Measurement of Lens Protein Aggregation in Vivo Using Dynamic Light Scattering in a Guinea Pig/UVA Model for Nuclear Cataract
The role of UVA radiation in the formation of human nuclear cataract is not well understood. We have previously shown that exposing guinea pigs for 5 months to a chronic low level of UVA light produces increased lens nuclear light scattering and elevated levels of protein disulfide. Here we have use...
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| Veröffentlicht in: | Photochemistry and photobiology 2008-11, Vol.84 (6), p.1589-1595 |
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| creator | Francis Simpanya, M. Ansari, Rafat R. Leverenz, Victor Giblin, Frank J. |
| description | The role of UVA radiation in the formation of human nuclear cataract is not well understood. We have previously shown that exposing guinea pigs for 5 months to a chronic low level of UVA light produces increased lens nuclear light scattering and elevated levels of protein disulfide. Here we have used the technique of dynamic light scattering (DLS) to investigate lens protein aggregation in vivo in the guinea pig/UVA model. DLS size distribution analysis conducted at the same location in the lens nucleus of control and UVA‐irradiated animals showed a 28% reduction in intensity of small diameter proteins in experimental lenses compared with controls (P |
| doi_str_mv | 10.1111/j.1751-1097.2008.00390.x |
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We have previously shown that exposing guinea pigs for 5 months to a chronic low level of UVA light produces increased lens nuclear light scattering and elevated levels of protein disulfide. Here we have used the technique of dynamic light scattering (DLS) to investigate lens protein aggregation in vivo in the guinea pig/UVA model. DLS size distribution analysis conducted at the same location in the lens nucleus of control and UVA‐irradiated animals showed a 28% reduction in intensity of small diameter proteins in experimental lenses compared with controls (P < 0.05). In addition, large diameter proteins in UVA‐exposed lens nuclei increased five‐fold in intensity compared to controls (P < 0.05). The UVA‐induced increase in apparent size of lens nuclear small diameter proteins was three‐fold (P < 0.01), and the size of large diameter aggregates was more than four‐fold in experimental lenses compared with controls. The diameter of crystallin aggregates in the UVA‐irradiated lens nucleus was estimated to be 350 nm, a size able to scatter light. No significant changes in protein size were detected in the anterior cortex of UVA‐irradiated lenses. It is presumed that the presence of a UVA chromophore in the guinea pig lens (NADPH bound to zeta crystallin), as well as traces of oxygen, contributed to UVA‐induced crystallin aggregation. The results indicate a potentially harmful role for UVA light in the lens nucleus. A similar process of UVA‐irradiated protein aggregation may take place in the older human lens nucleus, accelerating the formation of human nuclear cataract.</description><identifier>ISSN: 0031-8655</identifier><identifier>EISSN: 1751-1097</identifier><identifier>DOI: 10.1111/j.1751-1097.2008.00390.x</identifier><identifier>PMID: 18627516</identifier><identifier>CODEN: PHCBAP</identifier><language>eng</language><publisher>Oxford, UK: Blackwell Publishing Ltd</publisher><subject>Animals ; Brownian motion ; Cataract - metabolism ; Cataracts ; Crystallins - analysis ; Crystallins - metabolism ; Disease Models, Animal ; Guinea Pigs ; Hair loss ; Lamps ; Male ; Older people ; Proteins ; Studies ; Ultraviolet Rays</subject><ispartof>Photochemistry and photobiology, 2008-11, Vol.84 (6), p.1589-1595</ispartof><rights>2008 The Authors. Journal Compilation. 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We have previously shown that exposing guinea pigs for 5 months to a chronic low level of UVA light produces increased lens nuclear light scattering and elevated levels of protein disulfide. Here we have used the technique of dynamic light scattering (DLS) to investigate lens protein aggregation in vivo in the guinea pig/UVA model. DLS size distribution analysis conducted at the same location in the lens nucleus of control and UVA‐irradiated animals showed a 28% reduction in intensity of small diameter proteins in experimental lenses compared with controls (P < 0.05). In addition, large diameter proteins in UVA‐exposed lens nuclei increased five‐fold in intensity compared to controls (P < 0.05). The UVA‐induced increase in apparent size of lens nuclear small diameter proteins was three‐fold (P < 0.01), and the size of large diameter aggregates was more than four‐fold in experimental lenses compared with controls. The diameter of crystallin aggregates in the UVA‐irradiated lens nucleus was estimated to be 350 nm, a size able to scatter light. No significant changes in protein size were detected in the anterior cortex of UVA‐irradiated lenses. It is presumed that the presence of a UVA chromophore in the guinea pig lens (NADPH bound to zeta crystallin), as well as traces of oxygen, contributed to UVA‐induced crystallin aggregation. The results indicate a potentially harmful role for UVA light in the lens nucleus. A similar process of UVA‐irradiated protein aggregation may take place in the older human lens nucleus, accelerating the formation of human nuclear cataract.