PXD001593

PXD001593 is an original dataset announced via ProteomeXchange.

Title	Age-related cleavages of crystallins in human lens cortical fibre cells generate a plethora of low molecular weight peptides and cross-linked crystallin complexes
Description	A large variety of low molecular weight (LMW) peptides, derived from the breakdown of crystallins, have been reported in middle to old age human lenses. The proliferation of these LMW peptides coincides with the earliest stages of cataract formation, suggesting that the protein cleavages involved may contribute to the aggregation and insolubilisation of crystallins – these being hall marks of cataractogenesis. This study reports the identification of 238 endogenous LMW crystallin peptides from the cortical extracts of human lenses aged 16, 44, 75 and 83 years. Analysis of the peptide terminal amino acids showed that Lys and Arg were situated at the C-terminus with significantly higher frequency compared to other residues, suggesting that trypsin-like proteolysis may be active in the lens cortical fibre cells. Selected reaction monitoring (SRM) analysis of a prominent αA-crystallin peptide (αA57-65) showed that the concentration of this peptide in the human lens increased gradually to middle age, after which the rate of αA57-65 formation escalated significantly. Using 2-D gel electrophoresis and nanoLC-ESI-MS/MS, 13 protein complexes of 40-150 kDa consisting of multiple crystallin components were characterised from the water soluble cortical extracts of an adult human lens. The detection of these protein complexes suggested the possibility of crystallin cross-linking, with these complexes potentially acting to stabilise degraded crystallins by sequestration into water soluble complexes.
HostingRepository	PRIDE
AnnounceDate	2016-09-29
AnnouncementXML	Submission_2016-09-29_01:38:37.xml
DigitalObjectIdentifier	https://dx.doi.org/10.6019/PXD001593
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Supported dataset by repository
PrimarySubmitter	Xiaomin Song
SpeciesList	scientific name: Homo sapiens (Human); NCBI TaxID: 9606;
ModificationList	Oxidation
Instrument	QSTAR

Revision	Datetime	Status	ChangeLog Entry
0	2014-12-10 02:11:30	ID requested
⏵ 1	2016-09-29 01:38:38	announced

Su SP, Song X, Xavier D, Aquilina JA, Age-related cleavages of crystallins in human lens cortical fiber cells generate a plethora of endogenous peptides and high molecular weight complexes. Proteins, 83(10):1878-86(2015) [pubmed]

curator keyword: Biological, Biomedical

submitter keyword: Human lens, crystallin, endogeneuous peptidesLens aging

crystallin

cataract

mass spectrometry

endogenous peptides

2-D gel electrophoresis

nanoLC-ESI-MS/MS

trypsin-like cleavage

Xiaomin Song
contact affiliation	Australian Proteome Analysis Facility
contact email	xsong@proteome.org.au
lab head
Xiaomin Song
contact affiliation	APAF
contact email	xsong@proteome.org.au
dataset submitter

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PRIDE project URI

• PRIDE
  1. PXD001593
     1. Label: PRIDE project
     2. Name: Age-related cleavages of crystallins in human lens cortical fibre cells generate a plethora of low molecular weight peptides and cross-linked crystallin complexes