SPARC overexpression in primary tumors correlates with disease recurrence and overall survival in patients with triple negative breast cancer

Zhu, Anjie; Yuan, Peng; Du, Feng; Hong, Ruoxi; Ding, Xiaoyan; Shi, Xiuqing; Fan, Ying; Wang, Jiayu; Luo, Yang; Ma, Fei; Zhang, Pin; Li, Qing; Xu, Binghe

doi:10.18632/oncotarget.10532

Cited by 54 publications

(69 citation statements)

References 22 publications

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“…The pathological complete response and secreted protein acidic and rich in cysteine expression in patients with breast cancer receiving neoadjuvant nab-paclitaxel chemotherapy dehydrogenase (DPD) (7), ATP-binding cassette, sub-family B, member 1 (MDR1) (8), ATP-binding cassette, sub-family C, member 1 (MRP1) (9), and topoisomerase (DNA) II alpha (Topo IIα) (10,11), have attracted attention as predictive factors of treatment response to chemotherapy. Secreted protein acidic and rich in cysteine (SPARC), also known as osteonectin or BM-40, is an albumin-binding glycoprotein that is secreted by cells to modulate their interactions with the extracellular matrix (12)(13)(14)(15)(16)(17)(18). SPARC plays a critical role in the regulation of cellular functions, such as proliferation and cell migration, and its overexpression is associated with tumor growth, metastasis, and aggressiveness (12)(13)(14)(15)(16)(17)(18)(19).…”

Section: Introductionmentioning

confidence: 99%

The pathological complete response and secreted protein acidic and rich in cysteine expression in patients with breast cancer receiving neoadjuvant nab‑paclitaxel chemotherapy

Nakazawa

Kurozumi

et al. 2020

Oncol Lett

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Biomarkers that can accurately predict treatment response are required for indicating optimal neoadjuvant treatments. The current study assessed the predictive value of secreted protein acidic and rich in cysteine (SPARC) mRNA expression for the response to neoadjuvant nab-paclitaxel (nab-PTX) therapy in patients with breast cancer. It was hypothesized that SPARC expression can affect the response to albumin-bound taxanes, including nab-PTX since SPARC binds albumin with a high affinity. Pre-therapeutic specimens of core needle biopsies were analyzed from 50 patients in a phase II trial of neoadjuvant nab-PTX and the factors that were associated with a pathological complete response (pCR) were assessed. The pre-therapeutic tumor mRNA levels of chemotherapy-related proteins were quantified, including SPARC, and the correlations with post-therapeutic clinicopathological factors were assessed, including with pCR. The results demonstrated that pre-therapeutic SPARC mRNA expression was significantly higher in non-pCR patients compared with patients with pCR (92.37±55.33 vs. 56.53±30.19; P=0.027). A cutoff point of 48.5 was determined using receiver operating characteristic (ROC) curve analysis (sensitivity, 83.3%; specificity, 50.0%), and patients were classified into low and high SPARC expression groups. High SPARC expression was associated with histological grade (P=0.035), estrogen receptor expression (P=0.037), and progesterone receptor expression (P=0.002) but not with HER2 (P=0.895), and Ki-67 LI (P=0.743) expression. The results of the current study indicated that a high SPARC mRNA expression was a negative predictor of pCR following neoadjuvant nab-PTX therapy regardless of breast cancer subtype. The phase II study was conducted in accordance with the Declaration of Helsinki, and the protocol was approved by the Ethics Committee of the National Hospital Organization Takasaki General Medical Center (Registration nos. H23-9 and H23-33).

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Section: Introductionmentioning

confidence: 99%

The pathological complete response and secreted protein acidic and rich in cysteine expression in patients with breast cancer receiving neoadjuvant nab‑paclitaxel chemotherapy

Nakazawa

Kurozumi

et al. 2020

Oncol Lett

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“…The correlation between SPARC expression and poor prognosis [22] has been corroborated in a breast cancer subgroup enriched for an ECM gene signature, named ECM3, which has SPARC as a leading gene. This signature identifies high-grade tumors with EMT features and the likelihood to progress and metastasize [25].…”

Section: Tumor-produced Opn and Sparc Affect Mdsc Recruitment And Phementioning

confidence: 89%

“…Matricellular proteins are released by several cell subsets populating the tumor microenvironment; they are abundantly produced by neoplastic cells, whereas less expressed by infiltrating accessory cells. High expression of OPN and SPARC has been reported in both mouse tumor models and human cancers and correlates with aggressive disease and poor prognosis [21,22].…”

Section: Tumor-produced Opn and Sparc Affect Mdsc Recruitment And Phementioning

confidence: 99%

Matricellular proteins tune myeloid-derived suppressor cell recruitment and function in breast cancer

Chiodoni

Sangaletti

Colombo

2017

Journal of Leukocyte Biology

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Solid tumor progression is often associated with the expansion of myeloid-derived suppressor cells (MDSCs), a heterogeneous population of immature myeloid cells that actively foster tumor growth and metastatic dissemination through a plethora of mechanisms, including, but not limited to, their major suppressive activity on the immune response. Indeed, MDSCs may sustain tumor progression by dynamically remodeling the tumor microenvironment through the production of angiogenic factors and metalloproteases, by helping the establishment of a premetastatic niche, and by promoting stemness and epithelial-to-mesenchymal transition (EMT) features in tumor cells. MDSCs are also regulated by a growing list of factors that mainly comprise 2 sets of signals: those responsible for their expansion and recruitment, such as GM-, M-, and G-CSF and other growth factors, and those relevant for the induction of their suppressive activity, which include proinflammatory cytokines and transcription factors. We review here a new class of MDSC regulators-matricellular proteins-with a particular focus on osteopontin (OPN) and secreted acidic cysteine-rich glycoprotein (SPARC), which seem to affect the expansion/recruitment and the immune-suppressive activity of MDSCs. Matricellular proteins function indirectly on MDSCs through the induction of other mediators when produced by tumor cells and cell autonomously when expressed-likely in an intracellular form-directly by MDSCs.

