Distribution and developmentally regulated expression of murine polycystin
L. Geng, Y. Segal, A. Pavlova, E. J. Barros, C. Lohning, W. Lu, S. K. Nigam, A. M. Frischauf, S. T. Reeders and J. Zhou Renal Division, Brigham and Women's Hospital, Harvard Medical School, Boston, Massachusetts 02115, USA. PKD1, the gene that is mutated in approximately 85% of autosomal domina...
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| Veröffentlicht in: | American journal of physiology. Renal physiology 1997-04, Vol.272 (4), p.451-F459 |
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| creator | Geng, L Segal, Y Pavlova, A Barros, E. J Lohning, C Lu, W Nigam, S. K Frischauf, A. M Reeders, S. T Zhou, J |
| description | L. Geng, Y. Segal, A. Pavlova, E. J. Barros, C. Lohning, W. Lu, S. K. Nigam, A. M. Frischauf, S. T. Reeders and J. Zhou
Renal Division, Brigham and Women's Hospital, Harvard Medical School, Boston, Massachusetts 02115, USA.
PKD1, the gene that is mutated in approximately 85% of autosomal dominant
polycystic kidney disease (ADPKD) cases in humans, has recently been
identified (Eur. PKD Consortium. Cell 77: 881-894, 1994; also, erratum in
Cell 78: 1994). The longest open-reading frame of PKD1 encodes polycystin,
a novel approximately 460-kDa protein that contains a series of
NH2-terminal adhesive domains (J. Hughes, C. J. Ward, B. Peral, R.
Aspinwall, K. Clark, J. San Millan, V. Gamble, and P. C. Harris. Nat.
Genet. 10: 151-160, 1995; and Int. PKD Consortium. Cell 81: 289-298, 1995)
and several putative transmembrane segments. To extend studies of
polycystin to an experimentally accessible animal, we have isolated a cDNA
clone encoding the 3' end of Pkd1, the mouse homologue of PKD1, and raised
a specific antibody to recombinant murine polycystin. This antibody was
used to determine the subcellular localization and tissue distribution of
the protein by Western analysis and immunocytochemistry. In the mouse,
polycystin is an approximately 400-kDa molecule that is predominantly found
in membrane fractions of tissue and cell extracts. It is expressed in many
tissues including kidney, liver, pancreas, heart, intestine, lung, and
brain. Renal expression, which is confined to tubular epithelia, is highest
in late fetal and early neonatal life and drops 20-fold by the third
postnatal week, maintaining this level into adulthood. Thus the temporal
profile of polycystin expression coincides with kidney tubule
differentiation and maturation. |
| doi_str_mv | 10.1152/ajprenal.1997.272.4.F451 |
| format | Article |
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Renal Division, Brigham and Women's Hospital, Harvard Medical School, Boston, Massachusetts 02115, USA.
PKD1, the gene that is mutated in approximately 85% of autosomal dominant
polycystic kidney disease (ADPKD) cases in humans, has recently been
identified (Eur. PKD Consortium. Cell 77: 881-894, 1994; also, erratum in
Cell 78: 1994). The longest open-reading frame of PKD1 encodes polycystin,
a novel approximately 460-kDa protein that contains a series of
NH2-terminal adhesive domains (J. Hughes, C. J. Ward, B. Peral, R.
Aspinwall, K. Clark, J. San Millan, V. Gamble, and P. C. Harris. Nat.
