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Identification of crystallin family proteins in vitreous body in rat endotoxin‐induced uveitis: Involvement of crystallin truncation in uveitis pathogenesis
Author(s) -
Bahk SongChul,
Lee SookHee,
Jang JungUn,
Choi ChangUk,
Lee BokSoo,
Chae SooCheon,
Song HyeJin,
Park ZeeYong,
Yang YunSik,
Chung HunTaeg
Publication year - 2006
Publication title -
proteomics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.26
H-Index - 167
eISSN - 1615-9861
pISSN - 1615-9853
DOI - 10.1002/pmic.200500779
Subject(s) - crystallin , uveitis , pathogenesis , inflammation , chemistry , biology , pathology , medicine , immunology , biochemistry
Abstract Endotoxin‐induced uveitis (EIU) is an animal model of acute ocular inflammation. To characterize the mechanism of EIU, we analyzed the infiltration of proteins in the vitreous bodies of rats with EIU and normal rats using 2‐DE and micro LC/LC‐MS/MS. Twenty spots were identified in vitreous bodies of rats. Eighteen of these spots were members of the crystallin family. The truncated form of beta A4‐ and beta B2‐crystallin were predominant in normal vitreous bodies, but there were intact form of crystallins in lipopolysaccharide‐injected rats with EIU. These results suggest that crystallin family proteins are the major group of proteins involved in uveitic vitreous and that C‐terminal truncation of beta‐crystallins may play a role in EIU‐related disease progression.