Identification of the Primary Targets of Carbamylation in Bovine Lens Proteins by Mass Spectrometry
Purpose: Carbamylation, an important post-translational modification of proteins, inevitably causes conformational changes of lens proteins. It may increase aggregation between crystallin molecules and disrupt the close packing required for transparency thus leading to cataract. The aim of this stud...
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Published in | Current eye research Vol. 33; no. 11-12; pp. 963 - 976 |
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Main Authors | , , , , , |
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Language | English |
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01.01.2008
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Abstract | Purpose: Carbamylation, an important post-translational modification of proteins, inevitably causes conformational changes of lens proteins. It may increase aggregation between crystallin molecules and disrupt the close packing required for transparency thus leading to cataract. The aim of this study was to isolate the primary targets of carbamylation in the lens and identify them by mass spectrometry. Materials and Methods: Fresh intact bovine lenses were incubated with 100 mM potassium cyanate for 7 days. The proteins in the water-soluble fractions from the normal control and the cyanate-modified lens proteins were separated by two-dimensional (2-D) gel electrophoresis with identification after silver staining. Protein spots that differed between the normal and carbamylated groups were selected for further analysis using matrix-assisted laser desorption ionization time-of-flight mass spectrometry (MALDI-TOF-MS). Results: The 2-D gel results showed that the major lens proteins were in the section of pI 5-8, with relative molecular masses of 20-35 kDa, and changes in the carbamylated fraction like strings of beads indicating modification. The mass spectrometry analysis and a database search identified carbamylated proteins originating from αA-crystallin, βB2- and γS-(βS)-crystallins. Conclusions: These crystallins may be vulnerable proteins targeted by carbamylation. The accumulated aggregation and loss of chaperone activity may contribute to cataract formation. |
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AbstractList | PURPOSECarbamylation, an important post-translational modification of proteins, inevitably causes conformational changes of lens proteins. It may increase aggregation between crystallin molecules and disrupt the close packing required for transparency thus leading to cataract. The aim of this study was to isolate the primary targets of carbamylation in the lens and identify them by mass spectrometry.MATERIALS AND METHODSFresh intact bovine lenses were incubated with 100 mM potassium cyanate for 7 days. The proteins in the water-soluble fractions from the normal control and the cyanate-modified lens proteins were separated by two-dimensional (2-D) gel electrophoresis with identification after silver staining. Protein spots that differed between the normal and carbamylated groups were selected for further analysis using matrix-assisted laser desorption ionization time-of-flight mass spectrometry (MALDI-TOF-MS).RESULTSThe 2-D gel results showed that the major lens proteins were in the section of pI 5-8, with relative molecular masses of 20-35 kDa, and changes in the carbamylated fraction like strings of beads indicating modification. The mass spectrometry analysis and a database search identified carbamylated proteins originating from alphaA-crystallin, betaB2- and gammaS-(betaS)-crystallins.CONCLUSIONSThese crystallins may be vulnerable proteins targeted by carbamylation. The accumulated aggregation and loss of chaperone activity may contribute to cataract formation. Purpose: Carbamylation, an important post-translational modification of proteins, inevitably causes conformational changes of lens proteins. It may increase aggregation between crystallin molecules and disrupt the close packing required for transparency thus leading to cataract. The aim of this study was to isolate the primary targets of carbamylation in the lens and identify them by mass spectrometry. Materials and Methods: Fresh intact bovine lenses were incubated with 100 mM potassium cyanate for 7 days. The proteins in the water-soluble fractions from the normal control and the cyanate-modified lens proteins were separated by two-dimensional (2-D) gel electrophoresis with identification after silver staining. Protein spots that differed between the normal and carbamylated groups were selected for further analysis using matrix-assisted laser desorption ionization time-of-flight mass spectrometry (MALDI-TOF-MS). Results: The 2-D gel results showed that the major lens proteins were in the section of pI 5-8, with relative molecular masses of 20-35 kDa, and