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Mitogen-activated protein kinase activates human placental lactogen-B enhancer by an NF-IL6-dependent pathway.

Abstract：

:Computer analysis of the human placental lactogen-B (hPL-B) enhancer reveals two putative binding sites for the transcription factor NF-IL6, but the role of NF-IL6 in the regulation of the enhancer is unknown. Using gel mobility shift and supershift assays, we demonstrated that NF-IL6 binds to both enhancer sites. Transient transfection studies indicated that the transcription factor NF-IL6 stimulates hPL-B enhancer activity by 4.4-fold in primary cultures of human trophoblast cells and by 32.0- and 8.4-fold in JAR and BeWo choriocarcinoma cells, respectively. Overexpression of MEK (mitogen-activated protein [MAP] kinase kinase), which is known to stimulate phosphorylation of NF-IL6, induced a 3.6-fold increase in hPL-B enhancer activity. The induction by MEK was completely inhibited by an expression plasmid for a dominant/negative mutant of NF-IL6 or by mutation of the NF-IL6 binding sites on the enhancer. PD98059, an inhibitor of MEK, inhibited hPL release from cultured trophoblast cells by about 50%. Taken together, these results indicate that MAP kinase stimulates the hPL-B enhancer by an NF-IL-6-dependent pathway.

journal_name

Endocrine

journal_title

Endocrine

authors

Brar AK,Richards RG,Cheng YH,Richardson B,Kanda Y,Handwerger S

doi

10.1385/ENDO:12:1:47

subject

Has Abstract

pub_date

2000-02-01 00:00:00

pages

47-52

issue

1

eissn

1355-008X

issn

1559-0100

pii

ENDO:12:1:47

journal_volume

12

pub_type

杂志文章

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