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Interleukin-1 modulates protein tyrosine phosphatase activity and permeability of brain endothelial cells.

Abstract：

:Interleukin-1 alpha (IL-1 alpha) and interleukin-6 (IL-6), both known to be able to open the blood-brain barrier (BBB), downregulated plasma membrane-associated tyrosine phosphatase activity in primary porcine brain endothelial cells (PBEC). In contrast, transforming growth factor beta (TGF-beta) upregulated PTP activity and tumor necrosis factor alpha (TNF-alpha) had no effect. Plasma membrane-associated PTP activity of PBEC was upregulated at contact inhibited growth arrest. Tightly confluent cells reduced 3H-inulin permeability by 34% compared with just confluent cells indicating the formation of barrier properties. The decrease in permeability temporally correlated with the elevated PTP activity of the cells at growth arrest and was reversed to control by IL-1 alpha. Vanadate, a broad-specificity PTP inhibitor, also enhanced 3H-inulin permeability. These data suggest that IL-1 alpha-induced endothelial permeability could be controlled through lowering PTP activity.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Gloor SM,Weber A,Adachi N,Frei K

doi

10.1006/bbrc.1997.7557

subject

Has Abstract

pub_date

1997-10-29 00:00:00

pages

804-9

issue

3

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(97)97557-4

journal_volume

239

pub_type

杂志文章

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