Proteolytic Activation of Corneal Matrix Metalloproteinase byPseudomonas AeruginosaElastase
作者:
MatsumotoKoki,
ShamsNaveed B.K.,
HanninenLaila A.,
KenyonKenneth R.,
期刊:
Current Eye Research
(Taylor Available online 1992)
卷期:
Volume 11,
issue 11
页码: 1105-1109
ISSN:0271-3683
年代: 1992
DOI:10.3109/02713689209015082
出版商: Taylor&Francis
数据来源: Taylor
摘要:
PurifiedPseudomonas aeruginosaelastase cleaved a 65 kDa gelatinase [inactive proenzyme form of matrix metalloproteinase (MMP-2)] from human corneal fibroblasts into a biologically active fragment with an approximate molecular mass of 58 kDa. However, purified pseudomonal alkaline protease did not cleave MMP-2 appreciably. Since activated MMP-2 is known to degrade native type IV, V and VII collagens, all components of the corneal basement membrane or stroma, our results suggest a new role for pseudomonal elastase in the pathogenesis of corneal infection, inflammation and ulceration.
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