The PKD1 gene product
We would like to bring to your attention a report that has significant implications for an autosomal dominant polycystic kidney disease study that was reported in the April issue of Nature Medicine. This study described the characterization and localization of an extracellular matrix protein using a...
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| Veröffentlicht in: | Nature medicine 1995-06, Vol.1 (6), p.493-493 |
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| creator | Harris, Peter C Germino, Gregory Klinger, Kathy Landes, Greg Adelsberg, Janet Van |
| description | We would like to bring to your attention a report that has significant implications for an autosomal dominant polycystic kidney disease study that was reported in the April issue of Nature Medicine. This study described the characterization and localization of an extracellular matrix protein using antibodies raised against a decapeptide from the predicted extreme COOH-terminal domain of the PKD1 gene product. The American Polycystic Kidney Disease Consortium has identified an important difference between their sequence and that previously published; a two-base pair insertion results in the replacement of the originally predicted 92 COOH-terminal residues with 12 novel residues. This sequence difference has been found in two cloned genomic templates and one cDNA template and has been confirmed using allele-specific oligonucleotides and PCR products derived from the genomic DNA of nine individuals. The European Polycystic Kidney Disease Consortium has also re-analysed the original sequence and confirmed the presence of the two-base pair insertion. We therefore conclude that there are currently no data supporting the presence of the originally published COOH terminal peptide sequence within the final PKD1 gene product. It is clear, therefore, that the relationship between the PKD1 gene product to the extracellular matrix protein identified with these anti-peptide antibodies is uncertain and should be viewed with caution. |
| doi_str_mv | 10.1038/nm0695-493a |
| format | Article |
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This study described the characterization and localization of an extracellular matrix protein using antibodies raised against a decapeptide from the predicted extreme COOH-terminal domain of the PKD1 gene product. The American Polycystic Kidney Disease Consortium has identified an important difference between their sequence and that previously published; a two-base pair insertion results in the replacement of the originally predicted 92 COOH-terminal residues with 12 novel residues. This sequence difference has been found in two cloned genomic templates and one cDNA template and has been confirmed using allele-specific oligonucleotides and PCR products derived from the genomic DNA of nine individuals. The European Polycystic Kidney Disease Consortium has also re-analysed the original sequence and confirmed the presence of the two-base pair insertion. We therefore conclude that there are currently no data supporting the presence of the originally published COOH terminal peptide sequence within the final PKD1 gene product. It is clear, therefore, that the relationship between the PKD1 gene product to the extracellular matrix protein identified with these anti-peptide antibodies is uncertain and should be viewed with caution.</description><identifier>ISSN: 1078-8956</identifier><identifier>EISSN: 1546-170X</identifier><identifier>DOI: 10.1038/nm0695-493a</identifier><identifier>PMID: 7585106</identifier><language>eng</language><publisher>New York: Nature Publishing Group US</publisher><subject>Amino Acid Sequence ; Biomedicine ; Cancer Research ; Chromosome Mapping ; Cloning, Molecular ; DNA, Complementary - genetics ; extracellular matrix ; Extracellular Matrix Proteins - genetics ; Extracellular Matrix Proteins - immunology ; gene products ; Humans ; Infectious Diseases ; letters-to-the-editor ; man ; Metabolic Diseases ; Molecular Medicine ; Neurosciences ; Peptide Fragments - chemical synthesis ; Peptide Fragments - chemistry ; Peptide Fragments - immunology ; PKD1 gene ; polycystic kidney ; Polycystic kidney disease 1 protein ; Polycystic Kidney, Autosomal Dominant - genetics ; Proteins - chemistry ; Proteins - genetics ; Proteins - immunology ; Sequence Analysis ; TRPP Cation Channels</subject><ispartof>Nature medicine, 1995-06, Vol.1 (6), p.493-493</ispartof><rights>Springer Nature America, Inc. 1995</rights><rights>Copyright Nature Publishing Group Jun 