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“…SPARC promoted the formation of tumor stroma and migration in endometrial cancer stem‐like cells . High SPARC level in triple‐negative breast cancer patients contributed to a decreased disease‐free survival . Overexpression of SPARC was associated with poor prognosis in cervical carcinoma patients .…”

Section: Introductionmentioning

confidence: 98%

“…Secreted protein acidic and rich in cysteine (SPARC), also known as osteonectin or BM‐40, is a 43‐kD glycoprotein and has a high binding affinity to albumin. SPARC regulates the interactions of cells and their extracellular matrix, modulates the cells’ microenvironment, and has an important effects on cell proliferation, survival, and migration . SPARC was secreted by endothelial cells and usually expressed in bone or normal tissues that undergo development or repair.…”

Section: Introductionmentioning

confidence: 99%

SPARC acts as a mediator of TGF‐β1 in promoting epithelial‐to‐mesenchymal transition in A549 and H1299 lung cancer cells

et al. 2018

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Migration and metastasis of tumor cells greatly contributes to the failure of cancer treatment. Recently, the extracellular protein secreted protein acidic and rich in cysteine (SPARC) has been reported closely related to tumorigenesis. Some articles have suggested that SPARC promoted metastasis in several highly metastatic tumors. However, there are also some studies shown that SPARC acted as an antitumor factor. SPARC-induced epithelial-tomesenchymal transition (EMT) in melanoma cells and promoted EMT in hepatocellular carcinoma. Therefore, the role of SPARC in tumorigenesis and its relationship with EMT is still unclear. In this study, we investigated the expression change of SPARC in A549 and H1299 lung cancer cells undergoing EMT process. Our study indicated that SPARC was upregulated in A549 and H1299 cells EMT process. We further investigated the function of SPARC on proliferation, migration, and EMT process of A549 and H1299 cells. Overexpression of SPARC promoted the migration and EMT of A549 and H1299 cells. Knockdown SPARC inhibited the EMT of A549 cells. Overexpression of SPARC induced the increased expression of p-Akt and P-ERK. Furthermore, exogenous SPARC peptide promoted transforming growth factor (TGF)-β1-induced EMT of A549 and H1299 cells. SPARC knockdown partially eliminated TGF-β1 function in inducing EMT of A549 cells. SPARC follistatin-like functional domain reduced the expression of E-cadherin, but had no effect on the expression of p-Akt and p-ERK. In conclusion, we elucidated that SPARC contributes to tumorigenesis by promoting migration and EMT of A549 and H1299 lung cancer cells. These results will provide some new suggestion for lung cancer treatment. © 2018 BioFactors, 44(5):453-464, 2018Abbreviations: A549, A human lung adenocarinoma epithelial cell line; Akt, A serine/threonine-specific protein kinase; BSA, bovine serum albumin; CCK-8, cell counting kit-8; DMEM, Dulbecco's modified Eagle's Medium; EC, extracellular calcium-binding domain; EDTA, ethylenediaminetetraacetic acid; EGFP, enhancer green fluorescent protein; EGF, epidermal growth factor; EMT, epithelial-to-mesenchymal transition; ERK, extracellular signal-regulated kinases; FBS, fetal bovine serum; FS, follistatin-like functional domain; Fyn, Fyn proto-oncogene, Src family tyrosine kinase; GAPDH, glyceraldehyde-3-phosphate dehydrogenase; H1299, A human non-small cell lung carcinoma cell line; ILK, integrin-linked kinase; MDM2, mouse double minute 2 homolog; NF-κB, nuclear factor kappa B subunit 1; Nab-PTX, nanoparticle albumin bound paclitaxel; NSCLC, nonsmall cell lung cancer; NT, N terminal acidic domain; PBS, phosphate-buffered saline; PARP, poly (ADP-ribose) polymerase 1; PMSF, phenylmethane sulfonyl fluoride; RIPA, radioimmunoprecipitation assay buffer; SDS, sodium dodecyl sulfate; SPARC, secreted protein acidic and rich in cysteine; TGF-β, transforming growth factor; TBST, a mixture of tris-buffered saline and Tween 20 Additional Supporting Information may be found in the online version of this article.

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SPARC overexpression in primary tumors correlates with disease recurrence and overall survival in patients with triple negative breast cancer

Cited by 54 publications

References 22 publications

The pathological complete response and secreted protein acidic and rich in cysteine expression in patients with breast cancer receiving neoadjuvant nab‑paclitaxel chemotherapy

The pathological complete response and secreted protein acidic and rich in cysteine expression in patients with breast cancer receiving neoadjuvant nab‑paclitaxel chemotherapy

Matricellular proteins tune myeloid-derived suppressor cell recruitment and function in breast cancer

SPARC acts as a mediator of TGF‐β1 in promoting epithelial‐to‐mesenchymal transition in A549 and H1299 lung cancer cells

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