Abstract
Protein arginine methyltransferase 5 (PRMT5) catalyzes the formation of ω-NG,N'G-symmetric dimethylarginine residues on histones as well as other proteins. These modifications play an important role in cell differentiation and tumor cell growth. However, the role of PRMT5 in human glioma cells has not been characterized. In this study, we assessed protein expression profiles of PRMT5 in control brain, WHO grade II astrocytomas, anaplastic astrocytomas, and glioblastoma multiforme (GBM) by immunohistochemistry. PRMT5 was low in glial cells in control brain tissues and low grade astrocytomas. Its expression increased in parallel with malignant progression, and was highly expressed in GBM. Knockdown of PRMT5 by small hairpin RNA caused alterations of p-ERK1/2 and significantly repressed the clonogenic potential and viability of glioma cells. These findings indicate that PRMT5 is a marker of malignant progression in glioma tumors and plays a pivotal role in tumor growth.
Publication types
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Research Support, N.I.H., Extramural
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, Non-P.H.S.
MeSH terms
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Adult
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Aged
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Arginine / analogs & derivatives
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Arginine / metabolism
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Brain Neoplasms / metabolism*
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Brain Neoplasms / pathology
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Cell Differentiation / genetics
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Cell Proliferation / genetics
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Cell Proliferation / physiology*
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Colonic Neoplasms / metabolism
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Colonic Neoplasms / pathology
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Colony-Forming Units Assay
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Epithelium / metabolism
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Epithelium / pathology
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Female
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Glial Fibrillary Acidic Protein / metabolism
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Glioma / metabolism*
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Glioma / pathology
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Humans
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MAP Kinase Signaling System / genetics
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Male
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Middle Aged
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Neurons / metabolism
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Phosphopyruvate Hydratase / metabolism
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Protein-Arginine N-Methyltransferases / genetics
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Protein-Arginine N-Methyltransferases / metabolism*
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RNA, Small Interfering / genetics
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RNA, Small Interfering / metabolism
Substances
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Glial Fibrillary Acidic Protein
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RNA, Small Interfering
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dimethylarginine
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Arginine
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PRMT5 protein, human
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Protein-Arginine N-Methyltransferases
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Phosphopyruvate Hydratase