Na+ Pump Low and High Ouabain Affinity α Subunit Isoforms are Differently Distributed in Cells
Three isoforms (α 1, α 2, and α 3) of the catalytic (α ) subunit of the plasma membrane (PM) Na+ pump have been identified in the tissues of birds and mammals. These isoforms differ in their affinities for ions and for the Na+ pump inhibitor, ouabain. In the rat, α 1 has an unusually low affinity fo...
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| Veröffentlicht in: | Proceedings of the National Academy of Sciences - PNAS 1997-03, Vol.94 (5), p.1800-1805 |
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| creator | Juhaszova, Magdalena Blaustein, Mordecai P. |
| description | Three isoforms (α 1, α 2, and α 3) of the catalytic (α ) subunit of the plasma membrane (PM) Na+ pump have been identified in the tissues of birds and mammals. These isoforms differ in their affinities for ions and for the Na+ pump inhibitor, ouabain. In the rat, α 1 has an unusually low affinity for ouabain. The PM of most rat cells contains both low (α 1) and high (α 2 or α 3) ouabain affinity isoforms, but precise localization of specific isoforms, and their functional significance, are unknown. We employed high resolution immunocytochemical techniques to localize α subunit isoforms in primary cultured rat astrocytes, neurons, and arterial myocytes. Isoform α 1 was ubiquitously distributed over the surfaces of these cells. In contrast, high ouabain affinity isoforms (α 2 in astrocytes, α 3 in neurons and myocytes) were confined to a reticular distribution within the PM that paralleled underlying endoplasmic or sarcoplasmic reticulum. This distribution is identical to that of the PM Na/Ca exchanger. This raises the possibility that α 1 may regulate bulk cytosolic Na+, whereas α 2 and α 3 may regulate Na+ and, indirectly, Ca2+ in a restricted cytosolic space between the PM and reticulum. The high ouabain affinity Na+ pumps may thereby modulate reticulum Ca2+ content and Ca2+ signaling. |
| doi_str_mv | 10.1073/pnas.94.5.1800 |
| format | Article |
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These isoforms differ in their affinities for ions and for the Na+ pump inhibitor, ouabain. In the rat, α 1 has an unusually low affinity for ouabain. The PM of most rat cells contains both low (α 1) and high (α 2 or α 3) ouabain affinity isoforms, but precise localization of specific isoforms, and their functional significance, are unknown. We employed high resolution immunocytochemical techniques to localize α subunit isoforms in primary cultured rat astrocytes, neurons, and arterial myocytes. Isoform α 1 was ubiquitously distributed over the surfaces of these cells. In contrast, high ouabain affinity isoforms (α 2 in astrocytes, α 3 in neurons and myocytes) were confined to a reticular distribution within the PM that paralleled underlying endoplasmic or sarcoplasmic reticulum. This distribution is identical to that of the PM Na/Ca exchanger. This raises the possibility that α 1 may regulate bulk cytosolic Na+, whereas α 2 and α 3 may regulate Na+ and, indirectly, Ca2+ in a restricted cytosolic space between the PM and reticulum. The high ouabain affinity Na+ pumps may thereby modulate reticulum Ca2+ content and Ca2+ signaling.</description><identifier>ISSN: 0027-8424</identifier><identifier>EISSN: 1091-6490</identifier><identifier>DOI: 10.1073/pnas.94.5.1800</identifier><identifier>PMID: 9050859</identifier><language>eng</language><publisher>United States: National Academy of Sciences of the United States of America</publisher><subject>Animals ; Antibodies ; Antibodies - immunology ; Astrocytes ; Astrocytes - metabolism ; Biochemistry ; Biological Sciences ; Blotting, Western ; Calcium ; Calcium - metabolism ; Cell Membrane - metabolism ; Cells ; Cells, Cultured ; Cellular biology ; Cultured cells ; Immunohistochemistry ; Magnification ; Membrane Proteins - metabolism ; Microscopy, Fluorescence ; Mitochondria ; Muscle, Smooth, Vascular - cytology ; Muscle, Smooth, Vascular - metabolism ; Neurons ; Neurons - cytology ; Neurons - metabolism ; Ouabain - metabolism ; Ouabain - pharmacology ; Physiological regulation ; Protein isoforms ; Pumps ; Rats ; Rodents ; Sodium ; Sodium - metabolism ; Sodium-Potassium-Exchanging ATPase - chemistry ; Sodium-Potassium-Exchanging ATPase - metabolism</subject><ispartof>Proceedings of the National Academy of Sciences - PNAS, 1997-03, Vol.94 (5), p.1800-1805</ispartof><rights>Copyright 1997 National Academy of Sciences</rights><rights>Copyright National Academy of Sciences Mar 4, 1997</rights><rights>Copyright © 1997, The National Academy of Sciences of the USA 1997</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c482t-52b949ea8efa44cbab932d926de402b603cb506488994c40649f4940f9c162d33</citedby><cites>FETCH-LOGICAL-c482t-52b949ea8efa44cbab932d926de402b603cb506488994c40649f4940f9c162d33</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Uhttp://www.pnas.org/content/94/5.cover.gif</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/41540$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/41540$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>230,314,723,776,780,799,881,27901,27902,53766,53768,57992,58225</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/9050859$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Juhaszova, Magdalena</creatorcontrib><creatorcontrib>Blaustein, Mordecai P.