Noninvasive Two-Photon Imaging Reveals Retinyl Ester Storage Structures in the Eye
Visual sensation in vertebrates is triggered when light strikes retinal photoreceptor cells causing photoisomerization of the rhodopsin chromophore 11-cis-retinal to all-trans-retinal. The regeneration of preillumination conditions of the photoreceptor cells requires formation of 11-cis-retinal in t...
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| Veröffentlicht in: | The Journal of cell biology 2004-02, Vol.164 (3), p.373-383 |
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| creator | Imanishi, Yoshikazu Batten, Matthew L. Piston, David W. Baehr, Wolfgang Palczewski, Krzysztof |
| description | Visual sensation in vertebrates is triggered when light strikes retinal photoreceptor cells causing photoisomerization of the rhodopsin chromophore 11-cis-retinal to all-trans-retinal. The regeneration of preillumination conditions of the photoreceptor cells requires formation of 11-cis-retinal in the adjacent retinal pigment epithelium (RPE). Using the intrinsic fluorescence of alltrans-retinyl esters, noninvasive two-photon microscopy revealed previously uncharacterized structures (6.9 ± 1.1 μm in length and 0.8 ± 0.2 μm in diameter) distinct from other cellular organelles, termed the retinyl ester storage particles (RESTs), or retinosomes. These structures form autonomous all-trans-retinyl ester-rich intracellular compartments distinct from other organelles and colocalize with adipose differentiation-related protein. As demonstrated by in vivo experiments using wild-type mice, the RESTs participate in 11-cis-retinal formation. RESTs accumulate in Rpe65-/-mice incapable of carrying out the enzymatic isomerization, and correspondingly, are absent in the eyes of Lrat-/-mice deficient in retinyl ester synthesis. These results indicate that RESTs located close to the RPE plasma membrane are essential components in 11-cis-retinal production. |
| doi_str_mv | 10.1083/jcb.200311079 |
| format | Article |
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The regeneration of preillumination conditions of the photoreceptor cells requires formation of 11-cis-retinal in the adjacent retinal pigment epithelium (RPE). Using the intrinsic fluorescence of alltrans-retinyl esters, noninvasive two-photon microscopy revealed previously uncharacterized structures (6.9 ± 1.1 μm in length and 0.8 ± 0.2 μm in diameter) distinct from other cellular organelles, termed the retinyl ester storage particles (RESTs), or retinosomes. These structures form autonomous all-trans-retinyl ester-rich intracellular compartments distinct from other organelles and colocalize with adipose differentiation-related protein. As demonstrated by in vivo experiments using wild-type mice, the RESTs participate in 11-cis-retinal formation. RESTs accumulate in Rpe65-/-mice incapable of carrying out the enzymatic isomerization, and correspondingly, are absent in the eyes of Lrat-/-mice deficient in retinyl ester synthesis. These results indicate that RESTs located close to the RPE plasma membrane are essential components in 11-cis-retinal production.</description><identifier>ISSN: 0021-9525</identifier><identifier>EISSN: 1540-8140</identifier><identifier>DOI: 10.1083/jcb.200311079</identifier><identifier>PMID: 14745001</identifier><identifier>CODEN: JCLBA3</identifier><language>eng</language><publisher>United States: Rockefeller University Press</publisher><subject>Acyltransferases - genetics ; Acyltransferases - metabolism ; Animals ; Atoms & subatomic particles ; Carrier Proteins ; Cellular biology ; cis-trans-Isomerases ; Cytoplasmic Vesicles - chemistry ; Cytoplasmic Vesicles - metabolism ; Esters ; Esters - analysis ; Eye - chemistry ; Eye - metabolism ; Eye - ultrastructure ; Eye Proteins ; Eyes ; Eyes & eyesight ; Fluorescence ; Membrane Proteins - metabolism ; Mice ; Mice, Inbred Strains ; Mice, Knockout ; Microscopy ; Microscopy, Fluorescence - methods ; Models, Molecular ; Molecular Structure ; Perilipin-2 ; Photoreceptors ; Pigment Epithelium of Eye - cytology ; Pigment Epithelium of Eye - metabolism ; Proteins - genetics ; Proteins - metabolism ; Retina ; Retinal pigments ; Retinaldehyde - administration & dosage ; Retinaldehyde - chemistry ; Retinaldehyde - metabolism ; Retinoids ; Vertebrates ; Visual Perception - physiology ; Vitamin A - chemistry ; Vitamin A - metabolism</subject><ispartof>The Journal of cell biology, 2004-02, Vol.164 (3), p.373-383</ispartof><rights>Copyright 2004 The Rockefeller University Press</rights><rights>Copyright The Rockefeller University Press</rights><rights>Copyright Rockefeller University Press Feb 2, 2004</rights><rights>Copyright © 2004, The Rockefeller University Press</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c528t-b10b0017b25089f0bb69411bef24b6b8aa1276a6c1bfdc37ee418d885c3630a3</citedby><cites>FETCH-LOGICAL-c528t-b10b0017b25089f0bb69411bef24b6b8aa1276a6c1bfdc37ee418d885c3630a3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>230,314,780,784,885,27915,27916</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/14745001$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Imanishi, Yoshikazu</creatorcontrib><creatorcontrib>Batten, Matthew L.</creatorcontrib><creatorcontrib>Piston, David W.</creatorcontrib><creatorcontrib>Baehr, Wolfgang</creatorcontrib><creatorcontrib>Palczewski, Krzysztof</creatorcontrib><title>Noninvasive Two-Photon Imaging Reveals Retinyl Ester Storage Structures in the Eye</title><title>The Journal of cell biology</title><addtitle>J Cell Biol</addtitle><description>Visual sensation in vertebrates is triggered when light strikes retinal photoreceptor cells causing photoisomerization of the rhodopsin chromophore 11-cis-retinal to all-trans-retinal. The regeneration of preillumination conditions of the photoreceptor cells requires formation of 11-cis-retinal in the adjacent retinal pigment epithelium (RPE). Using the intrinsic fluorescence of alltrans-retinyl esters, noninvasive two-photon microscopy revealed previously uncharacterized structures (6.9 ± 1.1 μm in length and 0.8 ± 0.2 μm in diameter) distinct from other cellular organelles, termed the retinyl ester storage particles (RESTs), or retinosomes. These structures form autonomous all-trans-retinyl ester-rich intracellular compartments distinct from other organelles and colocalize with adipose differentiation-related protein. As demonstrated by in vivo experiments using wild-type mice, the RESTs participate in 11-cis-retinal formation. RESTs accumulate in Rpe65-/-mice incapable of carrying out the enzymatic isomerization, and correspondingly, are absent in the eyes of Lrat-/-mice deficient in retinyl ester synthesis. These results indicate that RESTs located close to the RPE plasma membrane are essential components in 11-cis-retinal production.</description><subject>Acyltransferases - genetics</subject><subject>Acyltransferases - metabolism</subject><subject>Animals</subject><subject>Atoms & subatomic particles</subject><subject>Carrier Proteins</subject><subject>Cellular biology</subject><subject>cis-trans-Isomerases</subject><subject>Cytoplasmic Vesicles - chemistry</subject><subject>Cytoplasmic Vesicles - metabolism</subject><subject>Esters</subject><subject>Esters - analysis</subject><subject>Eye - chemistry</subject><subject>Eye - metabolism</subject><subject>Eye - ultrastructure</subject><subject>Eye Proteins</subject><subject>Eyes</subject><subject>Eyes & eyesight</subject><subject>Fluorescence</subject><subject>Membrane Proteins - metabolism</subject><subject>Mice</subject><subject>Mice, Inbred Strains</subject><subject>Mice, Knockout</subject><subject>Microscopy</subject><subject>Microscopy, Fluorescence - methods</subject><subject>Models, Molecular</subject><subject>Molecular Structure</subject><subject>Perilipin-2</subject><subject>Photoreceptors</subject><subject>Pigment Epithelium of Eye - cytology</subject><subject>Pigment Epithelium of Eye - metabolism</subject><subject>Proteins - genetics</subject><subject>Proteins - metabolism</subject><subject>Retina</subject><subject>Retinal pigments</subject><subject>Retinaldehyde - administration & dosage</subject><subject>Retinaldehyde - chemistry</subject><subject>Retinaldehyde - metabolism</subject><subject>Retinoids</subject><subject>Vertebrates</subject><subject>Visual Perception - physiology</subject><subject>Vitamin A - chemistry</subject><subject>Vitamin A - metabolism</subject><issn>0021-9525</issn><issn>1540-8140</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2004</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkUFvEzEQhS1ERUPhyA2hFQduW2bs9a73glRVASpVBZXcLdvxJo42drG9Qfn3mCZqKRdO7zDfPM28R8gbhHMEwT5ujD6nAAwRuv4ZmSFvoBbYwHMyA6BY95zyU_IypQ0ANF3DXpBTLMoBcEZub4J3fqeS29lq8SvU39chB19dbdXK-VV1a3dWjalodn4_VvOUbax-5BDVyhaNk8lTtKlyvsprW8339hU5GcqKfX3UM7L4PF9cfq2vv325ury4rg2nItcaQZcTOk05iH4Ardu-QdR2oI1utVAKadeq1qAeloZ11jYolkJww1oGip2RTwfbu0lv7dJYn6Ma5V10WxX3Mignn068W8tV2ElkbcmlKQYfjgYx_JxsynLrkrHjqLwNU5ICkAEX7X9B7JqSLGMFfP8PuAlT9CUESbFD4Oweqg-QiSGlaIeHkxHkn0plqVQ-VFr4d3__-UgfOyzA2wOwSaWWx3lLseec_QZWe6XN</recordid><startdate>20040202</startdate><enddate>20040202</enddate><creator>Imanishi, Yoshikazu</creator><creator>Batten, Matthew L.</creator><creator>Piston, David W.</creator><creator>Baehr, Wolfgang</creator><creator>Palczewski, Krzysztof</creator><general>Rockefeller University Press</general><general>The Rockefeller University Press</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>7QL</scope><scope>7QP</scope><scope>7QR</scope><scope>7TK</scope><scope>7TM</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>20040202</creationdate><title>Noninvasive Two-Photon Imaging Reveals Retinyl Ester Storage Structures in the Eye</title><author>Imanishi, Yoshikazu ; Batten, Matthew L. ; Piston, David W. ; Baehr, Wolfgang ; Palczewski, Krzysztof</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c528t-b10b0017b25089f0bb69411bef24b6b8aa1276a6c1bfdc37ee418d885c3630a3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2004</creationdate><topic>Acyltransferases - genetics</topic><topic>Acyltransferases - metabolism</topic><topic>Animals</topic><topic>Atoms & subatomic particles</topic><topic>Carrier Proteins</topic><topic>Cellular biology</topic><topic>cis-trans-Isomerases</topic><topic>Cytoplasmic Vesicles - chemistry</topic><topic>Cytoplasmic Vesicles - metabolism</topic><topic>Esters</topic><topic>Esters - analysis</topic><topic>Eye - chemistry</topic><topic>Eye - metabolism</topic><topic>Eye - ultrastructure</topic><topic>Eye Proteins</topic><topic>Eyes</topic><topic>Eyes & eyesight</topic><topic>Fluorescence</topic><topic>Membrane Proteins - metabolism</topic><topic>Mice</topic><topic>Mice, Inbred Strains</topic><topic>Mice, Knockout</topic><topic>Microscopy</topic><topic>Microscopy, Fluorescence - methods</topic><topic>Models, Molecular</topic><topic>Molecular Structure</topic><topic>Perilipin-2</topic><topic>Photoreceptors</topic><topic>Pigment Epithelium of Eye - cytology</topic><topic>Pigment Epithelium of Eye - metabolism</topic><topic>Proteins - genetics</topic><topic>Proteins - metabolism</topic><topic>Retina</topic><topic>Retinal pigments</topic><topic>Retinaldehyde - administration & dosage</topic><topic>Retinaldehyde - chemistry</topic><topic>Retinaldehyde - metabolism</topic><topic>Retinoids</topic><topic>Vertebrates</topic><topic>Visual Perception - physiology</topic><topic>Vitamin A - chemistry</topic><topic>Vitamin A - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Imanishi, Yoshikazu</creatorcontrib><creatorcontrib>Batten, Matthew L.