitellogenin genes in Xenopus oocytes by pure estrogen receptor and independent activation of albumin genes.

1990 ◽  
Vol 10 (12) ◽  
pp. 6674-6682 ◽  
Author(s):  
E A McKenzie ◽  
N A Cridland ◽  
J Knowland

We generate pure estrogen receptor protein in Xenopus oocytes by injecting them with estrogen receptor mRNA synthesized in vitro. A chromosomal vitellogenin gene, which normally responds to estrogen only in liver cells, is activated. Primer extension shows that initiation is accurate, and ribonuclease mapping shows that the first exon is correctly spliced out of the initial transcript. Long transcripts are produced, one being equal in length to poly(A)- vitellogenin mRNA. Immunochemical estimates of receptor levels in the oocyte nuclei suggest that pure receptor, acting alone, cannot activate oocyte vitellogenin genes unless unusually large amounts are present. However, when a receptor-free extract from liver cells is also injected, the amount of receptor required is reduced. Such an extract, but not pure receptor, can also activate albumin genes in oocytes.

1990 ◽  
Vol 10 (12) ◽  
pp. 6674-6682
Author(s):  
E A McKenzie ◽  
N A Cridland ◽  
J Knowland

We generate pure estrogen receptor protein in Xenopus oocytes by injecting them with estrogen receptor mRNA synthesized in vitro. A chromosomal vitellogenin gene, which normally responds to estrogen only in liver cells, is activated. Primer extension shows that initiation is accurate, and ribonuclease mapping shows that the first exon is correctly spliced out of the initial transcript. Long transcripts are produced, one being equal in length to poly(A)- vitellogenin mRNA. Immunochemical estimates of receptor levels in the oocyte nuclei suggest that pure receptor, acting alone, cannot activate oocyte vitellogenin genes unless unusually large amounts are present. However, when a receptor-free extract from liver cells is also injected, the amount of receptor required is reduced. Such an extract, but not pure receptor, can also activate albumin genes in oocytes.


Author(s):  
L. Muruganandam ◽  
Maheswari R.

Objective: To evaluate the anticancer activities of selective Mannich bases by in silico methods.Methods: X-ray crystallographic structure of Estrogen receptor protein (PDB ID 2YAT) was downloaded from the protein data bank (PDB) and is docked with the target Mannich bases using Accelyrs Discovery Studio client version 2.5 software.Results: Based on the in silico analysis results of the target compounds with standard drug tamoxifen, the best-docked compound is identified and its anticancer activity is confirmed by using in vitro MTS analysis using Raju and Jurkat cell lines.Conclusion: The mannich base compound N-[(Diphenylamino) methyl] acetamide showed fourfold higher activity than standard drug tamoxifen, may be used to overcome the drug resistance of Estrogen receptor protein.


Cancer ◽  
1981 ◽  
Vol 47 (10) ◽  
pp. 2364-2367 ◽  
Author(s):  
David W. Kinne ◽  
Roy Ashikari ◽  
Avital Butler ◽  
Celia Menendez-Botet ◽  
Paul Peter Rosen ◽  
...  

1982 ◽  
Vol 25 (4) ◽  
pp. 348-350 ◽  
Author(s):  
Michael V. Agrez ◽  
Robert J. Spencer

2005 ◽  
Vol 129 (3) ◽  
pp. 338-347 ◽  
Author(s):  
Fionnuala P. O'Connell ◽  
Helen H. Wang ◽  
Robert D. Odze

Abstract Context.—Breast carcinoma often metastasizes to the gastrointestinal tract, especially the stomach, where it is frequently difficult to distinguish from a primary gastric carcinoma. Objective.—To evaluate the utility of immunohistochemical stains in differentiating primary gastric carcinomas from metastatic breast carcinomas. Design.—Mucosal biopsy specimens from 47 adenocarcinomas involving the gastrointestinal tract (28 primary gastric carcinomas and 19 metastatic breast carcinomas) and 16 control cases of primary breast carcinomas without metastasis were immunohistochemically stained for estrogen receptor protein (ER), progesterone receptor protein (PR), gross cystic disease fluid protein (GCDFP), human epidermal growth factor receptor 2 protein, cytokeratin (CK) 5/6, CK/7, CK/20, a panel of mucin glycoprotein antigens (MUC2, MUC3, MUC5AC, and MUC6), monoclonal antibody DAS-1, and caudal-type homeobox transcription factor CDX2 and compared between primary and metastatic adenocarcinomas. Results.—Highly significant proportions of metastatic breast carcinomas were positive for ER (72%), PR (33%), GCDFP (78%), and CK5/6 (61%) compared with primary gastric carcinomas (ER, 0%; PR, 0%; GCDFP, 0%; and CK5/6, 14%) (P < .001, P = .002, P < .001, and P = .004, respectively). Of these immunostains, ER, PR, and GCDFP were 100% specific. Primary breast tumors and their metastases showed a similar phenotypic profile. In contrast, primary gastric carcinomas showed significantly higher proportions of cases that stained with CK20 (50%), MUC2 (54%), MUC5AC (71%), MUC6 (39%), DAS-1 (43%), and CDX2 (67%) compared with metastatic breast carcinomas (CK20, 0%; MUC2, 24%; MUC5AC, 6%; MUC6, 0%; DAS-1, 0%; and CDX2, 0%) (P = .001, P = .01, P < .001, P = .02, P = .009, and P < .001, respectively). No significant differences were observed with regard to any of the other immunostains (human epidermal growth factor receptor 2 protein, CK7, and MUC3) between the patient groups. Conclusions.—Estrogen receptor protein, PR, GCDFP, CK5/6, CK20, MUC5AC, MUC6, DAS-1, and CDX2 are helpful in distinguishing primary gastric carcinomas from metastatic breast carcinomas. Of these, ER, PR, and GCDFP are highly specific for metastatic breast carcinomas, whereas CK20, DAS-1, MUC2, MUC5AC, MUC6, and CDX2 are highly specific for primary gastric carcinomas.


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