Intracellular localization and membrane topology of 11-cis retinol dehydrogenase in the retinal pigment epithelium suggest a compartmentalized synthesis of 11-cis retinaldehyde
11-cis retinol dehydrogenase (EC 1.1.1.105) catalyses the last step in the biosynthetic pathway generating 11-cis retinaldehyde, the common chromophore of all visual pigments in higher animals. The enzyme is abundantly expressed in retinal pigment epithelium of the eye and is a member of the short c...
Gespeichert in:
| Veröffentlicht in: | Journal of cell science 1999-02, Vol.112 ( Pt 4) (4), p.549-558 |
|---|---|
| Hauptverfasser: | , , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 558 |
|---|---|
| container_issue | 4 |
| container_start_page | 549 |
| container_title | Journal of cell science |
| container_volume | 112 ( Pt 4) |
| creator | Simon, A Romert, A Gustafson, A L McCaffery, J M Eriksson, U |
| description | 11-cis retinol dehydrogenase (EC 1.1.1.105) catalyses the last step in the biosynthetic pathway generating 11-cis retinaldehyde, the common chromophore of all visual pigments in higher animals. The enzyme is abundantly expressed in retinal pigment epithelium of the eye and is a member of the short chain dehydrogenase/reductase superfamily. In this work we demonstrate that a majority of 11-cis retinol dehydrogenase is associated with the smooth ER in retinal pigment epithelial cells and that the enzyme is an integral membrane protein, anchored to membranes by two hydrophobic peptide segments. The catalytic domain of the enzyme is confined to a lumenal compartment and is not present on the cytosolic aspect of membranes. Thus, the subcellular localization and the membrane topology of 11-cis retinol dehydrogenase suggest that generation of 11-cis retinaldehyde is a compartmentalized process. |
| doi_str_mv | 10.1242/jcs.112.4.549 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_swepu</sourceid><recordid>TN_cdi_swepub_primary_oai_swepub_ki_se_432557</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>69556832</sourcerecordid><originalsourceid>FETCH-LOGICAL-c427t-4de9cd8c88563024189637527c0cd88f0a4bfc63d11f5bfb600cd174f08efa133</originalsourceid><addsrcrecordid>eNpdkUtv1DAUhS1EVYa2S5ZIXrHL4GccL1HFo1IlNnRtOc516uLEwU6Ehl_FT8TDjIrE6l4dfzpHvgehN5TsKRPs_ZMre0rZXuyl0C_QjgqlGk25eol2hDDaaMn5K_S6lCdCiGJaXaJLramgbbtDv-_mNVsHMW7RZhyTszH8smtIM7bzgCeY-mxnwGtaUkzjASePKW1cKDjDGuYU8QCPhyGnEWZbAIcZr49werQRL2GcYF4xLKHKMWwTLts4QlmxxS5Ni83rETjGwoDLYa5Yqe7_5dj4Nwau0YW3scDNeV6hh08fv91-ae6_fr67_XDfOMHU2ogBtBs613Wy5YQJ2umWK8mUI1XuPLGi967lA6Ve9r5vSdWpEp504C3l_Ao1J9_yE5atN0sOk80Hk2wwZ-l73cAIzqRUlX934pecfmz1e2YK5XjXery0FdNqKduOs3_GLqdSMvhna0rMsVFTGzW1USNMbbTyb8_GWz_B8EyfK-R_APlEoho</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>69556832</pqid></control><display><type>article</type><title>Intracellular localization and membrane topology of 11-cis retinol dehydrogenase in the retinal pigment epithelium suggest a compartmentalized synthesis of 11-cis retinaldehyde</title><source>MEDLINE</source><source>Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals</source><source>Company of Biologists</source><creator>Simon, A ; Romert, A ; Gustafson, A L ; McCaffery, J M ; Eriksson, U</creator><creatorcontrib>Simon, A ; Romert, A ; Gustafson, A L ; McCaffery, J M ; Eriksson, U</creatorcontrib><description>11-cis retinol dehydrogenase (EC 1.1.1.105) catalyses the last step in the biosynthetic pathway generating 11-cis retinaldehyde, the common chromophore of all visual pigments in higher animals. The enzyme is abundantly expressed in retinal pigment epithelium of the eye and is a member of the short chain dehydrogenase/reductase superfamily. In this work we demonstrate that a majority of 11-cis retinol dehydrogenase is associated with the smooth ER in retinal pigment epithelial cells and that the enzyme is an integral membrane protein, anchored to membranes by two hydrophobic peptide segments. The catalytic domain of the enzyme is confined to a lumenal compartment and is not present on the cytosolic aspect of membranes. Thus, the subcellular localization and the membrane topology of 11-cis retinol dehydrogenase suggest that generation of 11-cis retinaldehyde is a compartmentalized process.