Genet. 10: 151-160, 1995; and Int. PKD Consortium. Cell 81: 289-298, 1995)
and several putative transmembrane segments. To extend studies of
polycystin to an experimentally accessible animal, we have isolated a cDNA
clone encoding the 3' end of Pkd1, the mouse homologue of PKD1, and raised
a specific antibody to recombinant murine polycystin. This antibody was
used to determine the subcellular localization and tissue distribution of
the protein by Western analysis and immunocytochemistry. In the mouse,
polycystin is an approximately 400-kDa molecule that is predominantly found
in membrane fractions of tissue and cell extracts. It is expressed in many
tissues including kidney, liver, pancreas, heart, intestine, lung, and
brain. Renal expression, which is confined to tubular epithelia, is highest
in late fetal and early neonatal life and drops 20-fold by the third
postnatal week, maintaining this level into adulthood. Thus the temporal
profile of polycystin expression coincides with kidney tubule
differentiation and maturation.</description><identifier>ISSN: 0363-6127</identifier><identifier>ISSN: 0002-9513</identifier><identifier>ISSN: 1931-857X</identifier><identifier>EISSN: 2161-1157</identifier><identifier>EISSN: 1522-1466</identifier><identifier>DOI: 10.1152/ajprenal.1997.272.4.F451</identifier><identifier>PMID: 9140045</identifier><language>eng</language><publisher>United States</publisher><subject>Aging - metabolism ; Amino Acid Sequence ; Animals ; Cloning, Molecular ; Embryonic and Fetal Development ; Female ; Gene Expression Regulation, Developmental ; Gestational Age ; Humans ; Immunohistochemistry ; Kidney - embryology ; Kidney - growth & development ; Kidney - metabolism ; Mice ; Molecular Sequence Data ; Open Reading Frames ; Polycystic Kidney, Autosomal Dominant - genetics ; Pregnancy ; Protein Biosynthesis ; Proteins - chemistry ; Proteins - genetics ; Recombinant Fusion Proteins - biosynthesis ; Recombinant Fusion Proteins - chemistry ; Sequence Homology, Amino Acid ; Subcellular Fractions - metabolism ; TRPP Cation Channels</subject><ispartof>American journal of physiology. Renal physiology, 1997-04, Vol.272 (4), p.451-F459</ispartof><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c401t-ab7a4b3a3824fad4452cd06198e37dca5b849bc5f9af22098cd14d4c017a24f83</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,3026,27901,27902</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/9140045$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Geng, L</creatorcontrib><creatorcontrib>Segal, Y</creatorcontrib><creatorcontrib>Pavlova, A</creatorcontrib><creatorcontrib>Barros, E. J</creatorcontrib><creatorcontrib>Lohning, C</creatorcontrib><creatorcontrib>Lu, W</creatorcontrib><creatorcontrib>Nigam, S. K</creatorcontrib><creatorcontrib>Frischauf, A. M</creatorcontrib><creatorcontrib>Reeders, S. T</creatorcontrib><creatorcontrib>Zhou, J</creatorcontrib><title>Distribution and developmentally regulated expression of murine polycystin</title><title>American journal of physiology. Renal physiology</title><addtitle>Am J Physiol</addtitle><description>L. Geng, Y. Segal, A. Pavlova, E. J. Barros, C. Lohning, W. Lu, S. K. Nigam, A. M. Frischauf, S. T. Reeders and J. Zhou
Renal Division, Brigham and Women's Hospital, Harvard Medical School, Boston, Massachusetts 02115, USA.
PKD1, the gene that is mutated in approximately 85% of autosomal dominant
polycystic kidney disease (ADPKD) cases in humans, has recently been
identified (Eur. PKD Consortium. Cell 77: 881-894, 1994; also, erratum in
Cell 78: 1994). The longest open-reading frame of PKD1 encodes polycystin,
a novel approximately 460-kDa protein that contains a series of
NH2-terminal adhesive domains (J. Hughes, C. J. Ward, B. Peral, R.
Aspinwall, K. Clark, J. San Millan, V. Gamble, and P. C. Harris. Nat.
