Differential proteomics analysis of proteins from human diabetic and age-related cataractous lenses
Backgound: To investigate the differential lens proteomics between diabetic cataract, age-related cataract, and natural subjects. Materials and Methods: Two-dimensional electrophoresis (2-DE), mass spectrometry (MS), and enzyme-linked immunosorbent assay (ELISA) were employed. Total soluble proteins...
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| Format: | Article |
| Language: | English |
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Wolters Kluwer Medknow Publications
2013-01-01
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| Series: | Journal of Research in Medical Sciences |
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| Online Access: | http://www.jmsjournal.net/article.asp?issn=1735-1995;year=2013;volume=18;issue=11;spage=984;epage=989;aulast=Zhu |
| _version_ | 1828416723871596544 |
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| author | Jing Zhu Jun Shao Yong Yao Zhao Dong Chu Qian Qian Yu Wei Zhao Qing Lin Zi Yin Zhang |
| author_facet | Jing Zhu Jun Shao Yong Yao Zhao Dong Chu Qian Qian Yu Wei Zhao Qing Lin Zi Yin Zhang |
| author_sort | Jing Zhu |
| collection | DOAJ |
| description | Backgound: To investigate the differential lens proteomics between diabetic cataract, age-related cataract, and natural subjects. Materials and Methods: Two-dimensional electrophoresis (2-DE), mass spectrometry (MS), and enzyme-linked immunosorbent assay (ELISA) were employed. Total soluble proteins in lenses of type I diabetic cataract, age-related cataract (nondiabetic) patients, and normal control were extracted and subjected to 2-DE. The differential protein spots were recovered, digested with trypsin, and further applied to MALDI-TOF-MS. ELISA analysis was used to determine the levels of differential proteins in lenses of three groups. Results: 2-DE analysis reflected that lens proteins of normal control, diabetic, and age-related cataract subjects were in the section of pH 5-9 and the relative molecular weights were 14-97 kDa, while relative molecular weight of more abundant crystallines was localized at 20-31 kDa. five differential protein spots were detected and identified using MALDI-TOF-MS, including beta-crystallin A3, alpha-crystallin B chain, chain A of crystal structure of truncated human beta-B1-crystallin, beta-crystallin B1, and an interesting unnamed protein product highly similar to alpha-crystallin B chain, respectively. ELISA analysis revealed that lenses of diabetic cataract patients should contain significantly more concentrations of beta-crystallin A3, alpha-crystallin B chain, and beta-crystallin B1 than those of age-related cataract patients and normal control. Conclusion: This study clearly reflected the differential proteins of diabetic cataract, age-related cataract lenses compared with natural subjects, and it is helpful for the further research on the principles and mechanisms of different types of cataract. |
| first_indexed | 2024-12-10T14:06:34Z |
| format | Article |
| id | doaj.art-687838fbb22f4aa29b2c007f54c6eb03 |
| institution | Directory Open Access Journal |
| issn | 1735-1995 1735-7136 |
| language | English |
| last_indexed | 2024-12-10T14:06:34Z |
| publishDate | 2013-01-01 |
| publisher | Wolters Kluwer Medknow Publications |
| record_format | Article |
| series | Journal of Research in Medical Sciences |
| spelling | doaj.art-687838fbb22f4aa29b2c007f54c6eb032022-12-22T01:45:38ZengWolters Kluwer Medknow PublicationsJournal of Research in Medical Sciences1735-19951735-71362013-01-011811984989Differential proteomics analysis of proteins from human diabetic and age-related cataractous lensesJing ZhuJun ShaoYong YaoZhao Dong ChuQian Qian YuWei ZhaoQing LinZi Yin ZhangBackgound: To investigate the differential lens proteomics between diabetic cataract, age-related cataract, and natural subjects. Materials and Methods: Two-dimensional electrophoresis (2-DE), mass spectrometry (MS), and enzyme-linked immunosorbent assay (ELISA) were employed. Total soluble proteins in lenses of type I diabetic cataract, age-related cataract (nondiabetic) patients, and normal control were extracted and subjected to 2-DE. The differential protein spots were recovered, digested with trypsin, and further applied to MALDI-TOF-MS. ELISA analysis was used to determine the levels of differential proteins in lenses of three groups. Results: 2-DE analysis reflected that lens proteins of normal control, diabetic, and age-related cataract subjects were in the section of pH 5-9 and the relative molecular weights were 14-97 kDa, while relative molecular weight of more abundant crystallines was localized at 20-31 kDa. five differential protein spots were detected and identified using MALDI-TOF-MS, including beta-crystallin A3, alpha-crystallin B chain, chain A of crystal structure of truncated human beta-B1-crystallin, beta-crystallin B1, and an interesting unnamed protein product highly similar to alpha-crystallin B chain, respectively. ELISA analysis revealed that lenses of diabetic cataract patients should contain significantly more concentrations of beta-crystallin A3, alpha-crystallin B chain, and beta-crystallin B1 than those of age-related cataract patients and normal control. Conclusion: This study clearly reflected the differential proteins of diabetic cataract, age-related cataract lenses compared with natural subjects, and it is helpful for the further research on the principles and mechanisms of different types of cataract.http://www.jmsjournal.net/article.asp?issn=1735-1995;year=2013;volume=18;issue=11;spage=984;epage=989;aulast=ZhuAge-related cataractcrystallinediabetic cataractmass spectrometryproteomicstwo dimensional electrophoresis |
| spellingShingle | Jing Zhu Jun Shao Yong Yao Zhao Dong Chu Qian Qian Yu Wei Zhao Qing Lin Zi Yin Zhang Differential proteomics analysis of proteins from human diabetic and age-related cataractous lenses Journal of Research in Medical Sciences Age-related cataract crystalline diabetic cataract mass spectrometry proteomics two dimensional electrophoresis |
| title | Differential proteomics analysis of proteins from human diabetic and age-related cataractous lenses |
| title_full | Differential proteomics analysis of proteins from human diabetic and age-related cataractous lenses |
| title_fullStr | Differential proteomics analysis of proteins from human diabetic and age-related cataractous lenses |
| title_full_unstemmed | Differential proteomics analysis of proteins from human diabetic and age-related cataractous lenses |
| title_short | Differential proteomics analysis of proteins from human diabetic and age-related cataractous lenses |
| title_sort | differential proteomics analysis of proteins from human diabetic and age related cataractous lenses |
| topic | Age-related cataract crystalline diabetic cataract mass spectrometry proteomics two dimensional electrophoresis |
| url | http://www.jmsjournal.net/article.asp?issn=1735-1995;year=2013;volume=18;issue=11;spage=984;epage=989;aulast=Zhu |
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