</description><identifier>ISSN: 0021-9533</identifier><identifier>EISSN: 1477-9137</identifier><identifier>DOI: 10.1242/jcs.112.4.549</identifier><identifier>PMID: 9914166</identifier><language>eng</language><publisher>England</publisher><subject>Alcohol Oxidoreductases - chemistry ; Alcohol Oxidoreductases - metabolism ; Animals ; Catalytic Domain ; Cattle ; Cell Compartmentation - physiology ; Endopeptidase K - metabolism ; Endoplasmic Reticulum, Smooth - metabolism ; Endoplasmic Reticulum, Smooth - ultrastructure ; Hexosaminidases - metabolism ; Immunohistochemistry ; Intracellular Membranes - metabolism ; Membrane Proteins - metabolism ; Microscopy, Electron ; Microsomes - enzymology ; Microsomes - metabolism ; Pigment Epithelium of Eye - enzymology ; Pigment Epithelium of Eye - metabolism ; Pigment Epithelium of Eye - ultrastructure ; Recombinant Proteins - metabolism ; Retina - metabolism ; Retina - ultrastructure ; Retinaldehyde - biosynthesis ; Subcellular Fractions - metabolism</subject><ispartof>Journal of cell science, 1999-02, Vol.112 ( Pt 4) (4), p.549-558</ispartof><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c427t-4de9cd8c88563024189637527c0cd88f0a4bfc63d11f5bfb600cd174f08efa133</citedby><cites>FETCH-LOGICAL-c427t-4de9cd8c88563024189637527c0cd88f0a4bfc63d11f5bfb600cd174f08efa133</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>230,314,776,780,881,3665,27901,27902</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/9914166$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttp://kipublications.ki.se/Default.aspx?queryparsed=id:15557995$$DView record from Swedish Publication Index$$Hfree_for_read</backlink></links><search><creatorcontrib>Simon, A</creatorcontrib><creatorcontrib>Romert, A</creatorcontrib><creatorcontrib>Gustafson, A L</creatorcontrib><creatorcontrib>McCaffery, J M</creatorcontrib><creatorcontrib>Eriksson, U</creatorcontrib><title>Intracellular localization and membrane topology of 11-cis retinol dehydrogenase in the retinal pigment epithelium suggest a compartmentalized synthesis of 11-cis retinaldehyde</title><title>Journal of cell science</title><addtitle>J Cell Sci</addtitle><description>11-cis retinol dehydrogenase (EC 1.1.1.105) catalyses the last step in the biosynthetic pathway generating 11-cis retinaldehyde, the common chromophore of all visual pigments in higher animals. The enzyme is abundantly expressed in retinal pigment epithelium of the eye and is a member of the short chain dehydrogenase/reductase superfamily. In this work we demonstrate that a majority of 11-cis retinol dehydrogenase is associated with the smooth ER in retinal pigment epithelial cells and that the enzyme is an integral membrane protein, anchored to membranes by two hydrophobic peptide segments. The catalytic domain of the enzyme is confined to a lumenal compartment and is not present on the cytosolic aspect of membranes. Thus, the subcellular localization and the membrane topology of 11-cis retinol dehydrogenase suggest that generation of 11-cis retinaldehyde is a compartmentalized process.