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. 2017 Feb 11;8(4):570-577.
doi: 10.7150/jca.17414. eCollection 2017.

Proteomic Characterization Reveals a Molecular Portrait of Nasopharyngeal Carcinoma Differentiation

Zhefeng Xiao  1 , Maoyu Li  1 , Guoqing Li  1 , Ying Fu  1 , Fang Peng  1 , Yongheng Chen  2 , Zhuchu Chen  2
Affiliations

Proteomic Characterization Reveals a Molecular Portrait of Nasopharyngeal Carcinoma Differentiation

Zhefeng Xiao et al. J Cancer. .

Abstract

Nasopharyngeal carcinoma (NPC) is categorized into three different differentiated subtypes by World Health Organization (WHO). Based on an earlier comparative proteomic database of the three histological subtypes, the study was to deepen our understanding of molecular mechanisms associated with NPC differentiation through bio-information mining. Among the three subtypes were 194 differentially expressed proteins (DEPs) of 725 identified proteins. Two DEPs, heat shock protein family B (small) member 1 (HSPB1) and keratin 5 (KRT5), were validated in a series of NPC tissue samples by using immunohistochemistry. Quantified protein families including keratins, S100 proteins (S100s) and heat shock proteins exhibited characteristic expression alterations. Comparisons of predicted bio-function activation states among different subtypes, including formation of cellular protrusion, metastasis, cell death, and viral infections, were conducted. Canonical pathway analysis inferred that Rho GTPases related signaling pathways regulated the motility and invasion of dedifferentiated NPC. In conclusion, the study explored the proteomic characteristics of NPC differentiation, which could deepen our knowledge of NPC tumorigenesis and allow the development of novel targets of therapeutic and prognostic value in NPC.

Keywords: Ingenuity pathway analysis.; formalin-fixed paraffin-embedded; nasopharyngeal carcinoma; proteomics.

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Conflict of interest statement

Competing Interests: The authors have declared that no competing interest exists.

Figures

Figure 1
Figure 1
Expression alterations of the representative protein families among the three subtypes of NPC. A. heat shock proteins; B. keratins; C. S100As; D. EEFs and EIFs.
Figure 2
Figure 2
Representative immunohistochemistry results of HSPB1 and KRT5 in clinical NPC samples. Immunohistochemistry of HSPB1 in WHO type I (A), WHO type II (B), and WHO type III (C); immunohistochemistry of KRT5 in WHO type I (D), WHO type II (E), and WHO type III (F); bar size=100 μm.
Figure 3
Figure 3
The predicted activation of formation of cellular protrusions between type I and III NPCs is explained by the contribution of the quantified proteins.
See this image and copyright information in PMC

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