Key peptide processing enzymes are expressed by breast cancer cells

The expression of the three key peptide processing enzyme families, represented by CPE, PAM, and PC1/3 plus PC2, were examined in MCF-7 and ZR-75-1 breast cancer cell lines. Both of these cell lines express vasopressin receptors as well as the vasopressin gene, but the processing of vasopressin gene...

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Veröffentlicht in:Cancer letters 2001-04, Vol.165 (2), p.211-218
Hauptverfasser: Du, Jinlin, Keegan, Brendan P., North, William G.
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container_title Cancer letters
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creator Du, Jinlin
Keegan, Brendan P.
North, William G.
description The expression of the three key peptide processing enzyme families, represented by CPE, PAM, and PC1/3 plus PC2, were examined in MCF-7 and ZR-75-1 breast cancer cell lines. Both of these cell lines express vasopressin receptors as well as the vasopressin gene, but the processing of vasopressin gene-related proteins appears to be limited. Products of the expected size for, CPE, PAM and PC1/PC3 could be amplified by reverse transcription-polymerase chain reaction (RT-PCR) from both cell lines. Cloning and sequencing of these RT-PCR products revealed that each enzyme mRNA had a structure identical to that published for the human form of the respective enzyme. Western analysis provided evidence that mRNAs for these enzymes are translated into proteins. Alternatively, PC2 mRNA was identified to be present in MCF-7 cells both by RT-PCR and Western blot analysis, but could not be demonstrated for ZR-75-1 cells. Our findings suggest that the key processing enzymes needed to generate active vasopressin and other neuropeptide growth factors are present in breast cancer cells.
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Both of these cell lines express vasopressin receptors as well as the vasopressin gene, but the processing of vasopressin gene-related proteins appears to be limited. Products of the expected size for, CPE, PAM and PC1/PC3 could be amplified by reverse transcription-polymerase chain reaction (RT-PCR) from both cell lines. Cloning and sequencing of these RT-PCR products revealed that each enzyme mRNA had a structure identical to that published for the human form of the respective enzyme. Western analysis provided evidence that mRNAs for these enzymes are translated into proteins. Alternatively, PC2 mRNA was identified to be present in MCF-7 cells both by RT-PCR and Western blot analysis, but could not be demonstrated for ZR-75-1 cells. 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Obstetrics</subject><subject>Humans</subject><subject>Mammary gland diseases</subject><subject>Medical sciences</subject><subject>Mixed Function Oxygenases - biosynthesis</subject><subject>Multienzyme Complexes</subject><subject>Neuropeptide</subject><subject>Peptidylglycine α-amidating monooxygenase</subject><subject>Processing</subject><subject>Prohormone convertase</subject><subject>Receptors, Vasopressin - biosynthesis</subject><subject>Reverse Transcriptase Polymerase Chain Reaction</subject><subject>RNA, Messenger - metabolism</subject><subject>Sequence Analysis, DNA</subject><subject>Subtilisins - biosynthesis</subject><subject>Tumor Cells, Cultured</subject><subject>Tumors</subject><subject>Vasopressin</subject><issn>0304-3835</issn><issn>1872-7980</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2001</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkE1LAzEQhoMotlZ_ghIQRA-rk81mkz2JFL9Q8KCeQ5pMJNKPNdmK9deb2lKPngaGZ2beeQg5ZHDOgNUXz8ChKrji4hTYGUAFTaG2SJ8pWRayUbBN-hukR_ZSegcAUUmxS3qMlVJwyfpk-IAL2mLbBYe0jTOLKYXpG8Xp92KCiZqIFL_amNvo6GhBRxFN6qg1U4uRWhyP0z7Z8Wac8GBdB-T15vpleFc8Pt3eD68eC8tV0xXKetEgNhUokz9QpfMKfS2MrwwXzgmsrEDvalNXXnAuSwWV8o2wtUAEwQfkZLU35_yYY-r0JKRlAjPF2TxpKQEkZ3UGxQq0cZZSRK_bGCYmLjQDvbSnf-3ppRoNTP_a0yrPHa0PzEcTdH9Ta10ZOF4DJlkz9jFbCGnDNUqqkmfqckVhlvEZMOpkA2ZfLkS0nXaz8E-QH0K1i0g</recordid><startdate>20010426</startdate><enddate>20010426</enddate><creator>Du, Jinlin</creator><creator>Keegan, Brendan P.