</creatorcontrib><title>Na+ Pump Low and High Ouabain Affinity α Subunit Isoforms are Differently Distributed in Cells</title><title>Proceedings of the National Academy of Sciences - PNAS</title><addtitle>Proc Natl Acad Sci U S A</addtitle><description>Three isoforms (α 1, α 2, and α 3) of the catalytic (α ) subunit of the plasma membrane (PM) Na+ pump have been identified in the tissues of birds and mammals. These isoforms differ in their affinities for ions and for the Na+ pump inhibitor, ouabain. In the rat, α 1 has an unusually low affinity for ouabain. The PM of most rat cells contains both low (α 1) and high (α 2 or α 3) ouabain affinity isoforms, but precise localization of specific isoforms, and their functional significance, are unknown. We employed high resolution immunocytochemical techniques to localize α subunit isoforms in primary cultured rat astrocytes, neurons, and arterial myocytes. Isoform α 1 was ubiquitously distributed over the surfaces of these cells. In contrast, high ouabain affinity isoforms (α 2 in astrocytes, α 3 in neurons and myocytes) were confined to a reticular distribution within the PM that paralleled underlying endoplasmic or sarcoplasmic reticulum. This distribution is identical to that of the PM Na/Ca exchanger. This raises the possibility that α 1 may regulate bulk cytosolic Na+, whereas α 2 and α 3 may regulate Na+ and, indirectly, Ca2+ in a restricted cytosolic space between the PM and reticulum. The high ouabain affinity Na+ pumps may thereby modulate reticulum Ca2+ content and Ca2+ signaling.</description><subject>Animals</subject><subject>Antibodies</subject><subject>Antibodies - immunology</subject><subject>Astrocytes</subject><subject>Astrocytes - metabolism</subject><subject>Biochemistry</subject><subject>Biological Sciences</subject><subject>Blotting, Western</subject><subject>Calcium</subject><subject>Calcium - metabolism</subject><subject>Cell Membrane - metabolism</subject><subject>Cells</subject><subject>Cells, Cultured</subject><subject>Cellular biology</subject><subject>Cultured cells</subject><subject>Immunohistochemistry</subject><subject>Magnification</subject><subject>Membrane Proteins - metabolism</subject><subject>Microscopy, Fluorescence</subject><subject>Mitochondria</subject><subject>Muscle, Smooth, Vascular - cytology</subject><subject>Muscle, Smooth, Vascular - metabolism</subject><subject>Neurons</subject><subject>Neurons - cytology</subject><subject>Neurons - metabolism</subject><subject>Ouabain - metabolism</subject><subject>Ouabain - pharmacology</subject><subject>Physiological regulation</subject><subject>Protein isoforms</subject><subject>Pumps</subject><subject>Rats</subject><subject>Rodents</subject><subject>Sodium</subject><subject>Sodium - metabolism</subject><subject>Sodium-Potassium-Exchanging ATPase - chemistry</subject><subject>Sodium-Potassium-Exchanging ATPase - metabolism</subject><issn>0027-8424</issn><issn>1091-6490</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1997</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNptkUFv1DAQhS1EVZbClQMSksWBC0oYJ07WI3GpFmgrrSgScLacxG69SuKtHQP7s_gj_Ca82u1qizh5pPe90Rs_Ql4wyBnMy3frUYUceV7lTAA8IjMGyLKaIzwmM4Bingle8CfkaQgrAMBKwCk5RahAVDgj8rN6S7_EYU2X7idVY0cv7c0tvY6qUXak58bY0U4b-uc3_RqbmGZ6FZxxfghUeU0_WGO01-PUb9IcJm-bOOmOJu9C9314Rk6M6oN-vn_PyPdPH78tLrPl9cXV4nyZtVwUU1YVDXLUSmijOG8b1WBZdFjUneZQNDWUbVNBzYVA5C1PExqOHAy2rC66sjwj73d717EZdNemRF71cu3toPxGOmXlQ2W0t_LG_ZAMEefJ_mZv9-4u6jDJwYY2HaBG7WKQc5F-SwiWwNf_gCsX_ZhOkwWwkmMtIEH5Dmq9C8Frc8jBQG5bk9vWJHJZyW1ryfDqOP0B39d0FG_rO6j3fmli30_613S06L9g0l_u9FWYnD8AnFUcyr_OhbRN</recordid><startdate>19970304</startdate><enddate>19970304</enddate><creator>Juhaszova, Magdalena</creator><creator>Blaustein, Mordecai P.</creator><general>National Academy of Sciences of the United States of America</general><general>National Acad Sciences</general><general>National Academy of Sciences</general><general>The National Academy of Sciences of the USA</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>7SN</scope><scope>7SS</scope><scope>7T5</scope><scope>7TK</scope><scope>7TM</scope><scope>7TO</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>19970304</creationdate><title>Na+ Pump Low and High Ouabain Affinity α Subunit Isoforms are Differently Distributed in Cells</title><author>Juhaszova, Magdalena ; Blaustein, Mordecai P.