Genet. 10: 151-160, 1995; and Int. PKD Consortium. Cell 81: 289-298, 1995)
and several putative transmembrane segments. To extend studies of
polycystin to an experimentally accessible animal, we have isolated a cDNA
clone encoding the 3' end of Pkd1, the mouse homologue of PKD1, and raised
a specific antibody to recombinant murine polycystin. This antibody was
used to determine the subcellular localization and tissue distribution of
the protein by Western analysis and immunocytochemistry. In the mouse,
polycystin is an approximately 400-kDa molecule that is predominantly found
in membrane fractions of tissue and cell extracts. It is expressed in many
tissues including kidney, liver, pancreas, heart, intestine, lung, and
brain. Renal expression, which is confined to tubular epithelia, is highest
in late fetal and early neonatal life and drops 20-fold by the third
postnatal week, maintaining this level into adulthood. Thus the temporal
profile of polycystin expression coincides with kidney tubule
differentiation and maturation.</description><subject>Aging - metabolism</subject><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Cloning, Molecular</subject><subject>Embryonic and Fetal Development</subject><subject>Female</subject><subject>Gene Expression Regulation, Developmental</subject><subject>Gestational Age</subject><subject>Humans</subject><subject>Immunohistochemistry</subject><subject>Kidney - embryology</subject><subject>Kidney - growth & development</subject><subject>Kidney - metabolism</subject><subject>Mice</subject><subject>Molecular Sequence Data</subject><subject>Open Reading Frames</subject><subject>Polycystic Kidney, Autosomal Dominant - genetics</subject><subject>Pregnancy</subject><subject>Protein Biosynthesis</subject><subject>Proteins - chemistry</subject><subject>Proteins - genetics</subject><subject>Recombinant Fusion Proteins - biosynthesis</subject><subject>Recombinant Fusion Proteins - chemistry</subject><subject>Sequence Homology, Amino Acid</subject><subject>Subcellular Fractions - metabolism</subject><subject>TRPP Cation Channels</subject><issn>0363-6127</issn><issn>0002-9513</issn><issn>1931-857X</issn><issn>2161-1157</issn><issn>1522-1466</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1997</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpNkMtOwzAURC0EKqXwCUhZsUuwHSd2lggoD1ViA2vLsZ3WlRMHOwHy97hqeazuYs7MlQ4ACYIZQgW-Ftve607YDFUVzTDFGcmWpEBHYI5RidII0WMwh3mZpyXC9BSchbCFEOOSlTMwqxCBkBRz8HxnwuBNPQ7GdYnoVKL0h7aub3U3CGunxOv1aMWgVaK_4tMQdqBrknb0ptNJ7-wkpzCY7hycNMIGfXG4C_C2vH-9fUxXLw9PtzerVBKIhlTUVJA6FznDpBGKkAJLBUtUMZ1TJUVRM1LVsmgq0WAMKyYVIopIiKiIDZYvwNV-t_fufdRh4K0JUlsrOu3GwCmraJ4zGkG2B6V3IXjd8N6bVviJI8h3GvmPRr7TyKNGTvhOY6xeHn6MdavVb_HgLebZPt-Y9ebTeM37zRTNWLee_lb_DX4DvmCDmQ</recordid><startdate>19970401</startdate><enddate>19970401</enddate><creator>Geng, L</creator><creator>Segal, Y</creator><creator>Pavlova, A</creator><creator>Barros, E. J</creator><creator>Lohning, C</creator><creator>Lu, W</creator><creator>Nigam, S. K</creator><creator>Frischauf, A. M</creator><creator>Reeders, S. T</creator><creator>Zhou, J</creator><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>19970401</creationdate><title>Distribution and developmentally regulated expression of murine polycystin</title><author>Geng, L ; Segal, Y ; Pavlova, A ; Barros, E. J ; Lohning, C ; Lu, W ; Nigam, S. K ; Frischauf, A. M ; Reeders, S. T ; Zhou, J</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c401t-ab7a4b3a3824fad4452cd06198e37dca5b849bc5f9af22098cd14d4c017a24f83</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1997</creationdate><topic>Aging - metabolism</topic><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Cloning, Molecular</topic><topic>Embryonic and Fetal Development</topic><topic>Female</topic><topic>Gene Expression Regulation, Developmental</topic><topic>Gestational Age</topic><topic>Humans</topic><topic>Immunohistochemistry</topic><topic>Kidney - embryology</topic><topic>Kidney - growth & development</topic><topic>Kidney - metabolism</topic><topic>Mice</topic><topic>Molecular Sequence Data</topic><topic>Open Reading Frames</topic><topic>Polycystic Kidney, Autosomal Dominant - genetics</topic><topic>Pregnancy</topic><topic>Protein Biosynthesis</topic><topic>Proteins - chemistry</topic><topic>Proteins - genetics</topic><topic>Recombinant