Dicer up-regulation by inhibition of specific proteolysis in differentiating monocytic cells.


Journal

Proceedings of the National Academy of Sciences of the United States of America
ISSN: 1091-6490
Titre abrégé: Proc Natl Acad Sci U S A
Pays: United States
ID NLM: 7505876

Informations de publication

Date de publication:
14 04 2020
Historique:
pubmed: 30 3 2020
medline: 22 7 2020
entrez: 30 3 2020
Statut: ppublish

Résumé

Dicer is a ribonuclease III enzyme in biosynthesis of micro-RNAs (miRNAs). Here we describe a regulation of Dicer expression in monocytic cells, based on proteolysis. In undifferentiated Mono Mac 6 (MM6) cells, full-length Dicer was undetectable; only an ∼50-kDa fragment appeared in Western blots. However, when MM6 cells were treated with zymosan or LPS during differentiation with TGF-β and 1,25diOHvitD3, full-length Dicer became abundant together with varying amounts of ∼170- and ∼50-kDa Dicer fragments. Mass spectrometry identified the Dicer fragments and showed cleavage about 450 residues upstream from the C terminus. Also, PGE

Identifiants

pubmed: 32220961
pii: 1916249117
doi: 10.1073/pnas.1916249117
pmc: PMC7165444
doi:

Substances chimiques

Lipopolysaccharides 0
MicroRNAs 0
Receptors, Prostaglandin E, EP2 Subtype 0
Receptors, Prostaglandin E, EP4 Subtype 0
Zymosan 9010-72-4
DICER1 protein, human EC 3.1.26.3
Ribonuclease III EC 3.1.26.3
DEAD-box RNA Helicases EC 3.6.4.13
PTGES protein, human EC 5.3.99.3
Prostaglandin-E Synthases EC 5.3.99.3
Dinoprostone K7Q1JQR04M

Types de publication

Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

8573-8583

Informations de copyright

Copyright © 2020 the Author(s). Published by PNAS.

Déclaration de conflit d'intérêts

The authors declare no competing interest.

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Auteurs

Devaraj Basavarajappa (D)

Division of Physiological Chemistry II, Department of Medical Biochemistry and Biophysics, Karolinska Institutet, S-17177 Stockholm, Sweden.

Stella Uebbing (S)

Division of Physiological Chemistry II, Department of Medical Biochemistry and Biophysics, Karolinska Institutet, S-17177 Stockholm, Sweden.
Department of Biology, Technical University, 64287 Darmstadt, Germany.
Institute of Pharmaceutical Chemistry, Goethe University, 60438 Frankfurt am Main, Germany.

Marius Kreiss (M)

Institute of Pharmaceutical Chemistry, Goethe University, 60438 Frankfurt am Main, Germany.

Ana Lukic (A)

Division of Physiological Chemistry II, Department of Medical Biochemistry and Biophysics, Karolinska Institutet, S-17177 Stockholm, Sweden.

Beatrix Suess (B)

Department of Biology, Technical University, 64287 Darmstadt, Germany.

Dieter Steinhilber (D)

Institute of Pharmaceutical Chemistry, Goethe University, 60438 Frankfurt am Main, Germany.

Bengt Samuelsson (B)

Division of Physiological Chemistry II, Department of Medical Biochemistry and Biophysics, Karolinska Institutet, S-17177 Stockholm, Sweden; bengt.samuelsson@ki.se olof.radmark@ki.se.

Olof Rådmark (O)

Division of Physiological Chemistry II, Department of Medical Biochemistry and Biophysics, Karolinska Institutet, S-17177 Stockholm, Sweden; bengt.samuelsson@ki.se olof.radmark@ki.se.

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Classifications MeSH