The transcription factor C/EBP α controls the role of cystatin F during the differentiation of monocytes to macrophages

European Journal of Cell Biology
Esmeralda DautovićJanko Kos

Abstract

Cystatin F is an inhibitor of cysteine peptidases expressed solely in immune cells. It is the only type II cystatin able to enter endosomal/lysosomal vesicles and to regulate directly the activity of intracellular cysteine cathepsins. Its expression in promonocytic U937 and promyeloblastic HL-60 cells is highly upregulated but, after differentiation with phorbol 12-myristate 13-acetate - PMA, its levels drop significantly. In contrast, the activities of intracellular cysteine cathepsins C, L and S are higher in differentiated cells than in non-differentiated ones due, presumably, to the lower inhibitory capacity of cystatin F. Using immunofluorescence confocal microscopy, proximity ligation assay and co-immunoprecipitation, cathepsins C, L and S were confirmed to be the main interacting partners of cystatin F in U937 and HL-60 cells. The promoter region of the cystatin F gene, CST7, contains a unique binding site for transcription factor C/EBP α, one of the main myeloid differentiation instructors. Using the chromatin immunoprecipitation assay, C/EBP α was shown to bind to CST7 gene in U937 cells. Following cell differentiation with PMA, the binding of C/EBP α was decreased significantly. The protein level of C/EBP α was also s...Continue Reading

Citations

Mar 7, 2019·Radiology and Oncology·Mateja PrunkJanko Kos
Sep 27, 2019·Frontiers in Immunology·Tanja JakošJanko Kos
May 8, 2021·BioMed Research International·Zhaojun LiuErzhen Chen
Jul 1, 2021·Cellular Oncology (Dordrecht)·Emanuela SenjorJanko Kos
Aug 28, 2021·International Journal of Molecular Sciences·Milica Perišić NanutJanko Kos

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