changes in the carbamylated fraction like strings of beads indicating modification. The mass spectrometry analysis and a database search identified carbamylated proteins originating from αA-crystallin, βB2- and γS-(βS)-crystallins. Conclusions: These crystallins may be vulnerable proteins targeted by carbamylation. The accumulated aggregation and loss of chaperone activity may contribute to cataract formation. Carbamylation, an important post-translational modification of proteins, inevitably causes conformational changes of lens proteins. It may increase aggregation between crystallin molecules and disrupt the close packing required for transparency thus leading to cataract. The aim of this study was to isolate the primary targets of carbamylation in the lens and identify them by mass spectrometry. Fresh intact bovine lenses were incubated with 100 mM potassium cyanate for 7 days. The proteins in the water-soluble fractions from the normal control and the cyanate-modified lens proteins were separated by two-dimensional (2-D) gel electrophoresis with identification after silver staining. Protein spots that differed between the normal and carbamylated groups were selected for further analysis using matrix-assisted laser desorption ionization time-of-flight mass spectrometry (MALDI-TOF-MS). The 2-D gel results showed that the major lens proteins were in the section of pI 5-8, with relative molecular masses of 20-35 kDa, and changes in the carbamylated fraction like strings of beads indicating modification. The mass spectrometry analysis and a database search identified carbamylated proteins originating from alphaA-crystallin, betaB2- and gammaS-(betaS)-crystallins. These crystallins may be vulnerable proteins targeted by carbamylation. The accumulated aggregation and loss of chaperone activity may contribute to cataract formation. |
Author | Ruan, Yu-Song Zhang, Jie Harding, John J. Wang, Xin Yan, Hong Liu, Zhen-Xiong |
Author_xml | – sequence: 1 givenname: Jie surname: Zhang fullname: Zhang, Jie organization: 1Department of Ophthalmology, Tangdu Hospital, Fourth Military Medical University, Xi'an, China – sequence: 2 givenname: Hong surname: Yan fullname: Yan, Hong organization: 1Department of Ophthalmology, Tangdu Hospital, Fourth Military Medical University, Xi'an, China – sequence: 3 givenname: John J. surname: Harding fullname: Harding, John J. organization: 1Department of Ophthalmology, Tangdu Hospital, Fourth Military Medical University, Xi'an, China – sequence: 4 givenname: Zhen-Xiong surname: Liu fullname: Liu, Zhen-Xiong organization: 1Department of Ophthalmology, Tangdu Hospital, Fourth Military Medical University, Xi'an, China – sequence: 5 givenname: Xin surname: Wang fullname: Wang, Xin organization: 1Department of Ophthalmology, Tangdu Hospital, Fourth Military Medical University, Xi'an, China – sequence: 6 givenname: Yu-Song surname: Ruan fullname: Ruan, Yu-Song organization: 1Department of Ophthalmology, Tangdu Hospital, Fourth Military Medical University, Xi'an, China |
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References_xml | – start-page: 207 volume-title: The Eye year: 1984 ident: CIT0007 doi: 10.1016/B978-0-12-206921-5.50008-8 contributor: fullname: Harding JJ – volume: 6 start-page: 3935 year: 2007 ident: CIT0012 publication-title: J Proteome Res doi: 10.1021/pr070138h contributor: fullname: Hains PG – volume: 223 start-page: 221 year: 1984 ident: CIT0018 publication-title: Biochem J doi: 10.1042/bj2230221 contributor: fullname: Beswick HT – volume: 41 start-page: 14645 year: 2002 ident: CIT0037 publication-title: Biochemistry doi: 10.1021/bi0267700 contributor: fullname: Lapko VN – volume: 6 start-page: 499 volume-title: Protein Misfolding, Aggregation, and Conformational Diseases. Part B. year: 2007 ident: CIT0003 doi: 10.1007/978-0-387-36534-3_25 contributor: fullname: Harding JJ – volume: 29 start-page: 421 year: 1997 ident: CIT0028 publication-title: Ophthalmic Res doi: 10.1159/000268043 contributor: fullname: Plater ML – volume: 11 start-page: 785 year: 1990 ident: CIT0023 publication-title: Electrophoresis doi: 10.1002/elps.1150111003 contributor: fullname: Rabilloud T – volume: 129 start-page: 97 year: 1972 ident: CIT0001 publication-title: Biochem J doi: 10.1042/bj1290097 contributor: fullname: Harding JJ – volume: 10 start-page: 1130 year: 2001 ident: CIT0020 publication-title: Protein Sci doi: 10.1110/ps.40901 contributor: fullname: Lapko VN – volume: 222 start-page: 626 year: 1996 ident: CIT0026 publication-title: Biophys Res doi: 10.1006/bbrc.1996.0794 contributor: fullname: Ganea E – volume: 262 start-page: 909 year: 1989 ident: CIT0017 publication-title: Biochem J doi: 10.1042/bj2620909 contributor: fullname: Martin S – volume: 374 start-page: 677 year: 2003 ident: CIT0021 publication-title: Biochem J doi: 10.1042/bj20030542 contributor: fullname: Yan H – volume: 1 start-page: 1111 year: 1986 