Cytochrome P450 and Glutathione Transferase Expression in Human Breast Cancer
Purpose: The cytochrome P-450 (CYP) and glutathione S -transferase (GST) enzyme systems may influence the biological effects of carcinogens, including estrogens. As such, these enzymes may predict the developmental risk of breast cancer, as well as be potential targets for chemoprevention. The purpo...
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| Veröffentlicht in: | Clinical cancer research 2003-05, Vol.9 (5), p.1705-1709 |
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| creator | EL-RAYES, Basil F ALI, Shadan HEILBRUN, Lance K LABABIDI, Samir BOUWMAN, David VISSCHER, David PHILIP, Philip A |
| description | Purpose: The cytochrome P-450 (CYP) and glutathione S -transferase (GST) enzyme systems may influence the biological effects of carcinogens, including estrogens. As such, these
enzymes may predict the developmental risk of breast cancer, as well as be potential targets for chemoprevention. The purpose
of this study was to compare the expression of GST-Pi and CYPs 1A1, 2B6, 2E1, and 3A4 in paired samples of normal and malignant
breast tissue from patients with breast cancer and women undergoing reduction mammoplasty.
Experimental design: Expression of CYPs 1A1, 2B6, 2E1, 3A4, and GST-Pi was quantified in breast tissue from 33 patients with breast cancer and
in 17 women without history of cancer who underwent reduction mammoplasty. The expression of CYP 1A1, 2B6, 2E1, 3A4, and GST-Pi
was quantified by immunoblotting.
Results: CYP 1A1, 2E1, and 3A4 expression was significantly lower ( P < 0.05) in malignant tissue as compared with morphologically normal adjacent tissue. Conversely, GST-Pi expression was marginally
lower in the normal tissue ( P = 0.08). No significant difference in enzyme expression was seen between the tissue from reduction mammoplasty and normal
tissue from breast cancer patients. There was a trend for higher expression of CYP 2B6 and GST-Pi in the estrogen receptor
expressing tumors than those tumors without expression ( P > 0.28).
Conclusion: The expression of these enzymes was similar in morphologically normal breast tissue from patients with or without breast
cancer. The expression of CYPs was down-regulated in the tumor tissue. The clinical significance of CYP alterations in breast
cancer will need further characterization. |
| format | Article |
| fullrecord | <record><control><sourceid>pubmed_pasca</sourceid><recordid>TN_cdi_pubmed_primary_12738724</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>12738724</sourcerecordid><originalsourceid>FETCH-LOGICAL-h269t-480fe8bebf66e02d9eb398662dc9abbd1ae45737f6d985689467a11914e8b8613</originalsourceid><addsrcrecordid>eNpFj0tLw0AUhQdRbK3-BZmNuArM-7HUUFuhoou6DjfJjYk0aZlJ0f57B1txdQ-X7xz4zsiUa20zKYw-T5lZlzElxYRcxfjJGFecqUsy4cJKZ4Wakpf8MG6rNmx7pG9KMwpDTReb_Qhj220HpOsAQ2wwQEQ6_94FjDH9aTfQ5b6HgT4GhDjSHIYKwzW5aGAT8eZ0Z-T9ab7Ol9nqdfGcP6yyVhg_ZsqxBl2JZWMMMlF7LKV3xoi68lCWNQdU2krbmNo7bZxXxgLnnqvUcobLGbk97u72ZY91sQtdD-FQ_Hkl4O4EQKxg0ySJqov_nLJeeiYSd3_k2u6j_eoCFtWvSNJECFVb-EIX3DItfwD0oWR8</addsrcrecordid><sourcetype>Index Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype></control><display><type>article</type><title>Cytochrome P450 and Glutathione Transferase Expression in Human Breast Cancer</title><source>MEDLINE</source><source>American Association for Cancer Research</source><source>EZB-FREE-00999 freely available EZB journals</source><source>Alma/SFX Local Collection</source><creator>EL-RAYES, Basil F ; ALI, Shadan ; HEILBRUN, Lance K ; LABABIDI, Samir ; BOUWMAN, David ; VISSCHER, David ; PHILIP, Philip A</creator><creatorcontrib>EL-RAYES, Basil F ; ALI, Shadan ; HEILBRUN, Lance K ; LABABIDI, Samir ; BOUWMAN, David ; VISSCHER, David ; PHILIP, Philip A</creatorcontrib><description>Purpose: The cytochrome P-450 (CYP) and glutathione S -transferase (GST) enzyme systems may influence the biological effects of carcinogens, including estrogens. As such, these
enzymes may predict the developmental risk of breast cancer, as well as be potential targets for chemoprevention. The purpose
of this study was to compare the expression of GST-Pi and CYPs 1A1, 2B6, 2E1, and 3A4 in paired samples of normal and malignant
breast tissue from patients with breast cancer and women undergoing reduction mammoplasty.
