RNA interference against SPARC promotes the growth of U-87MG human malignant glioma cells

Liu, Haiyan; Xu, Yuanyuan; Chen, Yun; Zhang, Haowen; Fan, Saijun; Feng, Shuang; Liu, Fenju

doi:10.3892/ol.2011.360

Cited by 4 publications

(3 citation statements)

References 30 publications

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“…SPARC was demonstrated to significantly suppress activation of Akt in hepatic and ovarian carcinoma (35,36). However, SPARC has also been reported to reduce tumor cell apoptosis and promote tumor cell survival by upregulating p-Akt in malignant glioma and melanoma (23,37). In this study, it was observed that Akt pathways, but not ERK pathways, were markedly activated in gastric cancer cells with high levels of expression of SPARC.…”

Section: Discussionmentioning

confidence: 66%

Secreted protein acidic and rich in cysteine antagonizes bufalin-induced apoptosis in gastric cancer cells

et al. 2015

Molecular Medicine Reports

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Bufalin is an active compound in the traditional Chinese medicine Chan Su, which has been shown to induce apoptosis in a range of cancer cell types. However, certain gastric cancer cells are known to be resistant to bufalin. Intracellular secreted protein acidic and rich in cysteine (SPARC) regulates proliferation and apoptosis. This study aimed to evaluate the role of SPARC in bufalin-induced apoptosis in SGC7901 and MGC803 gastric cancer cells. SGC7901 cells with high SPARC expression were more resistant to bufalin than MGC803 cells with low SPARC expression. This resistance was significantly reversed by small interfering (si)RNA-mediated knockdown of SPARC. Furthermore, it was shown that SPARC negatively regulated bufalin-induced intrinsic apoptosis by protecting mitochondrial integrity, decreasing the release of cytoplasmic cytochrome c and increasing the ratio of Bcl-2/Bax. In addition, SPARC overcame bufalin-induced G2/M phase arrest by increasing levels of Cyclin B1 and Cyclin A protein expression. SPARC also activated cellular survival signals, including Src and Akt, but not extracellular signal-regulated kinase. This study demonstrated that SPARC antagonizes bufalin-induced apoptosis via inhibition of the intrinsic apoptosis pathway, inhibition of cell cycle arrest and activation of certain pathways involved in proliferation. This provides novel evidence for SPARC as a potential target by which to sensitize gastric cancer cells to bufalin.

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Section: Discussionmentioning

confidence: 66%

Secreted protein acidic and rich in cysteine antagonizes bufalin-induced apoptosis in gastric cancer cells

et al. 2015

Molecular Medicine Reports

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“…Using glioblastoma as an example, SPARC expression has been correlated with increased migration and poor prognosis in humans (235, 236). However, when SPARC expression was inhibited using shRNA, a human cell line showed increased growth and tumorigenic potential (237). The multiple roles played by SPARC in the tumoral environment complicate its use as a biomarker and as a target for therapeutic inhibition.…”

Section: Introductionmentioning

confidence: 99%

Matricellular proteins in drug delivery: Therapeutic targets, active agents, and therapeutic localization

Sawyer

Kyriakides

2016

Advanced Drug Delivery Reviews

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Extracellular matrix is composed by a complex array of molecules that together provide structural and functional support to cells. These properties are mainly mediated by the activity of collagenous and elastic fibers, proteoglycans, and proteins such as fibronectin and laminin. ECM composition is tissue-specific and could include matricellular proteins whose primary role is to modulate cell-matrix interactions. In adults, matricellular proteins are primarily expressed during injury, inflammation and disease. Particularly, they are closely associated with the progression and prognosis of cardiovascular and fibrotic diseases, and cancer. This review aims to provide an overview of the potential use of matricellular proteins in drug delivery including the generation of therapeutic agents based on the properties and structures of these proteins as well as their utility as biomarkers for specific diseases.

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“…In addition, SPARC induced the migration of glioblastoma cell lines (10) and the downregulation of SPARC expression inhibited cell migration and invasion in malignant gliomas (11). However, other studies suggested that SPARC induced endoplasmic reticulum stress leading to autophagy-mediated apoptosis in neuroblastoma (12), and RNA interference against SPARC promoted the growth of malignant glioma cells (13). The aberrant methylation of SPARC was identified in human laryngeal and hypopharyngeal carcinomas (71).…”

Section: Discussionmentioning

confidence: 99%

Integrative genomic analyses of secreted protein acidic and rich in cysteine and its role in cancer prediction

Wang

Chen

et al. 2014

Molecular Medicine Reports

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Secreted protein acidic and rich in cysteine (SPARC), also termed osteonectin or basement‑membrane‑40 (BM‑40), is a matrix‑associated protein that elicits changes in cell shape, inhibits cell‑cycle progression and affects the synthesis of extracellular matrix (ECM). The final mature SPARC protein has 286 amino acids with three distinct domains, including an NH2‑terminal acidic domain (NT), follistatin‑like domain (FS) and C terminus domain (EC). The present study identified SPARC genes from 14 vertebrate genomes and revealed that SPARC existed in all types of vertebrates, including fish, amphibians, birds and mammals. In total, 21 single nucleotide polymorphisms (SNPs) causing missense mutations were identified, which may affect the formation of the truncated form of the SPARC protein. The human SPARC gene was found to be expressed in numerous tissues or organs, including in the bone marrow, whole blood, lymph node, thymus, brain, cerebellum, retina, heart, smooth muscle, skeletal muscle, spinal cord, intestine, colon, adipocyte, kidney, liver, pancreas, thyroid, salivary gland, skin, ovary, uterus, placenta, cervix and prostate. When searched in the PrognoScan database, the human SPARC gene was also found to be expressed in bladder, blood, breast, glioma, esophagus, colorectal, head and neck, ovarian, lung and skin cancer tissues. It was revealed that the association between the expression of SPARC and prognosis varied in different types of cancer, and even in the same cancer from different databases. It implied that the function of SPARC in these tumors may be multidimensional, functioning not just as a tumor suppressor or oncogene.

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RNA interference against SPARC promotes the growth of U-87MG human malignant glioma cells

Cited by 4 publications

References 30 publications

Secreted protein acidic and rich in cysteine antagonizes bufalin-induced apoptosis in gastric cancer cells

Secreted protein acidic and rich in cysteine antagonizes bufalin-induced apoptosis in gastric cancer cells

Matricellular proteins in drug delivery: Therapeutic targets, active agents, and therapeutic localization

Integrative genomic analyses of secreted protein acidic and rich in cysteine and its role in cancer prediction

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