</creatorcontrib><creatorcontrib>Piston, David W.</creatorcontrib><creatorcontrib>Baehr, Wolfgang</creatorcontrib><creatorcontrib>Palczewski, Krzysztof</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids 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>The Journal of cell biology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Imanishi, Yoshikazu</au><au>Batten, Matthew L.</au><au>Piston, David W.</au><au>Baehr, Wolfgang</au><au>Palczewski, Krzysztof</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Noninvasive Two-Photon Imaging Reveals Retinyl Ester Storage Structures in the Eye</atitle><jtitle>The Journal of cell biology</jtitle><addtitle>J Cell Biol</addtitle><date>2004-02-02</date><risdate>2004</risdate><volume>164</volume><issue>3</issue><spage>373</spage><epage>383</epage><pages>373-383</pages><issn>0021-9525</issn><eissn>1540-8140</eissn><coden>JCLBA3</coden><abstract>Visual sensation in vertebrates is triggered when light strikes retinal photoreceptor cells causing photoisomerization of the rhodopsin chromophore 11-cis-retinal to all-trans-retinal. The regeneration of preillumination conditions of the photoreceptor cells requires formation of 11-cis-retinal in the adjacent retinal pigment epithelium (RPE). Using the intrinsic fluorescence of alltrans-retinyl esters, noninvasive two-photon microscopy revealed previously uncharacterized structures (6.9 ± 1.1 μm in length and 0.8 ± 0.2 μm in diameter) distinct from other cellular organelles, termed the retinyl ester storage particles (RESTs), or retinosomes. These structures form autonomous all-trans-retinyl ester-rich intracellular compartments distinct from other organelles and colocalize with adipose differentiation-related protein. As demonstrated by in vivo experiments using wild-type mice, the RESTs participate in 11-cis-retinal formation. RESTs accumulate in Rpe65-/-mice incapable of carrying out the enzymatic isomerization, and correspondingly, are absent in the eyes of Lrat-/-mice deficient in retinyl ester synthesis. These results indicate that RESTs located close to the RPE plasma membrane are essential components in 11-cis-retinal production.</abstract><cop>United States</cop><pub>Rockefeller University Press</pub><pmid>14745001</pmid><doi>10.1083/jcb.200311079</doi><tpages>11</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | The Journal of cell biology, 2004-02, Vol.164 (3), p.373-383 |
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| subjects | Acyltransferases - genetics Acyltransferases - metabolism Animals Atoms & subatomic particles Carrier Proteins Cellular biology cis-trans-Isomerases Cytoplasmic Vesicles - chemistry Cytoplasmic Vesicles - metabolism Esters Esters - analysis Eye - chemistry Eye - metabolism Eye - ultrastructure Eye Proteins Eyes Eyes & eyesight Fluorescence Membrane Proteins - metabolism Mice Mice, Inbred Strains Mice, Knockout Microscopy Microscopy, Fluorescence - methods Models, Molecular Molecular Structure Perilipin-2 Photoreceptors Pigment Epithelium of Eye - cytology Pigment Epithelium of Eye - metabolism Proteins - genetics Proteins - metabolism Retina Retinal pigments Retinaldehyde - administration & dosage Retinaldehyde - chemistry Retinaldehyde - metabolism Retinoids Vertebrates Visual Perception - physiology Vitamin A - chemistry Vitamin A - metabolism |
| title | Noninvasive Two-Photon Imaging Reveals Retinyl Ester Storage Structures in the Eye |
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