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c482t-52b949ea8efa44cbab932d926de402b603cb506488994c40649f4940f9c162d33</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1997</creationdate><topic>Animals</topic><topic>Antibodies</topic><topic>Antibodies - immunology</topic><topic>Astrocytes</topic><topic>Astrocytes - metabolism</topic><topic>Biochemistry</topic><topic>Biological Sciences</topic><topic>Blotting, Western</topic><topic>Calcium</topic><topic>Calcium - metabolism</topic><topic>Cell Membrane - metabolism</topic><topic>Cells</topic><topic>Cells, Cultured</topic><topic>Cellular biology</topic><topic>Cultured cells</topic><topic>Immunohistochemistry</topic><topic>Magnification</topic><topic>Membrane Proteins - metabolism</topic><topic>Microscopy, Fluorescence</topic><topic>Mitochondria</topic><topic>Muscle, Smooth, Vascular - cytology</topic><topic>Muscle, Smooth, Vascular - metabolism</topic><topic>Neurons</topic><topic>Neurons - cytology</topic><topic>Neurons - metabolism</topic><topic>Ouabain - metabolism</topic><topic>Ouabain - pharmacology</topic><topic>Physiological regulation</topic><topic>Protein isoforms</topic><topic>Pumps</topic><topic>Rats</topic><topic>Rodents</topic><topic>Sodium</topic><topic>Sodium - metabolism</topic><topic>Sodium-Potassium-Exchanging ATPase - chemistry</topic><topic>Sodium-Potassium-Exchanging ATPase - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Juhaszova, Magdalena</creatorcontrib><creatorcontrib>Blaustein, Mordecai P.</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>Ecology Abstracts</collection><collection>Entomology Abstracts (Full archive)</collection><collection>Immunology Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Oncogenes and Growth Factors 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>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Juhaszova, Magdalena</au><au>Blaustein, Mordecai P.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Na+ Pump Low and High Ouabain Affinity α Subunit Isoforms are Differently Distributed in Cells</atitle><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle><addtitle>Proc Natl Acad Sci U S A</addtitle><date>1997-03-04</date><risdate>1997</risdate><volume>94</volume><issue>5</issue><spage>1800</spage><epage>1805</epage><pages>1800-1805</pages><issn>0027-8424</issn><eissn>1091-6490</eissn><abstract>Three isoforms (α 1, α 2, and α 3) of the catalytic (α ) subunit of the plasma membrane (PM) Na+ pump have been identified in the tissues of birds and mammals. These isoforms differ in their affinities for ions and for the Na+ pump inhibitor, ouabain. In the rat, α 1 has an unusually low affinity for ouabain. The PM of most rat cells contains both low (α 1) and high (α 2 or α 3) ouabain affinity isoforms, but precise localization of specific isoforms, and their functional significance, are unknown. We employed high resolution immunocytochemical techniques to localize α subunit isoforms in primary cultured rat astrocytes, neurons, and arterial myocytes. Isoform α 1 was ubiquitously distributed over the surfaces of these cells. In contrast, high ouabain affinity isoforms (α 2 in astrocytes, α 3 in neurons and myocytes) were confined to a reticular distribution within the PM that paralleled underlying endoplasmic or sarcoplasmic reticulum. This distribution is identical to that of the PM Na/Ca exchanger. This raises the possibility that α 1 may regulate bulk cytosolic Na+, whereas α 2 and α 3 may regulate Na+ and, indirectly, Ca2+ in a restricted cytosolic space between the PM and reticulum. The high ouabain affinity Na+ pumps may thereby modulate reticulum Ca2+ content and Ca2+ signaling.</abstract><cop>United States</cop><pub>National Academy of Sciences of the United States of America</pub><pmid>9050859</pmid><doi>10.1073/pnas.94.5.1800</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | Proceedings of the National Academy of Sciences - PNAS, 1997-03, Vol.94 (5), p.1800-1805 |
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| subjects | Animals Antibodies Antibodies - immunology Astrocytes Astrocytes - metabolism Biochemistry Biological Sciences Blotting, Western Calcium Calcium - metabolism Cell Membrane - metabolism Cells Cells, Cultured Cellular biology Cultured cells Immunohistochemistry Magnification Membrane Proteins - metabolism Microscopy, Fluorescence Mitochondria Muscle, Smooth, Vascular - cytology Muscle, Smooth, Vascular - metabolism Neurons Neurons - cytology Neurons - metabolism Ouabain - metabolism Ouabain - pharmacology Physiological regulation Protein isoforms Pumps Rats Rodents Sodium Sodium - metabolism Sodium-Potassium-Exchanging ATPase - chemistry Sodium-Potassium-Exchanging ATPase - metabolism |
| title | Na+ Pump Low and High Ouabain Affinity α Subunit Isoforms are Differently Distributed in Cells |
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