Experimental design: Expression of CYPs 1A1, 2B6, 2E1, 3A4, and GST-Pi was quantified in breast tissue from 33 patients with breast cancer and
in 17 women without history of cancer who underwent reduction mammoplasty. The expression of CYP 1A1, 2B6, 2E1, 3A4, and GST-Pi
was quantified by immunoblotting.
Results: CYP 1A1, 2E1, and 3A4 expression was significantly lower ( P < 0.05) in malignant tissue as compared with morphologically normal adjacent tissue. Conversely, GST-Pi expression was marginally
lower in the normal tissue ( P = 0.08). No significant difference in enzyme expression was seen between the tissue from reduction mammoplasty and normal
tissue from breast cancer patients. There was a trend for higher expression of CYP 2B6 and GST-Pi in the estrogen receptor
expressing tumors than those tumors without expression ( P > 0.28).
Conclusion: The expression of these enzymes was similar in morphologically normal breast tissue from patients with or without breast
cancer. The expression of CYPs was down-regulated in the tumor tissue. The clinical significance of CYP alterations in breast
cancer will need further characterization.</description><identifier>ISSN: 1078-0432</identifier><identifier>EISSN: 1557-3265</identifier><identifier>PMID: 12738724</identifier><language>eng</language><publisher>Philadelphia, PA: American Association for Cancer Research</publisher><subject>Aryl Hydrocarbon Hydroxylases - metabolism ; Biological and medical sciences ; Blotting, Western ; Breast - metabolism ; Breast Neoplasms - enzymology ; Cytochrome P-450 CYP1A1 - metabolism ; Cytochrome P-450 CYP2B6 ; Cytochrome P-450 CYP2E1 - metabolism ; Cytochrome P-450 CYP3A ; Cytochrome P-450 Enzyme System - metabolism ; Female ; Gene Expression Regulation, Enzymologic ; Glutathione S-Transferase pi ; Glutathione Transferase - metabolism ; Gynecology. Andrology. Obstetrics ; Humans ; Immunoenzyme Techniques ; Isoenzymes - metabolism ; Mammaplasty ; Mammary gland diseases ; Medical sciences ; Oxidoreductases, N-Demethylating - metabolism ; Receptors, Estrogen - metabolism ; Tumors</subject><ispartof>Clinical cancer research, 2003-05, Vol.9 (5), p.1705-1709</ispartof><rights>2003 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=14793902$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/12738724$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>EL-RAYES, Basil F</creatorcontrib><creatorcontrib>ALI, Shadan</creatorcontrib><creatorcontrib>HEILBRUN, Lance K</creatorcontrib><creatorcontrib>LABABIDI, Samir</creatorcontrib><creatorcontrib>BOUWMAN, David</creatorcontrib><creatorcontrib>VISSCHER, David</creatorcontrib><creatorcontrib>PHILIP, Philip A</creatorcontrib><title>Cytochrome P450 and Glutathione Transferase Expression in Human Breast Cancer</title><title>Clinical cancer research</title><addtitle>Clin Cancer Res</addtitle><description>Purpose: The cytochrome P-450 (CYP) and glutathione S -transferase (GST) enzyme systems may influence the biological effects of carcinogens, including estrogens. As such, these
enzymes may predict the developmental risk of breast cancer, as well as be potential targets for chemoprevention. The purpose
of this study was to compare the expression of GST-Pi and CYPs 1A1, 2B6, 2E1, and 3A4 in paired samples of normal and malignant
breast tissue from patients with breast cancer and women undergoing reduction mammoplasty.
Experimental design: Expression of CYPs 1A1, 2B6, 2E1, 3A4, and GST-Pi was quantified in breast tissue from 33 patients with breast cancer and
in 17 women without history of cancer who underwent reduction mammoplasty. The expression of CYP 1A1, 2B6, 2E1, 3A4, and GST-Pi
was quantified by immunoblotting.
