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The molecular background of the differential UV absorbance of the human lens in the 240-400 nm range.

Authors
  • Pajer, Viktor
  • Tiboldi, Akos
  • Bae, Narkhyun
  • Li, Kongzhao
  • Kang, Sung Ung
  • Hopp, Béla
  • Kolozsvári, Lajos
  • Lubec, Gert
  • Nógrádi, Antal
Type
Published Article
Journal
Photochemistry and Photobiology
Publisher
Wiley (Blackwell Publishing)
Publication Date
2013
Volume
89
Issue
4
Pages
856–863
Identifiers
DOI: 10.1111/php.12063
PMID: 23425351
Source
Medline
License
Unknown

Abstract

The ultraviolet (UV) absorption of various sections of the human lens was studied and compared with protein expression paralleling differential UV absorbance in anterior and posterior lenticular tissue. The UV absorbance of serial lens cryostat sections (60 μm) and that of lens capsules was determined using a Shimadzu scanning spectrophotometer, and the absorption coefficients were calculated. Two-dimensional gel electrophoresis was performed using two pooled lenticular protein extracts (anterior and posterior sections). Protein spots were quantified and significantly different spots were identified by mass spectrometry following in-gel digestion with trypsin and chymotrypsin. The UV-C and UV-B absorption of the human lens increased toward the posterior parts of the lens. The anterior and posterior lens capsules also effectively absorbed UV radiation. Levels of molecular chaperone proteins Beta-crystallin B2 (UniProtKB ID:P43320), A3 (UniProtKB ID:P05813) and of glyceraldehyde 3-phosphate dehydrogenase (UniProtKB ID:P04406) were significantly higher in the anterior part of the lens, whereas lens proteins Beta-crystallin B1 (UniProtKB ID:P53674) and Alpha-crystallin A chain (UniProtKB ID:P02489) were higher in the posterior sections. These results provide evidence that differential UV absorption in the anterior and posterior lens is accompanied by differential protein expression.

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