Transcription of the human ferredoxin gene through a single promoter which contains the 3',5'-cyclic adenosine monophosphate-responsive sequence and Sp 1-binding site.

Chang, Chih-Hao; Huang, Cory; Guo, Ing-Cherng; Tsai, Huei Man; Wu, Du An; Chung, Bon Chu

doi:10.1210/mend.6.9.1331772

Cited by 9 publications

(3 citation statements)

References 2 publications

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“…[] +pKa the human ferredoxin 5"-flanking region, the same patterns of transcripts were detected as in Y1 cells [1]. The levels of these transcripts, however, were not stimulated by forskolin treatment ( fig.…”

Section: [] Controlsupporting

confidence: 57%

Sp1-like proteins function in the transcription of human ferredoxin genes

2000

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We characterized a regulatory element located in the -76 to -62 region of the human ferredoxin gene. This region bound to Sp1-like proteins with low affinity, as shown using electrophoretic mobility shift, competition, antibody binding, and Southwestern experiments. The similarity of the regulatory element to Sp1 extends beyond its DNA-binding domain, as cloned Sp1 functioned equally well when fused to a peptide that bound to an irrelevant site. The function of these Sp1-binding sites is mediated through the cAMP-dependent protein kinase (PKA) signaling pathway, because reporter genes downstream of the Sp1-binding sites were not activated in a PKA-deficient cell line. Transfection of the catalytic subunit of PKA restored activated transcription. Similar Sp1-binding sites identified in the CYP11A1 and CYP21 genes also controlled cAMP-dependent transcription of the reporter gene. Our finding of the function of Sp1-like proteins in steroidogenic gene transcription adds one more role Sp1 plays in controlling physiological events.

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Section: [] Controlsupporting

confidence: 57%

Sp1-like proteins function in the transcription of human ferredoxin genes

2000

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“…In Kin-8 cells, which do not have active PKA, steroidogenic gene expression was impaired [43]. When Kin-8 cells were transfected with the CAT reporter plasmids driven using different lengths of the human ferredoxin 5)-flanking region, the same patterns of transcripts were detected as in Y1 cells [1]. The levels of these transcripts, however, were not stimulated by forskolin treatment ( fig.…”

Section: Presence Of the Sp1-binding Site In Three Steroidogenic Genesmentioning

confidence: 98%

“…We have previously shown that the -76/-62 sequence of the human ferredoxin gene promoter activated transcription [1]. Proteins bound to this -76/-62 sequence were examined using electrophoretic mobility shift assay with Y1 nuclear extract ( fig.…”

Section: Sp1-like Proteins Bind To the -76/-62 Region Of The Human Fementioning

confidence: 99%

Sp1-Like Proteins Function in the Transcription of Human Ferredoxin Genes

Yeh¹,

Hsu²,

Chung³

2000

J Biomed Sci

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We characterized a regulatory element located in the –76 to –62 region of the human ferredoxin gene. This region bound to Sp1-like proteins with low affinity, as shown using electrophoretic mobility shift, competition, antibody binding, and Southwestern experiments. The similarity of the regulatory element to Sp1 extends beyond its DNA-binding domain, as cloned Sp1 functioned equally well when fused to a peptide that bound to an irrelevant site. The function of these Sp1-binding sites is mediated through the cAMP-dependent protein kinase (PKA) signaling pathway, because reporter genes downstream of the Sp1-binding sites were not activated in a PKA-deficient cell line. Transfection of the catalytic subunit of PKA restored activated transcription. Similar Sp1-binding sites identified in the CYP11A1 and CYP21 genes also controlled cAMP-dependent transcription of the reporter gene. Our finding of the function of Sp1-like proteins in steroidogenic gene transcription adds one more role Sp1 plays in controlling physiological events.

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Transcriptional regulation of multidrug resistance in breast cancer

Glazer

Rohlff

1994

Breast Cancer Res Tr

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The development of cross-resistance to many natural product anticancer drugs, termed multidrug resistance (MDR), is one of the major reasons why cancer chemotherapy ultimately fails. This type of MDR is often associated with over-expression of the MDR1 gene product, P-glycoprotein (Pgp), a multifunctional drug transporter. The expression of MDR in breast tumors is related to their origination from a tissue that constitutively expresses Pgp as well as to the development of resistance during successive courses of chemotherapy. Therefore, understanding the mechanisms that regulate the transcriptional activation of MDR1 may afford a means of reducing or eliminating MDR. We have found that MDR1 expression can be modulated by type I cAMP-dependent protein kinase (PKA), opening up the possibility of modulating MDR by selectively down-regulating the activity of PKA-dependent transcription factors which upregulate MDR1 expression. High levels of type I PKA occurs in primary breast carcinomas and patients exhibiting this phenotype show decreased survival. The selective type I cAMP-dependent protein kinase (PKA) inhibitors, 8-Cl-cAMP and Rp8-Cl-cAMP[S] may be particularly useful for downregulating PKA-dependent MDR-associated transcription factors, and we have found these compounds to downregulate transient expression of a reporter gene under the control of several MDR1 promoter elements. Thus, investigations of this nature should not only lead to a greater understanding of the mechanisms governing the expression of MDR, but also provide a focus for pharmacologic intervention by a new class of inhibitors.

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Transcription of the human ferredoxin gene through a single promoter which contains the 3',5'-cyclic adenosine monophosphate-responsive sequence and Sp 1-binding site.

Cited by 9 publications

References 2 publications

Sp1-like proteins function in the transcription of human ferredoxin genes

Sp1-like proteins function in the transcription of human ferredoxin genes

Sp1-Like Proteins Function in the Transcription of Human Ferredoxin Genes

Transcriptional regulation of multidrug resistance in breast cancer

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