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PTPIP51—A New RelA-tionship with the NFκB Signaling Pathway.

Brobeil A, Kämmerer F, Tag C, Steger K, Gattenlöhner S, Wimmer M - Biomolecules (2015)

Bottom Line: This hints to the fact that in un-stimulated conditions PTPIP51 forms a complex with RelA and IκBα.Here, PTPIP51 and Raf-1 interactions were slightly repressed.The newly established relationship of PTPIP51 and the NFκB signaling pathway provides the basis for a possible therapeutic impact.

View Article: PubMed Central - PubMed

Affiliation: Institute of Anatomy and Cell Biology, Justus-Liebig-University, Gießen 35392, Germany. alexander.brobeil@patho.med.uni-giessen.de.

ABSTRACT
The present study shows a new connection of protein tyrosine phosphatase interacting protein 51 (PTPIP51) to the nuclear factor κB (NFκB) signalling pathway. PTPIP51 mRNA and protein expression is regulated by RelA. If bound to the PTPIP51 promoter, RelA repress the mRNA and protein expression of PTPIP51. The parallel treatment with pyrrolidine dithiocarbamate (PDTC) reversed the suppression of PTPIP51 protein expression induced by TNFα. Using the intensity correlation analysis PTPIP51 verified a co-localization with RelA, which is also regulated by TNFα administration. Moreover, the direct interaction of PTPIP51 and RelA was established using the DuoLink proximity ligation assay. IκBα, the known inhibitor of RelA, also interacted with PTPIP51. This hints to the fact that in un-stimulated conditions PTPIP51 forms a complex with RelA and IκBα. The PTPIP51/RelA/IκBα complex is modulated by TNFα. Interestingly, the impact on the mitogen activated protein kinase pathway was negligible except in highest TNFα concentration. Here, PTPIP51 and Raf-1 interactions were slightly repressed. The newly established relationship of PTPIP51 and the NFκB signaling pathway provides the basis for a possible therapeutic impact.

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Immunocytochemical staining of PTPIP51 and RelA in human keratinocytes. Upper panel: untreated controls: PTPIP5, RelA, overlay. Second panel: 50 ng/mL TNFα treated cells: PTPIP51, RelA, overlay. Third panel: 200 ng/mL TNFα treated cells: PTPIP51, RelA, overlay. Fourth panel: 400 ng/mL TNFα treated cells: PTPIP51, RelA, overlay. Co-localization is indicated by organge colour.
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biomolecules-05-00485-f003: Immunocytochemical staining of PTPIP51 and RelA in human keratinocytes. Upper panel: untreated controls: PTPIP5, RelA, overlay. Second panel: 50 ng/mL TNFα treated cells: PTPIP51, RelA, overlay. Third panel: 200 ng/mL TNFα treated cells: PTPIP51, RelA, overlay. Fourth panel: 400 ng/mL TNFα treated cells: PTPIP51, RelA, overlay. Co-localization is indicated by organge colour.

Mentions: Confocal laser scanning microscopy experiments displayed a co-localization of PTPIP51 with RelA (Figure 3 first row). The co-localization is indicated by the orange color in the overlayed PTPIP51 and RelA confocal images (Figure 3 right row Overlay).


PTPIP51—A New RelA-tionship with the NFκB Signaling Pathway.

Brobeil A, Kämmerer F, Tag C, Steger K, Gattenlöhner S, Wimmer M - Biomolecules (2015)

Immunocytochemical staining of PTPIP51 and RelA in human keratinocytes. Upper panel: untreated controls: PTPIP5, RelA, overlay. Second panel: 50 ng/mL TNFα treated cells: PTPIP51, RelA, overlay. Third panel: 200 ng/mL TNFα treated cells: PTPIP51, RelA, overlay. Fourth panel: 400 ng/mL TNFα treated cells: PTPIP51, RelA, overlay. Co-localization is indicated by organge colour.
© Copyright Policy
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC4496682&req=5

biomolecules-05-00485-f003: Immunocytochemical staining of PTPIP51 and RelA in human keratinocytes. Upper panel: untreated controls: PTPIP5, RelA, overlay. Second panel: 50 ng/mL TNFα treated cells: PTPIP51, RelA, overlay. Third panel: 200 ng/mL TNFα treated cells: PTPIP51, RelA, overlay. Fourth panel: 400 ng/mL TNFα treated cells: PTPIP51, RelA, overlay. Co-localization is indicated by organge colour.
Mentions: Confocal laser scanning microscopy experiments displayed a co-localization of PTPIP51 with RelA (Figure 3 first row). The co-localization is indicated by the orange color in the overlayed PTPIP51 and RelA confocal images (Figure 3 right row Overlay).

Bottom Line: This hints to the fact that in un-stimulated conditions PTPIP51 forms a complex with RelA and IκBα.Here, PTPIP51 and Raf-1 interactions were slightly repressed.The newly established relationship of PTPIP51 and the NFκB signaling pathway provides the basis for a possible therapeutic impact.

View Article: PubMed Central - PubMed

Affiliation: Institute of Anatomy and Cell Biology, Justus-Liebig-University, Gießen 35392, Germany. alexander.brobeil@patho.med.uni-giessen.de.

ABSTRACT
The present study shows a new connection of protein tyrosine phosphatase interacting protein 51 (PTPIP51) to the nuclear factor κB (NFκB) signalling pathway. PTPIP51 mRNA and protein expression is regulated by RelA. If bound to the PTPIP51 promoter, RelA repress the mRNA and protein expression of PTPIP51. The parallel treatment with pyrrolidine dithiocarbamate (PDTC) reversed the suppression of PTPIP51 protein expression induced by TNFα. Using the intensity correlation analysis PTPIP51 verified a co-localization with RelA, which is also regulated by TNFα administration. Moreover, the direct interaction of PTPIP51 and RelA was established using the DuoLink proximity ligation assay. IκBα, the known inhibitor of RelA, also interacted with PTPIP51. This hints to the fact that in un-stimulated conditions PTPIP51 forms a complex with RelA and IκBα. The PTPIP51/RelA/IκBα complex is modulated by TNFα. Interestingly, the impact on the mitogen activated protein kinase pathway was negligible except in highest TNFα concentration. Here, PTPIP51 and Raf-1 interactions were slightly repressed. The newly established relationship of PTPIP51 and the NFκB signaling pathway provides the basis for a possible therapeutic impact.

Show MeSH
Related in: MedlinePlus