</description><subject>Alcohol Oxidoreductases - chemistry</subject><subject>Alcohol Oxidoreductases - metabolism</subject><subject>Animals</subject><subject>Catalytic Domain</subject><subject>Cattle</subject><subject>Cell Compartmentation - physiology</subject><subject>Endopeptidase K - metabolism</subject><subject>Endoplasmic Reticulum, Smooth - metabolism</subject><subject>Endoplasmic Reticulum, Smooth - ultrastructure</subject><subject>Hexosaminidases - metabolism</subject><subject>Immunohistochemistry</subject><subject>Intracellular Membranes - metabolism</subject><subject>Membrane Proteins - metabolism</subject><subject>Microscopy, Electron</subject><subject>Microsomes - enzymology</subject><subject>Microsomes - metabolism</subject><subject>Pigment Epithelium of Eye - enzymology</subject><subject>Pigment Epithelium of Eye - metabolism</subject><subject>Pigment Epithelium of Eye - ultrastructure</subject><subject>Recombinant Proteins - metabolism</subject><subject>Retina - metabolism</subject><subject>Retina - ultrastructure</subject><subject>Retinaldehyde - biosynthesis</subject><subject>Subcellular Fractions - metabolism</subject><issn>0021-9533</issn><issn>1477-9137</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1999</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpdkUtv1DAUhS1EVYa2S5ZIXrHL4GccL1HFo1IlNnRtOc516uLEwU6Ehl_FT8TDjIrE6l4dfzpHvgehN5TsKRPs_ZMre0rZXuyl0C_QjgqlGk25eol2hDDaaMn5K_S6lCdCiGJaXaJLramgbbtDv-_mNVsHMW7RZhyTszH8smtIM7bzgCeY-mxnwGtaUkzjASePKW1cKDjDGuYU8QCPhyGnEWZbAIcZr49werQRL2GcYF4xLKHKMWwTLts4QlmxxS5Ni83rETjGwoDLYa5Yqe7_5dj4Nwau0YW3scDNeV6hh08fv91-ae6_fr67_XDfOMHU2ogBtBs613Wy5YQJ2umWK8mUI1XuPLGi967lA6Ve9r5vSdWpEp504C3l_Ao1J9_yE5atN0sOk80Hk2wwZ-l73cAIzqRUlX934pecfmz1e2YK5XjXery0FdNqKduOs3_GLqdSMvhna0rMsVFTGzW1USNMbbTyb8_GWz_B8EyfK-R_APlEoho</recordid><startdate>19990215</startdate><enddate>19990215</enddate><creator>Simon, A</creator><creator>Romert, A</creator><creator>Gustafson, A L</creator><creator>McCaffery, J M</creator><creator>Eriksson, U</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><scope>ADTPV</scope><scope>AOWAS</scope></search><sort><creationdate>19990215</creationdate><title>Intracellular localization and membrane topology of 11-cis retinol dehydrogenase in the retinal pigment epithelium suggest a compartmentalized synthesis of 11-cis retinaldehyde</title><author>Simon, A ; Romert, A ; Gustafson, A L ; McCaffery, J M ; Eriksson, U</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c427t-4de9cd8c88563024189637527c0cd88f0a4bfc63d11f5bfb600cd174f08efa133</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1999</creationdate><topic>Alcohol Oxidoreductases - chemistry</topic><topic>Alcohol Oxidoreductases - metabolism</topic><topic>Animals</topic><topic>Catalytic Domain</topic><topic>Cattle</topic><topic>Cell Compartmentation - physiology</topic><topic>Endopeptidase K - metabolism</topic><topic>Endoplasmic Reticulum, Smooth - metabolism</topic><topic>Endoplasmic Reticulum, Smooth - ultrastructure</topic><topic>Hexosaminidases - metabolism</topic><topic>Immunohistochemistry</topic><topic>Intracellular Membranes - metabolism</topic><topic>Membrane Proteins - metabolism</topic><topic>Microscopy, Electron</topic><topic>Microsomes - enzymology</topic><topic>Microsomes - metabolism</topic><topic>Pigment Epithelium of Eye - enzymology</topic><topic>Pigment Epithelium of Eye - metabolism</topic><topic>Pigment Epithelium of Eye - ultrastructure</topic><topic>Recombinant Proteins - metabolism</topic><topic>Retina - metabolism</topic><topic>Retina - ultrastructure</topic><topic>Retinaldehyde - biosynthesis</topic><topic>Subcellular Fractions - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Simon, A</creatorcontrib><creatorcontrib>Romert, A</creatorcontrib><creatorcontrib>Gustafson, A L</creatorcontrib><creatorcontrib>McCaffery, J M</creatorcontrib><creatorcontrib>Eriksson, U</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><collection>SwePub</collection><collection>SwePub