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Urokinase binding sites on human foreskin cells. Evidence for occupancy with endogenous urokinase.

Abstract：

:In cultures of human foreskin fibroblasts most of the cell surface binding sites for 2-chain urokinase are masked and can be exposed by 10 min. incubation on ice at pH 2.5 (A. Bajpai and J.B. Baker (1985), Biochem. Biophys. Res. Commun.133, 475-482). Here we show that incubation on ice at pH 2.5 also releases from the cell surface a plasminogen activator that is similar to 2-chain urokinase in terms of its electrophoretic mobility, chromatographic behavior on concanavalin A-Sepharose or p-amino-benzamidine-Sepharose, and sensitivity to anti-urokinase antibody. Two observations suggest that the masked binding sites are sites occupied by this cell surface urokinase. First, glucocorticoid-treated cells, which lack cell surface urokinase, have a large number of urokinase binding sites but none that are masked. Second, the extraction of surface urokinase and the exposure of urokinase binding sites exhibit similar pH dependence. Both are complete at about pH 4.0.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Bajpai A,Baker JB

doi

10.1016/0006-291x(85)91234-3

subject

Has Abstract

pub_date

1985-12-31 00:00:00

pages

994-1000

issue

3

eissn

0006-291X

issn

1090-2104

pii

0006-291X(85)91234-3

journal_volume

133

pub_type

杂志文章

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