Sp1 mediates phorbol ester (PMA)-induced expression of membrane-bound guanylyl cyclase GC-A in human monocytic THP-1 cells

• Authors: Małgorzata Mitkiewicz , Bernadeta Bac , Marianna Kuropatwa , Ewa Kurowska , Janusz Matuszyk , Jakub Siednienko
• Languages of publication: EN

Abstracts

EN

Cyclic guanosine monophosphate (cGMP) is synthesized by two types of enzymes: particulate (membrane-bound) guanylyl cyclases (pGCs) and soluble (cytosolic) guanylyl cyclases (sGCs). sGCs are primarily activated by binding of nitric oxide to their prosthetic heme group while pGCs are activated by binding of peptide ligands to their extracellular domains. One of them, pGC type A (GC-A) is activated by atrial and brain natriuretic peptides (ANP and BNP, respectively). Human monocytes isolated from peripheral blood mononuclear cells have been found to display sGC expression without concomitant expression of GC-A. However, GC-A activity appears in monocytes under certain conditions but a molecular mechanism of GC-A expression is still poorly understood. In this report we show that phorbol ester (PMA) induces transcription of a gene encoding GC-A in human monocytic THP-1 cells. Moreover, we find that PMA-treated THP-1 cells raise cGMP content following treatment with ANP. Studies using pharmacological inhibitors of protein kinases suggest involvement of protein kinase C (PKC), mitogen extracellular kinases (MEK1/2), and extracellular signal-regulated kinases (ERK1/2) in PMA-induced expression of the GC-A encoding gene in THP-1 cells. Finally, we show that PMA stimulates binding of Sp1 transcription factor to GC-rich DNA sequences and mithramycin A (a selective Sp1 inhibitor) inhibits expression of the GC-A mRNA in PMA-treated THP-1 cells. Taken together, our findings suggest that the PMA-stimulated PKC and MEK/ERK signaling pathways induce Sp1-mediated transcription of the GC-A encoding gene in human monocytic THP-1 cells.

Keywords

EN

membrane-bound guanylyl cyclase type A; phorbol 12-myristate 13-acetate; human monocytic cell line THP-1; protein kinases; Sp1 transcription factor

• Publisher: Polish Biochemical Society
• Journal: Acta Biochimica Polonica
• Year: 2018
• Volume: 65
• Issue: 3
• Pages: 409-414

Dates

published

2018

received

2017-10-18

revised

2018-06-09

accepted

2018-06-18

(unknown)

2018-06-30

Contributors

author

Małgorzata Mitkiewicz

• Laboratory of Signal Transduction Molecules, Ludwik Hirszfeld Institute of Immunology and Experimental Therapy, Polish Academy of Sciences, Wrocław, Poland

author

Bernadeta Bac

• Department of Chemistry, Wrocław University of Science and Technology, Wrocław, Poland

author

Marianna Kuropatwa

• Laboratory of Signal Transduction Molecules, Ludwik Hirszfeld Institute of Immunology and Experimental Therapy, Polish Academy of Sciences, Wrocław, Poland

author

Ewa Kurowska

• Laboratory of Signal Transduction Molecules, Ludwik Hirszfeld Institute of Immunology and Experimental Therapy, Polish Academy of Sciences, Wrocław, Poland

author

Janusz Matuszyk

• Laboratory of Signal Transduction Molecules, Ludwik Hirszfeld Institute of Immunology and Experimental Therapy, Polish Academy of Sciences, Wrocław, Poland

author

Jakub Siednienko

• Laboratory of Signal Transduction Molecules, Ludwik Hirszfeld Institute of Immunology and Experimental Therapy, Polish Academy of Sciences, Wrocław, Poland
• Nanobioengineering Laboratory, Wrocław Research Centre EIT+, Wrocław, Poland

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Identifiers

DOI

10.18388/abp.2017_2341