Expression of ERp29, an Endoplasmic Reticulum Secretion Factor in Basal-Cell Carcinoma

Abstract

The role of endoplasmic reticulum (ER)-stress proteins in the pathogenesis of neoplasia remains obscure. ERp29 encodes for an ER protein that is thought to facilitate the transport of secretory proteins in the early secretory pathway. ERp29 is expressed at varying levels in virtually every tissue tested, yet its precise role remains obscure. To test if ERp29 is associated with the pathogenesis of skin cancer, in the present study we have assessed the expression of ERp29 in basal-cell carcinoma of the skin. A bank of 104 basal skin carcinoma, including 50 nodular, 29 infiltrating, 15 superficial, 7 sclerosing, 2 fibroepithelial, and 1 pigmented cell carcinoma, were assessed by immunohistochemistry for ERp29 expression. Thirty-nine (37.5%) of the samples tested expressed ERp29 with the infiltrating carcinomas displaying more intense (++,+++) immunoreactivity (6/29, P < 0.05) and the superficial carcinomas exhibiting the less intense anti-ERp29 staining (1/15, P < 0.05). Collectively our results suggest that ERp29 is expressed in a subset of basal-cell carcinoma of the skin with the infiltrating carcinomas exhibiting the highest incidence of immunopositivity. The role of ERp29 in the pathogenesis of the disease and its potential diagnostic value should be explored in future investigations.

Identification of c-myc-dependent proteins in the medulloblastoma cell line D425Med

“…These findings are in disagreement with those by Bambang et al describing ERp29 as putative tumour suppressor in breast cancer due to its ability to reduce xenograft growth in nude mice, arrest cells at G0/G1 and inhibit cell proliferation (Bambang et al 2009). ERp29 has also been identified in other malignancies, such as in hepatocarcinoma cells (Feng et al 2007) or basal-cell carcinoma (Cheretis et al 2006). In this pathology, the degree of infiltration and malignancy was correlated to a higher ERp29 expression.…”

Integrated Endoplasmic Reticulum Stress Responses in Cancer

“…Other ER-resident proteins that participate to secretory protein folding also display an altered expression in various cancers. This is the case for the protein disulfide isomerase (PDI)-like protein ERp29 and for the ER oxidase Ero1 in basal skin carcinomas and breast carcinomas, respectively (4,5). The oligosaccharyltransferase complex component defender against death-1 and the lectin-like chaperone calreticulin (6) are overexpressed in HCC.…”

Triplex Profiling of Functionally Distinct Chaperones (ERp29/PDI/BiP) Reveals Marked Heterogeneity of the Endoplasmic Reticulum Proteome in Cancer

“…12 Their report did not include ERp29 however. As it still remains unclear whether ERp29 follows this pattern, 14,15,17,[29][30][31] we profiled ERp29/PDI/ BiP in spontaneous carcinomas using the same sampling approach. 12 Mammary and salivary carcinomas were obtained from rat, together with corresponding normal tissues.…”