</description><subject>Animals</subject><subject>Brownian motion</subject><subject>Cataract - metabolism</subject><subject>Cataracts</subject><subject>Crystallins - analysis</subject><subject>Crystallins - metabolism</subject><subject>Disease Models, Animal</subject><subject>Guinea Pigs</subject><subject>Hair loss</subject><subject>Lamps</subject><subject>Male</subject><subject>Older people</subject><subject>Proteins</subject><subject>Studies</subject><subject>Ultraviolet Rays</subject><issn>0031-8655</issn><issn>1751-1097</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2008</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><recordid>eNqNkl1v0zAUhiMEYmXwF5DFBXfJbCexYwkhVQU6pHZUgm4SN9Zp4mQuSbzZztZe7L_jrlX5uAHf-NjneV_5-JwoQgQnJKyzdUJ4TmKCBU8oxkWCcSpwsnkSjY6Jp9Eo3JK4YHl-Er1wbo0xyQQnz6MTUjAaODaKHuYK3GBVp3qPTI1mqndoYY1XukfjprGqAa9Nj8LxUt8ZtHS6b9CHbQ-dLtFMN9cefS3Be2V3iYABmg66V4AWujlbXo7R3FSqRbWx6GIoWwUWTcCDhdK_jJ7V0Dr16rCfRstPH79NzuPZl-nnyXgWlyxNcUwqQWBV84pCwWuacs5XKSYVxhklGYGsYoKGkFZFRXBOS0oFVHzFVQqUKZaeRu_3vjfDqlNVGYq10MobqzuwW2lAyz8zvb6WjbmTlGMqBAkGbw8G1twOynnZaVeqtoVemcFJJgrOU0H_CRLBijx_dHzzF7g2g-3DL8hQIM0wz0SAij1UWuOcVfXxyQTL3STItdw1XO4aLneTIB8nQW6C9PXvJf8SHlofgHd74F63avvfxnJxvghBkMd7uXZebY5ysD8k4ynP5dXFVH6fz6_oJGeSpD8B58bQQw</recordid><startdate>200811</startdate><enddate>200811</enddate><creator>Francis Simpanya, M.</creator><creator>Ansari, Rafat R.</creator><creator>Leverenz, Victor</creator><creator>Giblin, Frank J.</creator><general>Blackwell Publishing Ltd</general><scope>BSCLL</scope><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>3V.</scope><scope>4T-</scope><scope>7RV</scope><scope>7TM</scope><scope>7U7</scope><scope>7X2</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>88I</scope><scope>8AF</scope><scope>8AO</scope><scope>8FD</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>ATCPS</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>KB0</scope><scope>LK8</scope><scope>M0K</scope><scope>M0S</scope><scope>M1P</scope><scope>M2P</scope><scope>M7P</scope><scope>NAPCQ</scope><scope>P64</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>Q9U</scope><scope>RC3</scope><scope>S0X</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>200811</creationdate><title>Measurement of Lens Protein Aggregation in Vivo Using Dynamic Light Scattering in a Guinea Pig/UVA Model for Nuclear Cataract</title><author>Francis Simpanya, M. ; Ansari, Rafat R. ; Leverenz, Victor ; Giblin, Frank J.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c6330-1d91abf7d2a87f23777b301d0042141a4d6924212d8d1052c229ad7b7e3a26e63</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2008</creationdate><topic>Animals</topic><topic>Brownian motion</topic><topic>Cataract - 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Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Photochemistry and photobiology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Francis Simpanya, M.</au><au>Ansari, Rafat R.</au><au>Leverenz, Victor</au><au>Giblin, Frank J.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Measurement of Lens Protein Aggregation in Vivo Using Dynamic Light Scattering in a Guinea Pig/UVA Model for Nuclear Cataract</atitle><jtitle>Photochemistry and photobiology</jtitle><addtitle>Photochem Photobiol</addtitle><date>2008-11</date><risdate>2008</risdate><volume>84</volume><issue>6</issue><spage>1589</spage><epage>1595</epage><pages>1589-1595</pages><issn>0031-8655</issn><eissn>1751-1097</eissn><coden>PHCBAP</coden><abstract>The role of UVA radiation in the formation of human nuclear cataract is not well understood. We have previously shown that exposing guinea pigs for 5 months to a chronic low level of UVA light produces increased lens nuclear light scattering and elevated levels of protein disulfide. Here we have used the technique of dynamic light scattering (DLS) to investigate lens protein aggregation in vivo in the guinea pig/UVA model. DLS size distribution analysis conducted at the same location in the lens nucleus of control and UVA‐irradiated animals showed a 28% reduction in intensity of small diameter proteins in experimental lenses compared with controls (P < 0.05). In addition, large diameter proteins in UVA‐exposed lens nuclei increased five‐fold in intensity compared to controls (P < 0.05). The UVA‐induced increase in apparent size of lens nuclear small diameter proteins was three‐fold (P < 0.01), and the size of large diameter aggregates was more than four‐fold in experimental lenses compared with controls. The diameter of crystallin aggregates in the UVA‐irradiated lens nucleus was estimated to be 350 nm, a size able to scatter light. No significant changes in protein size were detected in the anterior cortex of UVA‐irradiated lenses. It is presumed that the presence of a UVA chromophore in the guinea pig lens (NADPH bound to zeta crystallin), as well as traces of oxygen, contributed to UVA‐induced crystallin aggregation. The results indicate a potentially harmful role for UVA light in the lens nucleus. A similar process of UVA‐irradiated protein aggregation may take place in the older human lens nucleus, accelerating the formation of human nuclear cataract.</abstract><cop>Oxford, UK</cop><pub>Blackwell Publishing Ltd</pub><pmid>18627516</pmid><doi>10.1111/j.1751-1097.2008.00390.x</doi><tpages>7</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Animals Brownian motion Cataract - metabolism Cataracts Crystallins - analysis Crystallins - metabolism Disease Models, Animal Guinea Pigs Hair loss Lamps Male Older people Proteins Studies Ultraviolet Rays |
| title | Measurement of Lens Protein Aggregation in Vivo Using Dynamic Light Scattering in a Guinea Pig/UVA Model for Nuclear Cataract |
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