Articles</collection><jtitle>Journal of cell science</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Simon, A</au><au>Romert, A</au><au>Gustafson, A L</au><au>McCaffery, J M</au><au>Eriksson, U</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Intracellular localization and membrane topology of 11-cis retinol dehydrogenase in the retinal pigment epithelium suggest a compartmentalized synthesis of 11-cis retinaldehyde</atitle><jtitle>Journal of cell science</jtitle><addtitle>J Cell Sci</addtitle><date>1999-02-15</date><risdate>1999</risdate><volume>112 ( Pt 4)</volume><issue>4</issue><spage>549</spage><epage>558</epage><pages>549-558</pages><issn>0021-9533</issn><eissn>1477-9137</eissn><abstract>11-cis retinol dehydrogenase (EC 1.1.1.105) catalyses the last step in the biosynthetic pathway generating 11-cis retinaldehyde, the common chromophore of all visual pigments in higher animals. The enzyme is abundantly expressed in retinal pigment epithelium of the eye and is a member of the short chain dehydrogenase/reductase superfamily. In this work we demonstrate that a majority of 11-cis retinol dehydrogenase is associated with the smooth ER in retinal pigment epithelial cells and that the enzyme is an integral membrane protein, anchored to membranes by two hydrophobic peptide segments. The catalytic domain of the enzyme is confined to a lumenal compartment and is not present on the cytosolic aspect of membranes. Thus, the subcellular localization and the membrane topology of 11-cis retinol dehydrogenase suggest that generation of 11-cis retinaldehyde is a compartmentalized process.</abstract><cop>England</cop><pmid>9914166</pmid><doi>10.1242/jcs.112.4.549</doi><tpages>10</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0021-9533 |
| ispartof | Journal of cell science, 1999-02, Vol.112 ( Pt 4) (4), p.549-558 |
| issn | 0021-9533 1477-9137 |
| language | eng |
| recordid | cdi_swepub_primary_oai_swepub_ki_se_432557 |
| source | MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Company of Biologists |
| subjects | Alcohol Oxidoreductases - chemistry Alcohol Oxidoreductases - metabolism Animals Catalytic Domain Cattle Cell Compartmentation - physiology Endopeptidase K - metabolism Endoplasmic Reticulum, Smooth - metabolism Endoplasmic Reticulum, Smooth - ultrastructure Hexosaminidases - metabolism Immunohistochemistry Intracellular Membranes - metabolism Membrane Proteins - metabolism Microscopy, Electron Microsomes - enzymology Microsomes - metabolism Pigment Epithelium of Eye - enzymology Pigment Epithelium of Eye - metabolism Pigment Epithelium of Eye - ultrastructure Recombinant Proteins - metabolism Retina - metabolism Retina - ultrastructure Retinaldehyde - biosynthesis Subcellular Fractions - metabolism |
| title | Intracellular localization and membrane topology of 11-cis retinol dehydrogenase in the retinal pigment epithelium suggest a compartmentalized synthesis of 11-cis retinaldehyde |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-02-19T08%3A06%3A34IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_swepu&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Intracellular%20localization%20and%20membrane%20topology%20of%2011-cis%20retinol%20dehydrogenase%20in%20the%20retinal%20pigment%20epithelium%20suggest%20a%20compartmentalized%20synthesis%20of%2011-cis%20retinaldehyde&rft.jtitle=Journal%20of%20cell%20science&rft.au=Simon,%20A&rft.date=1999-02-15&rft.volume=112%20(%20Pt%204)&rft.issue=4&rft.spage=549&rft.epage=558&rft.pages=549-558&rft.issn=0021-9533&rft.eissn=1477-9137&rft_id=info:doi/10.1242/jcs.112.4.549&rft_dat=%3Cproquest_swepu%3E69556832%3C/proquest_swepu%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=69556832&rft_id=info:pmid/9914166&rfr_iscdi=true |