</creator><creator>North, William G.</creator><general>Elsevier Ireland Ltd</general><general>Elsevier</general><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>20010426</creationdate><title>Key peptide processing enzymes are expressed by breast cancer cells</title><author>Du, Jinlin ; Keegan, Brendan P. ; North, William G.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c389t-8cf59ee9408a01682df8ef65af4a35dd5e4c5efd6a64f533728048f95c65ee053</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2001</creationdate><topic>Biological and medical sciences</topic><topic>Blotting, Western</topic><topic>Breast cancer</topic><topic>Breast Neoplasms - enzymology</topic><topic>Carboxypeptidase E</topic><topic>Carboxypeptidase H</topic><topic>Carboxypeptidases - biosynthesis</topic><topic>Cloning, Molecular</topic><topic>Furin</topic><topic>Gynecology. Andrology. Obstetrics</topic><topic>Humans</topic><topic>Mammary gland diseases</topic><topic>Medical sciences</topic><topic>Mixed Function Oxygenases - biosynthesis</topic><topic>Multienzyme Complexes</topic><topic>Neuropeptide</topic><topic>Peptidylglycine α-amidating monooxygenase</topic><topic>Processing</topic><topic>Prohormone convertase</topic><topic>Receptors, Vasopressin - biosynthesis</topic><topic>Reverse Transcriptase Polymerase Chain Reaction</topic><topic>RNA, Messenger - metabolism</topic><topic>Sequence Analysis, DNA</topic><topic>Subtilisins - biosynthesis</topic><topic>Tumor Cells, Cultured</topic><topic>Tumors</topic><topic>Vasopressin</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Du, Jinlin</creatorcontrib><creatorcontrib>Keegan, Brendan P.</creatorcontrib><creatorcontrib>North, William G.</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Cancer letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Du, Jinlin</au><au>Keegan, Brendan P.</au><au>North, William G.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Key peptide processing enzymes are expressed by breast cancer cells</atitle><jtitle>Cancer letters</jtitle><addtitle>Cancer Lett</addtitle><date>2001-04-26</date><risdate>2001</risdate><volume>165</volume><issue>2</issue><spage>211</spage><epage>218</epage><pages>211-218</pages><issn>0304-3835</issn><eissn>1872-7980</eissn><coden>CALEDQ</coden><abstract>The expression of the three key peptide processing enzyme families, represented by CPE, PAM, and PC1/3 plus PC2, were examined in MCF-7 and ZR-75-1 breast cancer cell lines. 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source MEDLINE; Elsevier ScienceDirect Journals
subjects Biological and medical sciences
Blotting, Western
Breast cancer
Breast Neoplasms - enzymology
Carboxypeptidase E
Carboxypeptidase H
Carboxypeptidases - biosynthesis
Cloning, Molecular
Furin
Gynecology. Andrology. Obstetrics
Humans
Mammary gland diseases
Medical sciences
Mixed Function Oxygenases - biosynthesis
Multienzyme Complexes
Neuropeptide
Peptidylglycine α-amidating monooxygenase
Processing
Prohormone convertase
Receptors, Vasopressin - biosynthesis
Reverse Transcriptase Polymerase Chain Reaction
RNA, Messenger - metabolism
Sequence Analysis, DNA
Subtilisins - biosynthesis
Tumor Cells, Cultured
Tumors
Vasopressin
title Key peptide processing enzymes are expressed by breast cancer cells
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