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Phosphatidylinositol 3-kinase in HL-60 nuclei is bound to the nuclear matrix and increases during granulocytic differentiation.

Abstract：

:We have used HL-60 leukemia cells to investigate phosphatidylinositol 3-kinase (PI 3-K) during granulocytic differentiation at the nuclear level. Nuclei of HL-60 cells showed a constitutive presence of PI 3-K that increased when cells were treated with differentiating doses of ATRA. PI 3-K was also detected tightly bound to nuclear matrices of HL-60 cells, isolated by nuclease treatment and high salt extraction. Four days of ATRA treatment induced a striking increase of nuclear matrix bound PI 3-K. In situ morphological analysis by confocal microscopy showed the translocation of PI 3-K to the nucleus and to the subnuclear fractions. PI 3-K enzymatic activity was stimulated during the granulocytic differentiation process and parallelled the increase in content of nuclei and subnuclear fractions. PI 3-K activity was recovered in nuclei also without the addition of exogenous substrates, consistent with the presence of both substrates and enzyme in the nucleus. These results indicate that specific intracellular localization of PI 3-K determines the production of different phosphoinositides in the sites of the enzyme translocation, and suggest that 3-phosphoinositide metabolism may play a specific role in the nucleus, candidating PI 3-K as a key enzyme in promoting granulocytic differentiation of HL-60 cells.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Marchisio M,Bertagnolo V,Colamussi ML,Capitani S,Neri LM

doi

10.1006/bbrc.1998.9787

subject

Has Abstract

pub_date

1998-12-18 00:00:00

pages

346-51

issue

2

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(98)99787-X

journal_volume

253

pub_type

杂志文章

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