American Association for Cancer Research
00085472can142718-sup-137887_1_supp_0_nkn7yj.doc (6.75 MB)

Supplementary Figures 1-6 from Aberrant Expression of proPTPRN2 in Cancer Cells Confers Resistance to Apoptosis

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journal contribution
posted on 2023-03-30, 23:25 authored by Alexey V. Sorokin, Binoj C. Nair, Yongkun Wei, Kathryn E. Aziz, Valentina Evdokimova, Mien-Chie Hung, Junjie Chen

Supplementary Figures 1-6 Supplementary Figure 1. PTPRN2 expression in normal and cancer tissues. Supplementary Figure 2. Validation of PTPRN2 antibodies for immunohistochemistry (IHC) and Western blot (WB) analysis. Supplementary Figure 3. MCF10A cells expressing proPTPRN2 forms larger acinar structures in Matrigel. Supplementary Figure 4. PTPRN2 is involved in IϰB/NF-ϰB and c-Jun N-terminal kinase (JNK)/AP-1 signaling pathways. Supplementary Figure 5. PTPRN2 knockdown induces apoptosis in MDA-MB-468 cells. Supplementary Figure 6. Overexpression of proPTPRN2 but not mature PTPRN2 suppresses TRAF2 phosphorylation.



The protein tyrosine phosphatase receptor PTPRN2 is expressed predominantly in endocrine and neuronal cells, where it functions in exocytosis. We found that its immature isoform proPTPRN2 is overexpressed in various cancers, including breast cancer. High proPTPRN2 expression was associated strongly with lymph node–positive breast cancer and poor clinical outcome. Loss of proPTPRN2 in breast cancer cells promoted apoptosis and blocked tumor formation in mice, whereas enforced expression of proPTPRN2 in nontransformed human mammary epithelial cells exerted a converse effect. Mechanistic investigations suggested that ProPTPRN2 elicited these effects through direct interaction with TRAF2, a hub scaffold protein for multiple kinase cascades, including ones that activate NF-κB. Overall, our results suggest PTPRN2 as a novel candidate biomarker and therapeutic target in breast cancer. Cancer Res; 75(9); 1846–58. ©2015 AACR.

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