Results: CYP 1A1, 2E1, and 3A4 expression was significantly lower ( P < 0.05) in malignant tissue as compared with morphologically normal adjacent tissue. Conversely, GST-Pi expression was marginally
lower in the normal tissue ( P = 0.08). No significant difference in enzyme expression was seen between the tissue from reduction mammoplasty and normal
tissue from breast cancer patients. There was a trend for higher expression of CYP 2B6 and GST-Pi in the estrogen receptor
expressing tumors than those tumors without expression ( P > 0.28).
Conclusion: The expression of these enzymes was similar in morphologically normal breast tissue from patients with or without breast
cancer. The expression of CYPs was down-regulated in the tumor tissue. The clinical significance of CYP alterations in breast
cancer will need further characterization.</description><subject>Aryl Hydrocarbon Hydroxylases - metabolism</subject><subject>Biological and medical sciences</subject><subject>Blotting, Western</subject><subject>Breast - metabolism</subject><subject>Breast Neoplasms - enzymology</subject><subject>Cytochrome P-450 CYP1A1 - metabolism</subject><subject>Cytochrome P-450 CYP2B6</subject><subject>Cytochrome P-450 CYP2E1 - metabolism</subject><subject>Cytochrome P-450 CYP3A</subject><subject>Cytochrome P-450 Enzyme System - metabolism</subject><subject>Female</subject><subject>Gene Expression Regulation, Enzymologic</subject><subject>Glutathione S-Transferase pi</subject><subject>Glutathione Transferase - metabolism</subject><subject>Gynecology. Andrology. Obstetrics</subject><subject>Humans</subject><subject>Immunoenzyme Techniques</subject><subject>Isoenzymes - metabolism</subject><subject>Mammaplasty</subject><subject>Mammary gland diseases</subject><subject>Medical sciences</subject><subject>Oxidoreductases, N-Demethylating - metabolism</subject><subject>Receptors, Estrogen - metabolism</subject><subject>Tumors</subject><issn>1078-0432</issn><issn>1557-3265</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2003</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpFj0tLw0AUhQdRbK3-BZmNuArM-7HUUFuhoou6DjfJjYk0aZlJ0f57B1txdQ-X7xz4zsiUa20zKYw-T5lZlzElxYRcxfjJGFecqUsy4cJKZ4Wakpf8MG6rNmx7pG9KMwpDTReb_Qhj220HpOsAQ2wwQEQ6_94FjDH9aTfQ5b6HgT4GhDjSHIYKwzW5aGAT8eZ0Z-T9ab7Ol9nqdfGcP6yyVhg_ZsqxBl2JZWMMMlF7LKV3xoi68lCWNQdU2krbmNo7bZxXxgLnnqvUcobLGbk97u72ZY91sQtdD-FQ_Hkl4O4EQKxg0ySJqov_nLJeeiYSd3_k2u6j_eoCFtWvSNJECFVb-EIX3DItfwD0oWR8</recordid><startdate>20030501</startdate><enddate>20030501</enddate><creator>EL-RAYES, Basil F</creator><creator>ALI, Shadan</creator><creator>HEILBRUN, Lance K</creator><creator>LABABIDI, Samir</creator><creator>BOUWMAN, David</creator><creator>VISSCHER, David</creator><creator>PHILIP, Philip A</creator><general>American Association for Cancer Research</general><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope></search><sort><creationdate>20030501</creationdate><title>Cytochrome P450 and Glutathione Transferase Expression in Human Breast Cancer</title><author>EL-RAYES, Basil F ; ALI, Shadan ; HEILBRUN, Lance K ; LABABIDI, Samir ; BOUWMAN, David ; VISSCHER, David ; PHILIP, Philip A</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-h269t-480fe8bebf66e02d9eb398662dc9abbd1ae45737f6d985689467a11914e8b8613</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2003</creationdate><topic>Aryl Hydrocarbon Hydroxylases - metabolism</topic><topic>Biological and medical sciences</topic><topic>Blotting, Western</topic><topic>Breast - metabolism</topic><topic>Breast Neoplasms - enzymology</topic><topic>Cytochrome P-450 CYP1A1 - metabolism</topic><topic>Cytochrome P-450 CYP2B6</topic><topic>Cytochrome P-450 CYP2E1 - metabolism</topic><topic>Cytochrome P-450 CYP3A</topic><topic>Cytochrome P-450 Enzyme System - metabolism</topic><topic>Female</topic><topic>Gene Expression Regulation, Enzymologic</topic><topic>Glutathione S-Transferase pi</topic><topic>Glutathione Transferase - metabolism</topic><topic>Gynecology. Andrology. Obstetrics</topic><topic>Humans</topic><topic>Immunoenzyme Techniques</topic><topic>Isoenzymes - metabolism</topic><topic>Mammaplasty</topic><topic>Mammary gland diseases</topic><topic>Medical sciences</topic><topic>Oxidoreductases, N-Demethylating - metabolism</topic><topic>Receptors, Estrogen - metabolism</topic><topic>Tumors</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>EL-RAYES, Basil F</creatorcontrib><creatorcontrib>ALI, Shadan</creatorcontrib><creatorcontrib>HEILBRUN, Lance K</creatorcontrib><creatorcontrib>LABABIDI, Samir</creatorcontrib><creatorcontrib>BOUWMAN, David</creatorcontrib><creatorcontrib>VISSCHER, David</creatorcontrib><creatorcontrib>PHILIP, Philip A</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><jtitle>Clinical cancer research</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>EL-RAYES, Basil F</au><au>ALI, Shadan</au><au>HEILBRUN, Lance K</au><au>LABABIDI, Samir</au><au>BOUWMAN, David</au><au>VISSCHER, David</au><au>PHILIP, Philip A</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Cytochrome P450 and Glutathione Transferase Expression in Human Breast Cancer</atitle><jtitle>Clinical cancer research</jtitle><addtitle>Clin Cancer Res</addtitle><date>2003-05-01</date><risdate>2003</risdate><volume>9</volume><issue>5</issue><spage>1705</spage><epage>1709</epage><pages>1705-1709</pages><issn>1078-0432</issn><eissn>1557-3265</eissn><abstract>Purpose: The cytochrome P-450 (CYP) and glutathione S -transferase (GST) enzyme systems may influence the biological effects of carcinogens, including estrogens. As such, these
enzymes may predict the developmental risk of breast cancer, as well as be potential targets for chemoprevention. The purpose
of this study was to compare the expression of GST-Pi and CYPs 1A1, 2B6, 2E1, and 3A4 in paired samples of normal and malignant
breast tissue from patients with breast cancer and women undergoing reduction mammoplasty.
Experimental design: Expression of CYPs 1A1, 2B6, 2E1, 3A4, and GST-Pi was quantified in breast tissue from 33 patients with breast cancer and
in 17 women without history of cancer who underwent reduction mammoplasty. The expression of CYP 1A1, 2B6, 2E1, 3A4, and GST-Pi
was quantified by immunoblotting.
Results: CYP 1A1, 2E1, and 3A4 expression was significantly lower ( P < 0.05) in malignant tissue as compared with morphologically normal adjacent tissue. Conversely, GST-Pi expression was marginally
lower in the normal tissue ( P = 0.08). No significant difference in enzyme expression was seen between the tissue from reduction mammoplasty and normal
tissue from breast cancer patients. There was a trend for higher expression of CYP 2B6 and GST-Pi in the estrogen receptor
expressing tumors than those tumors without expression ( P > 0.28).
Conclusion: The expression of these enzymes was similar in morphologically normal breast tissue from patients with or without breast
cancer. The expression of CYPs was down-regulated in the tumor tissue. The clinical significance of CYP alterations in breast
cancer will need further characterization.</abstract><cop>Philadelphia, PA</cop><pub>American Association for Cancer Research</pub><pmid>12738724</pmid><tpages>5</tpages></addata></record> |
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| source | MEDLINE; American Association for Cancer Research; EZB-FREE-00999 freely available EZB journals; Alma/SFX Local Collection |
| subjects | Aryl Hydrocarbon Hydroxylases - metabolism Biological and medical sciences Blotting, Western Breast - metabolism Breast Neoplasms - enzymology Cytochrome P-450 CYP1A1 - metabolism Cytochrome P-450 CYP2B6 Cytochrome P-450 CYP2E1 - metabolism Cytochrome P-450 CYP3A Cytochrome P-450 Enzyme System - metabolism Female Gene Expression Regulation, Enzymologic Glutathione S-Transferase pi Glutathione Transferase - metabolism Gynecology. Andrology. Obstetrics Humans Immunoenzyme Techniques Isoenzymes - metabolism Mammaplasty Mammary gland diseases Medical sciences Oxidoreductases, N-Demethylating - metabolism Receptors, Estrogen - metabolism Tumors |
| title | Cytochrome P450 and Glutathione Transferase Expression in Human Breast Cancer |
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