1995</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c443t-609ea921156c61624ddc0280de0cad5eb14e48d3e2b98a082ef993366f65820a3</citedby><cites>FETCH-LOGICAL-c443t-609ea921156c61624ddc0280de0cad5eb14e48d3e2b98a082ef993366f65820a3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,2727,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/7585106$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Harris, Peter C</creatorcontrib><creatorcontrib>Germino, Gregory</creatorcontrib><creatorcontrib>Klinger, Kathy</creatorcontrib><creatorcontrib>Landes, Greg</creatorcontrib><creatorcontrib>Adelsberg, Janet Van</creatorcontrib><title>The PKD1 gene product</title><title>Nature medicine</title><addtitle>Nat Med</addtitle><addtitle>Nat Med</addtitle><description>We would like to bring to your attention a report that has significant implications for an autosomal dominant polycystic kidney disease study that was reported in the April issue of Nature Medicine. This study described the characterization and localization of an extracellular matrix protein using antibodies raised against a decapeptide from the predicted extreme COOH-terminal domain of the PKD1 gene product. The American Polycystic Kidney Disease Consortium has identified an important difference between their sequence and that previously published; a two-base pair insertion results in the replacement of the originally predicted 92 COOH-terminal residues with 12 novel residues. This sequence difference has been found in two cloned genomic templates and one cDNA template and has been confirmed using allele-specific oligonucleotides and PCR products derived from the genomic DNA of nine individuals. The European Polycystic Kidney Disease Consortium has also re-analysed the original sequence and confirmed the presence of the two-base pair insertion. We therefore conclude that there are currently no data supporting the presence of the originally published COOH terminal peptide sequence within the final PKD1 gene product. It is clear, therefore, that the relationship between the PKD1 gene product to the extracellular matrix protein identified with these anti-peptide antibodies is uncertain and should be viewed with caution.</description><subject>Amino Acid Sequence</subject><subject>Biomedicine</subject><subject>Cancer Research</subject><subject>Chromosome Mapping</subject><subject>Cloning, Molecular</subject><subject>DNA, Complementary - genetics</subject><subject>extracellular matrix</subject><subject>Extracellular Matrix Proteins - genetics</subject><subject>Extracellular Matrix Proteins - immunology</subject><subject>gene products</subject><subject>Humans</subject><subject>Infectious Diseases</subject><subject>letters-to-the-editor</subject><subject>man</subject><subject>Metabolic Diseases</subject><subject>Molecular Medicine</subject><subject>Neurosciences</subject><subject>Peptide Fragments - chemical synthesis</subject><subject>Peptide Fragments - chemistry</subject><subject>Peptide Fragments - immunology</subject><subject>PKD1 gene</subject><subject>polycystic kidney</subject><subject>Polycystic kidney disease 1 protein</subject><subject>Polycystic Kidney, Autosomal Dominant - genetics</subject><subject>Proteins - chemistry</subject><subject>Proteins - genetics</subject><subject>Proteins - immunology</subject><subject>Sequence Analysis</subject><subject>TRPP Cation Channels</subject><issn>1078-8956</issn><issn>1546-170X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1995</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkc1Lw0AQxRdRaq2exKNQEbxodPYzu0epn1jQQwVvyzaZ1JYmrbvJwf_eLSlVRPA0A-_He8wbQg4pXFLg-qoqQRmZCMPdFulSKVRCU3jbjjukOtFGql2yF8IMADhI0yGdVGpJQXXJ0egd-y9PN7Q_wQr7S7_Im6zeJzuFmwc8WM8eeb27HQ0ekuHz_ePgephkQvA6UWDQGUapVJmiiok8z4BpyBEyl0scU4FC5xzZ2GgHmmFhDOdKFUpqBo73yFnrG3M_Ggy1Lachw_ncVbhogk1TZYSS4l-QKi2FYBDB01_gbNH4Kh5hGacqjVxKI3XeUplfhOCxsEs_LZ3_tBTsqlPbdmpXnUb6eO3ZjEvMN-y6xKhftHqISjVB_535t91Ji1eubjxu7H68kX8BkrqHEQ</recordid><startdate>19950601</startdate><enddate>19950601</enddate><creator>Harris, Peter C</creator><creator>Germino, Gregory</creator><creator>Klinger, Kathy</creator><creator>Landes, Greg</creator><creator>Adelsberg, Janet Van</creator><general>Nature Publishing Group US</general><general>Nature Publishing Group</general><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>7QG</scope><scope>7QL</scope><scope>7QP</scope><scope>7QR</scope><scope>7T5</scope><scope>7TK</scope><scope>7TM</scope><scope>7TO</scope><scope>7U7</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>K9.