Premium
Proteome analysis of human foetal, aged and advanced nuclear cataract lenses
Author(s) -
Hains Peter G.,
Truscott Roger J. W.
Publication year - 2008
Publication title -
proteomics – clinical applications
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.948
H-Index - 54
eISSN - 1862-8354
pISSN - 1862-8346
DOI - 10.1002/prca.200800085
Subject(s) - proteome , crystallin , human proteins , biology , complementary dna , cdna library , lens (geology) , acetylation , methionine , human proteome project , proteomics , computational biology , microbiology and biotechnology , biochemistry , amino acid , gene , paleontology
The most complete proteome of human lenses has been compiled using 2‐D LC‐MS/MS analysis of foetal, aged normal and advanced nuclear cataract lenses. A total of 231 proteins were identified across all lens groups, including 112 proteins that have not been reported previously. Proteins were grouped according to their PANTHER molecular function classification in order to facilitate comparisons. Previously unreported N‐terminal acetylation was detected in a number of proteins, with the majority being associated with the prior removal of a methionine residue. This pattern of proteolysis may indicate that methionine aminopeptidase activity is present in human lenses. Acetylation is likely to aid in the stability of proteins that are present in the lens for many decades. Protein sequences were also used to interrogate the three human lens cDNA libraries publicly available. Surprisingly, 84 proteins we identified were not present in the cDNA libraries.