Fusion Proteins - biosynthesis</topic><topic>Recombinant Fusion Proteins - chemistry</topic><topic>Sequence Homology, Amino Acid</topic><topic>Subcellular Fractions - metabolism</topic><topic>TRPP Cation Channels</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Geng, L</creatorcontrib><creatorcontrib>Segal, Y</creatorcontrib><creatorcontrib>Pavlova, A</creatorcontrib><creatorcontrib>Barros, E. J</creatorcontrib><creatorcontrib>Lohning, C</creatorcontrib><creatorcontrib>Lu, W</creatorcontrib><creatorcontrib>Nigam, S. K</creatorcontrib><creatorcontrib>Frischauf, A. M</creatorcontrib><creatorcontrib>Reeders, S. T</creatorcontrib><creatorcontrib>Zhou, J</creatorcontrib><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>American journal of physiology. Renal physiology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Geng, L</au><au>Segal, Y</au><au>Pavlova, A</au><au>Barros, E. J</au><au>Lohning, C</au><au>Lu, W</au><au>Nigam, S. K</au><au>Frischauf, A. M</au><au>Reeders, S. T</au><au>Zhou, J</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Distribution and developmentally regulated expression of murine polycystin</atitle><jtitle>American journal of physiology. Renal physiology</jtitle><addtitle>Am J Physiol</addtitle><date>1997-04-01</date><risdate>1997</risdate><volume>272</volume><issue>4</issue><spage>451</spage><epage>F459</epage><pages>451-F459</pages><issn>0363-6127</issn><issn>0002-9513</issn><issn>1931-857X</issn><eissn>2161-1157</eissn><eissn>1522-1466</eissn><abstract>L. Geng, Y. Segal, A. Pavlova, E. J. Barros, C. Lohning, W. Lu, S. K. Nigam, A. M. Frischauf, S. T. Reeders and J. Zhou
Renal Division, Brigham and Women's Hospital, Harvard Medical School, Boston, Massachusetts 02115, USA.
PKD1, the gene that is mutated in approximately 85% of autosomal dominant
polycystic kidney disease (ADPKD) cases in humans, has recently been
identified (Eur. PKD Consortium. Cell 77: 881-894, 1994; also, erratum in
Cell 78: 1994). The longest open-reading frame of PKD1 encodes polycystin,
a novel approximately 460-kDa protein that contains a series of
NH2-terminal adhesive domains (J. Hughes, C. J. Ward, B. Peral, R.
Aspinwall, K. Clark, J. San Millan, V. Gamble, and P. C. Harris. Nat.
Genet. 10: 151-160, 1995; and Int. PKD Consortium. Cell 81: 289-298, 1995)
and several putative transmembrane segments. To extend studies of
polycystin to an experimentally accessible animal, we have isolated a cDNA
clone encoding the 3' end of Pkd1, the mouse homologue of PKD1, and raised
a specific antibody to recombinant murine polycystin. This antibody was
used to determine the subcellular localization and tissue distribution of
the protein by Western analysis and immunocytochemistry. In the mouse,
polycystin is an approximately 400-kDa molecule that is predominantly found
in membrane fractions of tissue and cell extracts. It is expressed in many
tissues including kidney, liver, pancreas, heart, intestine, lung, and
brain. Renal expression, which is confined to tubular epithelia, is highest
in late fetal and early neonatal life and drops 20-fold by the third
postnatal week, maintaining this level into adulthood. Thus the temporal
profile of polycystin expression coincides with kidney tubule
differentiation and maturation.</abstract><cop>United States</cop><pmid>9140045</pmid><doi>10.1152/ajprenal.1997.272.4.F451</doi><oa>free_for_read</oa></addata></record> |
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| source | MEDLINE; American Physiological Society; EZB-FREE-00999 freely available EZB journals; Alma/SFX Local Collection |
| subjects | Aging - metabolism Amino Acid Sequence Animals Cloning, Molecular Embryonic and Fetal Development Female Gene Expression Regulation, Developmental Gestational Age Humans Immunohistochemistry Kidney - embryology Kidney - growth & development Kidney - metabolism Mice Molecular Sequence Data Open Reading Frames Polycystic Kidney, Autosomal Dominant - genetics Pregnancy Protein Biosynthesis Proteins - chemistry Proteins - genetics Recombinant Fusion Proteins - biosynthesis Recombinant Fusion Proteins - chemistry Sequence Homology, Amino Acid Subcellular Fractions - metabolism TRPP Cation Channels |
| title | Distribution and developmentally regulated expression of murine polycystin |
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