</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope><scope>7T3</scope><scope>7X8</scope></search><sort><creationdate>19950601</creationdate><title>The PKD1 gene product</title><author>Harris, Peter C ; Germino, Gregory ; Klinger, Kathy ; Landes, Greg ; Adelsberg, Janet Van</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c443t-609ea921156c61624ddc0280de0cad5eb14e48d3e2b98a082ef993366f65820a3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1995</creationdate><topic>Amino Acid Sequence</topic><topic>Biomedicine</topic><topic>Cancer Research</topic><topic>Chromosome Mapping</topic><topic>Cloning, Molecular</topic><topic>DNA, Complementary - genetics</topic><topic>extracellular matrix</topic><topic>Extracellular Matrix Proteins - genetics</topic><topic>Extracellular Matrix Proteins - immunology</topic><topic>gene products</topic><topic>Humans</topic><topic>Infectious Diseases</topic><topic>letters-to-the-editor</topic><topic>man</topic><topic>Metabolic Diseases</topic><topic>Molecular Medicine</topic><topic>Neurosciences</topic><topic>Peptide Fragments - chemical synthesis</topic><topic>Peptide Fragments - chemistry</topic><topic>Peptide Fragments - immunology</topic><topic>PKD1 gene</topic><topic>polycystic kidney</topic><topic>Polycystic kidney disease 1 protein</topic><topic>Polycystic Kidney, Autosomal Dominant - genetics</topic><topic>Proteins - chemistry</topic><topic>Proteins - genetics</topic><topic>Proteins - immunology</topic><topic>Sequence Analysis</topic><topic>TRPP Cation Channels</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Harris, Peter C</creatorcontrib><creatorcontrib>Germino, Gregory</creatorcontrib><creatorcontrib>Klinger, Kathy</creatorcontrib><creatorcontrib>Landes, Greg</creatorcontrib><creatorcontrib>Adelsberg, Janet Van</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Animal Behavior Abstracts</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Immunology Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Oncogenes and Growth Factors Abstracts</collection><collection>Toxicology Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>Human Genome Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Nature medicine</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Harris, Peter C</au><au>Germino, Gregory</au><au>Klinger, Kathy</au><au>Landes, Greg</au><au>Adelsberg, Janet Van</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The PKD1 gene product</atitle><jtitle>Nature medicine</jtitle><stitle>Nat Med</stitle><addtitle>Nat Med</addtitle><date>1995-06-01</date><risdate>1995</risdate><volume>1</volume><issue>6</issue><spage>493</spage><epage>493</epage><pages>493-493</pages><issn>1078-8956</issn><eissn>1546-170X</eissn><abstract>We would like to bring to your attention a report that has significant implications for an autosomal dominant polycystic kidney disease study that was reported in the April issue of Nature Medicine. This study described the characterization and localization of an extracellular matrix protein using antibodies raised against a decapeptide from the predicted extreme COOH-terminal domain of the PKD1 gene product. The American Polycystic Kidney Disease Consortium has identified an important difference between their sequence and that previously published; a two-base pair insertion results in the replacement of the originally predicted 92 COOH-terminal residues with 12 novel residues. This sequence difference has been found in two cloned genomic templates and one cDNA template and has been confirmed using allele-specific oligonucleotides and PCR products derived from the genomic DNA of nine individuals. The European Polycystic Kidney Disease Consortium has also re-analysed the original sequence and confirmed the presence of the two-base pair insertion. We therefore conclude that there are currently no data supporting the presence of the originally published COOH terminal peptide sequence within the final PKD1 gene product. It is clear, therefore, that the relationship between the PKD1 gene product to the extracellular matrix protein identified with these anti-peptide antibodies is uncertain and should be viewed with caution.</abstract><cop>New York</cop><pub>Nature Publishing Group US</pub><pmid>7585106</pmid><doi>10.1038/nm0695-493a</doi><tpages>1</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | Nature medicine, 1995-06, Vol.1 (6), p.493-493 |
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| subjects | Amino Acid Sequence Biomedicine Cancer Research Chromosome Mapping Cloning, Molecular DNA, Complementary - genetics extracellular matrix Extracellular Matrix Proteins - genetics Extracellular Matrix Proteins - immunology gene products Humans Infectious Diseases letters-to-the-editor man Metabolic Diseases Molecular Medicine Neurosciences Peptide Fragments - chemical synthesis Peptide Fragments - chemistry Peptide Fragments - immunology PKD1 gene polycystic kidney Polycystic kidney disease 1 protein Polycystic Kidney, Autosomal Dominant - genetics Proteins - chemistry Proteins - genetics Proteins - immunology Sequence Analysis TRPP Cation Channels |
| title | The PKD1 gene product |
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