Plasminogen activator inhibitor type 2 in human corneal epithelium

Darice L. Williams, Barbara Risse, Kim Sam, Darren Saunders, Stephen Orlin, Mark S. Baker, Pamela J. Jensen, Robert M. Lavker*

*Corresponding author for this work

Research output: Contribution to journalArticle

22 Citations (Scopus)

Abstract

Purpose. To examine normal human corneal epithelium in vivo and in vitro for expression and status of plasminogen activator inhibitor type 2 (PAI-2). Methods. Normal human corneas were prepared for frozen sections and for culture of corneal keratinocytes. PAI-2 was analyzed by immunohistochemistry and western blot analysis using antibodies that recognize all forms of PAI- 2. Results. In vivo and in vitro, PAI-2 was immunohistochemically localized to the superficial corneal keratinocytes. Immunostaining also revealed the presence of PAI-2 in its relaxed (i.e., cleaved) conformation. In vivo, the staining pattern of the relaxed form was identical with that of total PAI-2 but in vitro tile relaxed form was detected in a smaller subpopulation of superficial cells. In vitro, the staining pattern indicated a cytoplasmic localization for PAI-2. Western blot analysis revealed that most of the PAI- 2 was cell associated and functionally active. Conclusions. The present results are the first to show that PAI-2 is found in normal human corneal epithelium in vivo and in vitro, where it can be considered as a differentiation product. At least in vitro, all detectable PAI-2 is cell associated, with a cytoplasmic distribution. A subpopulation of keratinocytes also contains PAI-2 in its relaxed (i.e., cleaved) conformation. Cleavage by an as yet unidentified cytoplasmic proteinase may constitute a crucial aspect of the function of corneal epithelial PAI-2, which may be relevant to terminal differentiation and death of the corneal keratinocyte.

Original languageEnglish
Pages (from-to)1669-1675
Number of pages7
JournalInvestigative Ophthalmology and Visual Science
Volume40
Issue number8
Publication statusPublished - 1999
Externally publishedYes

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