ident: CIT0010 publication-title: Lancet doi: 10.1016/S0140-6736(86)91834-9 contributor: fullname: van Heyningen R – volume: 267 start-page: 26128 year: 1992 ident: CIT0024 publication-title: J Biol Chem doi: 10.1016/S0021-9258(18)35726-0 contributor: fullname: Qin W – volume: 14 start-page: 1282 year: 2005 ident: CIT0034 publication-title: Protein Sci doi: 10.1110/ps.041227805 contributor: fullname: Macdonald JT – ident: CIT0011 doi: 10.1021/pr050473a – volume: 1 start-page: 751 year: 1984 ident: CIT0008 publication-title: Lancet doi: 10.1016/S0140-6736(84)91274-1 contributor: fullname: Minassian DC – volume: 45 start-page: 569 year: 1987 ident: CIT0019 publication-title: Exp Eye Res doi: 10.1016/S0014-4835(87)80067-2 contributor: fullname: Beswick HT – volume: 161 start-page: 225 year: 1983 ident: CIT0030 publication-title: FEBS Lett doi: 10.1016/0014-5793(83)81013-8 contributor: fullname: Berbers GAM – volume: 73 start-page: 100 year: 1989 ident: CIT0009 publication-title: Br J Ophthalmol doi: 10.1136/bjo.73.2.100 contributor: fullname: Minassian DC – volume: 28 start-page: 739 year: 1979 ident: CIT0022 publication-title: Exp Eye Res doi: 10.1016/0014-4835(79)90074-5 contributor: fullname: Owers J – volume: 4 start-page: 1030 year: 1965 ident: CIT0013 publication-title: Biochemistry doi: 10.1021/bi00882a008 contributor: fullname: Stark GR – volume: 77 start-page: 259 year: 2003 ident: CIT0033 publication-title: Exp Eye Res doi: 10.1016/S0014-4835(03)00159-3 contributor: fullname: Zhang Z – volume: 89 start-page: 10449 year: 1992 ident: CIT0027 publication-title: Proc Natl Acad Sci USA doi: 10.1073/pnas.89.21.10449 contributor: fullname: Horwitz J – volume: 748 start-page: 213 year: 1983 ident: CIT0031 publication-title: Biochim Biophys Acta doi: 10.1016/0167-4838(83)90297-2 contributor: fullname: Berbers GAM – volume: 203 start-page: 675 year: 1982 ident: CIT0015 publication-title: Biochem J doi: 10.1042/bj2030675 contributor: fullname: Mellado W – volume: 239 start-page: 1411 year: 1964 ident: CIT0014 publication-title: J Biol Chem doi: 10.1016/S0021-9258(18)91330-X contributor: fullname: Stark GR – volume: 1764 start-page: 1436 year: 2006 ident: CIT0029 publication-title: Biochim Biophys Acta doi: 10.1016/j.bbapap.2006.08.001 contributor: fullname: Harding JJ – volume: 84 start-page: 122 year: 1987 ident: CIT0032 publication-title: Proc Natl Acad Sci USA doi: 10.1073/pnas.84.1.122 contributor: fullname: Clark JI – ident: CIT0005 – volume: 210 start-page: 795 year: 1983 ident: CIT0016 publication-title: Biochem J doi: 10.1042/bj2100795 contributor: fullname: Hasilik A – volume: 251 start-page: 5663 year: 1976 ident: CIT0025 publication-title: Biol Chem doi: 10.1016/S0021-9258(17)33109-5 contributor: fullname: Slebe JC – volume: 86 start-page: 407 year: 2004 ident: CIT0004 publication-title: Prog Biophys Mol Biol doi: 10.1016/j.pbiomolbio.2003.11.012 contributor: fullname: Bloemendal H – volume: 1 start-page: 465 year: 2002 ident: CIT0002 publication-title: Ageing Res Rev doi: 10.1016/S1568-1637(02)00012-0 contributor: fullname: Harding JJ – volume: 4 start-page: 2597 year: 1985 ident: CIT0035 publication-title: EMBO J doi: 10.1002/j.1460-2075.1985.tb03976.x contributor: fullname: Quax-Jeuken Y – volume: 31 start-page: 567 year: 1980 ident: CIT0006 publication-title: Exp Eye Res doi: 10.1016/S0014-4835(80)80015-7 contributor: fullname: Harding JJ – volume: 78 start-page: 225 year: 1989 ident: CIT0036 publication-title: Gene doi: 10.1016/0378-1119(89)90225-4 contributor: fullname: van Rens GLM |
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Snippet | Purpose: Carbamylation, an important post-translational modification of proteins, inevitably causes conformational changes of lens proteins. It may increase... Carbamylation, an important post-translational modification of proteins, inevitably causes conformational changes of lens proteins. It may increase aggregation... PURPOSECarbamylation, an important post-translational modification of proteins, inevitably causes conformational changes of lens proteins. It may increase... |
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SubjectTerms | alpha-Crystallin A Chain - chemistry alpha-Crystallin A Chain - metabolism Animals beta-Crystallin B Chain - chemistry beta-Crystallin B Chain - metabolism carbamylation cataract Cattle cyanate Electrophoresis, Gel, Two-Dimensional gamma-Crystallins - chemistry gamma-Crystallins - metabolism In Vitro Techniques Lens, Crystalline - metabolism Mass Spectrometry matrix-assisted laser desorption ionization time-of-flight mass spectrometry Molecular Weight Protein Processing, Post-Translational Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization two-dimensional gel electrophoresis |
Title | Identification of the Primary Targets of Carbamylation in Bovine Lens Proteins by Mass Spectrometry |
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