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Inhibition of wortmannin activities by amino compounds.

Abstract：

:Wortmannin caused normal and strong inhibition on catecholamine secretion from bovine adrenal chromaffin cells and in vitro phosphoinositide 3-kinase activity in NaCl-, Na isethionate-, choline Cl-, Na acetate-, and N-acetyl glycine-based media. However, brief preincubation of wortmannin with the media containing amino compounds such as glutamate, aspartate, lysine, and glycine resulted in the prevention of the inhibitory effects of wortmannin on the above responses as two indexes of wortmannin activities. On the other hand, the amino compounds also caused several rapid changes in wortmannin medium; the changes in absorption spectrum of the medium; and the changes in the retention time of the peak on the HPLC chromatogram using a reverse-phase C-18 column and in the pattern of absorption spectrum of the peak. These changes were not observed in the cases of NaCl, Na isethionate, choline Cl, Na acetate or N-acetyl glycine. Another amino compound Tris, which was commonly used as a pH buffer, was unique in time course and induced the slow but parallel changes and reached maximal up to about 24h. These results taken together indicate that the amino compounds markedly inhibit the activities of wortmannin presumably through the binding of wortmannin to amino group.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Isosaki M

doi

10.1016/j.bbrc.2004.09.200

subject

Has Abstract

pub_date

2004-11-26 00:00:00

pages

1406-12

issue

4

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(04)02271-5

journal_volume

324

pub_type

杂志文章

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