Comparison of CYP1A1 and CYP1B1 expressions in tissue biopsies obtained from with diagnosis invasive breast lobular carcinoma
Abstract
Objective: Expression of CYPs may provoke tumor development targeting activation of procarcinogens or increase in development and proliferation of breast tumor cells. Moreover, it affects
the etiology of breast cancer
and they may also
change response
to treatment. So, we aimed to compare the protein expression of CYP1A1 and CYP1B1, which are the most commonly expressed in breast
cancer,
which is so important.
Method: Breast biopsy specimens from at least 14 invasive
breast lobular carcinoma were used
and
they obtained from Adiyaman University Pathology Department. The protein expression of
CYP1A1, CYP1B1 were determined by immunohistochemically method. Staining intensity was graded as 0 if no staining was observed, +1 if weak staining was present, +2 if moderate staining was observed, and +3
if strong staining was present.
Results: Results were assessment using the total number of participants.
When pathologic and
histological glands are considered, for right breast, as +3 staining CYP1A1 and CYP1B1
protein expressions were found to be 83.33 % and 16.67 % respectively. In +2 staining
CYP1A1 protein expressions was found to be 16.67 %, but CYPB1 not expressed. For left breast, CYP1A1 protein was strongly stained by 50 %. In account
of moderate staining. In terms of moderate staining, both CYP1A1 and CYP1B1 proteins were expressed in 33.33 % percent. Besides, weak staining results to be found. CYP1A1 and CYP1B1 were found to be 16.67 % and 33.33 %, respectively. No statistically significant difference was found between CYP1A1
and CYP1B1 (P>0.05).
Conclusions: CYP1A1 was expressed
in all cases, whereas CYP1B1 was
expressed less
or not at all. These results
indicate that CYP1A1 can
an important marker in breast
cancer cases.
Thanks
We thanks to 1st INTERNATIONAL CANCER DAYS to be held in Sivas Cumhuriyet University between 19-21 September 2019 Board and all Organizing Committee, Scientific Committee and others.
References
- [1] Oyama T, Morita M, Isse T, et al. Immunohistochemically evaluation of cytochrome P450 (CYP) and p53 in breast cancer. Frontiers in Bioscience. 2005; 10: 1156-6.
- [2] Buterin T, Hess MT, Luneva N, Geacintov NE, Amin S, Kroth H, Seidel A, Naegeli H. Unrepaired fjord region polycyclic aromatic hydrocarbon-DNA adducts in Ras codon 61 mutational hot spots. Cancer Research, 2000; 60, 1849-1856.
- [3] Hankinson O. The aryl hydrocarbon receptor complex. Annual Review Pharmacology Toxicology. 1995: 35: 307–340.
- [4] Hayes CL, Spink DC, Spink BC, Cao JQ, Walker NJ, Sutter TR. 17b-Estradiol hydroxylation catalyzed by human cytochrome P450 1B1. Proceedings of the National Academy of Sciences of the United States of America.1996; 93: 9776–9781.
- [5] Zhu BT, Conney A.H. Functional role of estrogen metabolism in target cells: review and perspectives. Carcinogenesis. 1998; 19: 1–27, 1998.
- [6] Hellmold H, Rylander T, Magnusson M, Reihner E, Warner M, Gustafsson, J. Characterization of cytochrome P450 enzymes in human breast tissue from reduction mammoplasties. Journal of Clinic Endocrinology Metabolism. 1998; 83, 886-895.
- [7] Larsen MC, Angus WG, Brake PB, Eltom SE, Sukow KA. Jefcoate CR. Characterization of CYP1B1 and CYP1A1 expression in human mammary epithelial cells: role of the aryl hydrocarbon receptor in polycyclic aromatic hydrocarbon metabolism. Cancer Research. 1998. 58: 2366-2374.
- [8] Murray GI, Patimala S, Steward KN, Miller ID, Heys SD. Profiling the expression of cytochrome P450 in breast cancer. Histopathology. 2010; 57(2): 02-11.
Abstract
References
- [1] Oyama T, Morita M, Isse T, et al. Immunohistochemically evaluation of cytochrome P450 (CYP) and p53 in breast cancer. Frontiers in Bioscience. 2005; 10: 1156-6.
- [2] Buterin T, Hess MT, Luneva N, Geacintov NE, Amin S, Kroth H, Seidel A, Naegeli H. Unrepaired fjord region polycyclic aromatic hydrocarbon-DNA adducts in Ras codon 61 mutational hot spots. Cancer Research, 2000; 60, 1849-1856.
- [3] Hankinson O. The aryl hydrocarbon receptor complex. Annual Review Pharmacology Toxicology. 1995: 35: 307–340.
- [4] Hayes CL, Spink DC, Spink BC, Cao JQ, Walker NJ, Sutter TR. 17b-Estradiol hydroxylation catalyzed by human cytochrome P450 1B1. Proceedings of the National Academy of Sciences of the United States of America.1996; 93: 9776–9781.
- [5] Zhu BT, Conney A.H. Functional role of estrogen metabolism in target cells: review and perspectives. Carcinogenesis. 1998; 19: 1–27, 1998.
- [6] Hellmold H, Rylander T, Magnusson M, Reihner E, Warner M, Gustafsson, J. Characterization of cytochrome P450 enzymes in human breast tissue from reduction mammoplasties. Journal of Clinic Endocrinology Metabolism. 1998; 83, 886-895.
- [7] Larsen MC, Angus WG, Brake PB, Eltom SE, Sukow KA. Jefcoate CR. Characterization of CYP1B1 and CYP1A1 expression in human mammary epithelial cells: role of the aryl hydrocarbon receptor in polycyclic aromatic hydrocarbon metabolism. Cancer Research. 1998. 58: 2366-2374.
- [8] Murray GI, Patimala S, Steward KN, Miller ID, Heys SD. Profiling the expression of cytochrome P450 in breast cancer. Histopathology. 2010; 57(2): 02-11.
Details
| Primary Language | English |
|---|---|
| Subjects | Health Care Administration |
| Journal Section | Surgical Science Research Articles |
| Authors | |
| Publication Date | December 31, 2019 |
| Acceptance Date | January 2, 2020 |
| Published in Issue | Year 2019 |