Mass spectrometric and immunological evaluation of AGEs during incubation of ribose with gelatin
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DOI[10.24659/gsr.10.1_16]to the data of the same series
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- Material Type
- 記事
- Title
- Author/Editor
- Nana KatsutaMime NagaiRyoji Nagai
- Publication, Distribution, etc.
- Publication Date
- 2023-03-31
- Publication Date (W3CDTF)
- 2023-03-31
- Periodical title
- Glycative stress research
- No. or year of volume/issue
- 10(1)
- Volume
- 10(1)
- ISSN (Periodical Title)
- 2188-3610
- ISSN-L (Periodical Title)
- 2188-3610
- Text Language Code
- eng
- DOI
- 10.24659/gsr.10.1_16
- Persistent ID (NDL)
- info:ndljp/pid/13120795
- Collection
- Collection (Materials For Handicapped People:1)
- Collection (particular)
- 国立国会図書館デジタルコレクション > 電子書籍・電子雑誌 > その他
- Acquisition Basis
- オンライン資料収集制度
- Date Accepted (W3CDTF)
- 2023-12-08T11:19:22+09:00
- Date Captured (W3CDTF)
- 2023-05-20
- Format (IMT)
- application/pdf
- Access Restrictions
- 国立国会図書館内限定公開
- Service for the Digitized Contents Transmission Service
- 図書館・個人送信対象外
- Availability of remote photoduplication service
- 可
- Periodical Title (URI)
- Periodical Title (Persistent ID (NDL))
- info:ndljp/pid/13120792
- Data Provider (Database)
- 国立国会図書館 : 国立国会図書館デジタルコレクション
- Collection (particular)
- 国立国会図書館デジタルコレクション > 電子書籍・電子雑誌 > その他
- Access Restrictions
- 国立国会図書館内限定公開
- Service for the Digitized Contents Transmission Service
- 図書館・個人送信対象外
- Availability of remote photoduplication service
- 可
- Holding library
- 国立国会図書館
- Call No.
- Z63-D541
- Related Material (URI)
- Related Material (Persistent ID (NDL))
- info:ndljp/pid/13120795
- Data Provider (Database)
- 国立国会図書館 : 国立国会図書館雑誌記事索引
- Bibliographic ID (NDL)
- 033430112
- Bibliographic Record Category (NDL)
- 632
- Summary, etc.
- Ribose produces advanced glycation end-products (AGEs) more rapidly than glucose. It has also been reported that <i>N<sup>ε</sup></i>-(carboxymethyl)arginine (CMA) is formed in collagen, which is the most abundant protein in organisms. In this study, AGEs produced by the reaction of ribose with gelatin, a soluble collagen, were evaluated by immunochemical methods using anti-AGEs antibodies, mass spectrometry, and fluorescence intensity measurements. Measurement by enzyme-linked immunosorbent assay (ELISA) and liquid chromatography-tandem mass spectrometry (LC-MS/MS) revealed that <i>N<sup>ε</sup></i>-(carboxymethyl)lysine (CML), <i>N<sup>δ</sup></i>-(5-hydro-5-methyl-4-imidazolone-2-yl)-ornithine (MG-H1) and CMA were significantly increased in the ribose-gelatin sample compared to the gelatin alone sample after a 7-day incubation at 37°C. The fluorescence intensity at excitation and emission of 370 nm and 440 nm, respectively, was also significantly increased, whereas the AGE structure detected was unknown. In addition, the pericarp hot water extract of<i>Trapa bispinosa</i> (TBE) and/or lutein were added to this reaction system to evaluate the inhibitory effect of AGE formation. As a result, inhibition of CML, MG-H1, and CMA formation was observed at ≥ 5 μg/mL of TBE in ELISA and LC-MS/MS. However, no similar inhibitory effect was detected in fluorescence measurements, suggesting that TBE does not inhibit the formation of fluorescent AGEs. Since the inhibition of AGE formation by lutein was not confirmed, it may be a difficult compound to evaluate by in vitro studies. This study showed that ELISA and LC-MS/MS measurement can detect three types of AGEs formation in the ribose-gelatin system and that they are useful for screening compounds, e.g., TBE, that inhibit AGE formation.
- DOI
- 10.24659/gsr.10.1_16
- Access Restrictions
- インターネット公開
- Data Provider (Database)
- 科学技術振興機構 : J-STAGE
- Summary, etc.
- Ribose produces advanced glycation end-products (AGEs) more rapidly than glucose. It has also been reported that <i>N<sup>ε</sup></i>-(carboxymethyl)arginine (CMA) is formed in collagen, which is the most abundant protein in organisms. In this study, AGEs produced by the reaction of ribose with gelatin, a soluble collagen, were evaluated by immunochemical methods using anti-AGEs antibodies, mass spectrometry, and fluorescence intensity measurements. Measurement by enzyme-linked immunosorbent assay (ELISA) and liquid chromatography-tandem mass spectrometry (LC-MS/MS) revealed that <i>N<sup>ε</sup></i>-(carboxymethyl)lysine (CML), <i>N<sup>δ</sup></i>-(5-hydro-5-methyl-4-imidazolone-2-yl)-ornithine (MG-H1) and CMA were significantly increased in the ribose-gelatin sample compared to the gelatin alone sample after a 7-day incubation at 37°C. The fluorescence intensity at excitation and emission of 370 nm and 440 nm, respectively, was also significantly increased, whereas the AGE structure detected was unknown. In addition, the pericarp hot water extract of<i>Trapa bispinosa</i> (TBE) and/or lutein were added to this reaction system to evaluate the inhibitory effect of AGE formation. As a result, inhibition of CML, MG-H1, and CMA formation was observed at ≥ 5 μg/mL of TBE in ELISA and LC-MS/MS. However, no similar inhibitory effect was detected in fluorescence measurements, suggesting that TBE does not inhibit the formation of fluorescent AGEs. Since the inhibition of AGE formation by lutein was not confirmed, it may be a difficult compound to evaluate by in vitro studies. This study showed that ELISA and LC-MS/MS measurement can detect three types of AGEs formation in the ribose-gelatin system and that they are useful for screening compounds, e.g., TBE, that inhibit AGE formation.
- DOI
- 10.24659/gsr.10.1_16
- Related Material (URI)
- Data Provider (Database)
- 国立情報学研究所 : CiNii Research
- Original Data Provider (Database)
- Japan Link Center雑誌記事索引データベース雑誌記事索引データベース
- Bibliographic ID (NDL)
- 03343011213120795