Proteomics and phosphoproteomics analysis of human lens fiber cell membranes.

@article{Wang2013ProteomicsAP,
  title={Proteomics and phosphoproteomics analysis of human lens fiber cell membranes.},
  author={Zhen Wang and Jun Han and Larry David and Kevin L. Schey},
  journal={Investigative ophthalmology \& visual science},
  year={2013},
  volume={54 2},
  pages={
          1135-43
        }
}
PURPOSE The human lens fiber cell insoluble membrane fraction contains important membrane proteins, cytoskeletal proteins, and cytosolic proteins that are strongly associated with the membrane. The purpose of this study was to characterize the lens fiber cell membrane proteome and phosphoproteome from human lenses. METHODS HPLC-mass spectrometry-based multidimensional protein identification technology (MudPIT), without or with phosphopeptide enrichment, was applied to study the proteome and… 
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References

SHOWING 1-10 OF 58 REFERENCES
The membrane proteome of the mouse lens fiber cell
Purpose Fiber cells of the ocular lens are bounded by a highly specialized plasma membrane. Despite the pivotal role that membrane proteins play in the physiology and pathophysiology of the lens, our…
Phosphoproteomics characterization of novel phosphorylated sites of lens proteins from normal and cataractous human eye lenses
TLDR
The quantitative analysis of the in vivo phosphoproteomics profiles of human normal and cataractous lenses revealed 20 newly discovered novel phosphorylation sites on lens proteins that may provide insights into phosphorylated human eye diseases, which warrant further investigation in the future.
Identification of in vivo phosphorylation sites of lens proteins from porcine eye lenses by a gel-free phosphoproteomics approach
TLDR
This study identified in vivo phosphorylation sites of various lens proteins including especially the major structural proteins of the crystallin family from porcine eye lenses by means of two-dimensional gel electrophoresis or immobilized metal affinity chromatography followed by liquid chromatography coupled with tandem mass spectrometry.
Tight binding of proteins to membranes from older human cells
TLDR
It is evident that protein–membrane interactions change significantly with age, and selected proteins that were formerly cytosolic become increasingly tightly bound to cell membranes with age and are not removed even by treatment with 7 M urea.
Analysis of Protein–Protein Interactions and Proteomic Profiles of Normal Human Lenses
TLDR
Key proteins of normal human lenses were studied by constructing a network chart of the identified lens PPIs and the results suggest that linear ion trap MS/MS is an effective tool for detecting low-abundance proteins of human lenses.
Posttranslational modifications of the bovine lens beaded filament proteins filensin and CP49.
TLDR
This study identified sites of phosphorylation and truncation in Filensin and CP49 and revealed two unusual PTMs: postproteolytic N-acetylation and N-myristoylation of filensin.
Novel fatty acid acylation of lens integral membrane protein aquaporin-0.
TLDR
In the present study, direct tissue profiling mass spectrometry of bovine and human lens sections revealed an abundant signal tentatively assigned as a lipid-modified form of aquaporin-0, suggesting a role in membrane domain targeting.
Shotgun identification of protein modifications from protein complexes and lens tissue
  • M. MacCoss, W. McDonald, J. Yates
  • Biology, Chemistry
    Proceedings of the National Academy of Sciences of the United States of America
  • 2002
TLDR
This work describes a process for the analysis of posttranslational modifications that is simple, robust, general, and can be applied to complicated protein mixtures and lens tissue from a patient with congenital cataracts.
Proteomic analysis of water insoluble proteins from normal and cataractous human lenses.
TLDR
The compositions of WI-US and WI-UI proteins, isolated from one normal and one cataractous lens, were different, which suggested a major role of alphaB-crystallin in the insolubilization process of crystallins.
Proteomic analysis of human age-related nuclear cataracts and normal lens nuclei.
TLDR
The results show that crystallins, especially αA-crystallin, aggregate irreversibly during ARNC development and some enzymes may be involved in and/or accelerate this process.
...
...