The increased expression of periostin during early stages of prostate cancer and advanced stages of cancer stroma

Tsunoda, Toshiyuki; Furusato, Bungo; Takashima, Yasuo; Ravulapalli, Suma; Dobi, Albert; Srivastava, Shiv; McLeod, David G.; Sesterhenn, Isabell A.; Ornstein, David K.; Shirasawa, Senji

doi:10.1002/pros.20988

Cited by 54 publications

(46 citation statements)

References 21 publications

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“…Increased expression of POSTN has been observed in various tumor types, including breast [44,48,[56][57][58], NSCLC [27,49,[59][60][61][62], colorectal [19,29,63], stomach cancers [64][65][66][67][68], pancreatic [32,69], prostate [70][71][72][73][74][75], ovarian cancer [76][77][78][79], and glioblastomas [80][81][82] (Table 1).…”

Section: Periostin Expression In Different Types Of Tumorsmentioning

confidence: 99%

The role of periostin in neoplastic processes

Ratajczak‐Wielgomas

Dzięgiel

2015

Folia Histochem Cytobiol.

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Periostin, also called osteoblast-specific factor 2 (OSF-2), is a multifunctional glycoprotein that belongs to the group of matricellular proteins. Due to its characteristic molecular structure containing integrin-binding domains, periostin is capable of binding to multiple integrin receptors (avb3, avb5, a6b4), thus affecting the regulation of the intracellular signaling pathways associated with protein kinases PI3K/AKT and focal adhesion kinase (FAK). This protein thus plays a role in the adhesion process, in the migration of many cells, and importantly, epithelial-mesenchymal transition of cancer cells. Periostin also participates in the processes of angiogenesis and lymphangiogenesis, metastases of cancer cells, and remodeling of the extracellular matrix. Increased expression of periostin has been observed in various tumor types, including breast, NSCLC, colorectal, pancreatic, prostate, and ovarian cancers, as well as tumors of the head and neck, and glioblastomas. Many groups have recently reported on periostin's key role in tumor progression, which suggests that periostin can be considered a potential therapeutic target.

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Section: Periostin Expression In Different Types Of Tumorsmentioning

confidence: 99%

The role of periostin in neoplastic processes

Ratajczak‐Wielgomas

Dzięgiel

2015

Folia Histochem Cytobiol.

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“…In addition, high reactive stromal grading is associated with lower biochemical recurrence-free survival rates than low reactive stromal grading [Ayala et al, 2003;Yanagisawa et al, 2007]. Recently, we have reported that periostin expression in CAFs was increased in the early stages of PCa tissues (Gleason score 6-7) and was significantly correlated with the degree of malignancy [Tsunoda et al, 2009]. Upregulation of collagen I, tenascin-C (TN-C), and transforming growth factor b (TGFb) have been observed in PCa specimens [Tuxhorn et al, 2002a].…”

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confidence: 94%

Heterogenous induction of carcinoma-associated fibroblast-like differentiation in normal human prostatic fibroblasts by co-culturing with prostate cancer cells

et al. 2011

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In the tumor microenvironment, carcinoma-associated fibroblasts (CAFs) are considered to play a critical role in the promotion of tumorigenesis. However, the mechanisms that generate CAFs are not well elucidated. To understand how CAFs are generated during primary cancer progression, we investigated the biochemical characteristics of normal human prostate stromal cells (PrSC) co-cultured with human prostate cancer (PCa) cells in vitro. In primary cultures of human PCa-derived stromal cells (PCaSC-8 and PCaSC-9), expression of TNC, ACTA2, EGF, FGF7, and IGF1 mRNA was generally higher than PrSC but gene expression patterns were not uniform between PCaSC-8 and PCaSC-9 cells. Transforming growth factor β (TGFβ) and vascular endothelial growth factor (VEGF) protein levels in both PCaSC-8 and PCaSC-9 cells were generally higher than PrSC but levels of both secreted proteins were not same. When PrSCs were co-cultured with androgen-sensitive LNCaP cells or its sublines, androgen-low-sensitive E9 cells and androgen-insensitive AIDL cells, mRNA expression of IGF1 was significantly increased in all combinations. In contrast, expression of COL1A1, TNC, and ACTA2 mRNA was significantly increased only in LNCaP + PrSC and E9 + PrSC co-cultures. Protein production of VEGF was significantly increased only in LNCaP + PrSC and E9 + PrSC co-cultures. Increase of TGFβ protein was observed only in E9 + PrSC co-cultures. These biochemical characteristics of PrSC were partially recapitulated in TGFβ-treated PrSC. We have demonstrated that normal fibroblasts co-cultured with cancer cells become activated and exhibit biochemical characteristics of CAFs in a heterogenous manner. Our results suggest that heterogenous induction of CAF-like differentiation might be strongly dependent on biochemical characteristics of adjacent cancer cells.

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“…The roles of periostin have also been reported in human bladder and prostate cancer tissues. Epithelial and stromal expression of periostin in normal prostate was detected in 74 and 13% of tissues examined, respectively (23). Periostin expression increased in the early stages of prostate cancer (Gleason score 6-7) but not in the advanced stages of prostate cancer.…”

Section: Discussionmentioning

confidence: 93%

Opposite regulation of epithelial-to-mesenchymal transition and cell invasiveness by periostin between prostate and bladder cancer cells

Inoue

2011

Int J Oncol

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Abstract. We previously showed that periostin expression is downregulated in human bladder cancer tissues and that ectopic expression of periostin suppresses the invasiveness of bladder cancer cells. However, in most other human cancers studied, the expression of periostin promotes cell invasiveness. In the present study, we investigated the regulation of the epithelialto-mesenchymal transition (EMT) and cell invasiveness by periostin in bladder and prostate cancer cell lines, and found opposite regulation of EMT and cell invasiveness by periostin. Periostin upregulated E-cadherin expression in bladder cancer cells but downregulated it in prostate cancer cells. Periostin suppressed cell invasiveness in bladder cancer cells but promoted it in prostate cancer cells. Snail, a negative regulator of E-cadherin, was upregulated by periostin in prostate cancer cells, while Twist, another negative regulator of E-cadherin, was downregulated in bladder cancer cells. The C-terminal region of periostin was sufficient for these functions in bladder cancer cells but not in prostate cancer cells. Knockdown of endogenous Snail by siRNA suppressed cell invasiveness in prostate cancer cells expressing periostin. Periostin also suppressed Akt phosphorylation in bladder cancer cells but enhanced it in prostate cancer cells. Treatment with Akt inhibitor increased E-cadherin expression and suppressed both Twist expression and cell invasiveness of bladder cancer cells. These results indicate that Akt signaling plays a role in the cell-type-dependent regulation of E-cadherin expression and cell invasiveness by periostin via Snail and Twist.

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The increased expression of periostin during early stages of prostate cancer and advanced stages of cancer stroma

Abstract: POSTN, one of the 3DC-associated genes, may serve as a potential biomarker for predicting the pathological grade and prognosis of CaP. Prostate 69: 1398-1403, 2009. (c) 2009 Wiley-Liss, Inc.

Cited by 54 publications

References 21 publications

The role of periostin in neoplastic processes

The role of periostin in neoplastic processes

Heterogenous induction of carcinoma-associated fibroblast-like differentiation in normal human prostatic fibroblasts by co-culturing with prostate cancer cells

Opposite regulation of epithelial-to-mesenchymal transition and cell invasiveness by periostin between prostate and bladder cancer cells

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