Gpnmb/osteoactivin, an attractive target in cancer immunotherapy

Zhou, Letian; Liu, F Y; Li, Y; Peng, Y M; Liu, Y H; Li, J

doi:10.4149/neo_2012_001

Cited by 52 publications

(48 citation statements)

References 35 publications

(67 reference statements)

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“…GPNMB is localized on the plasma membrane as well as in subcellular locations in various cell types. In normal cells, it is preferentially localized intracellularly, such as in melanosomes and endosomal/lysosomal compartments [13–16]. However, in cancer cells, including melanoma,TNBC, and glioblastomas, overall GPNMB expression increases and a greater proportion becomes plasma membrane-localized [5,8,17].…”

Section: Gpnmb Structure and Functionmentioning

confidence: 99%

“…In addition to bone, GPNMB is expressed in immune cells, such as macrophages and dendritic cells [14,29], and may impair T-cell activation to down-modulate anti-tumor immune responses [13,30,31]. Expression of GPNMB in antigen presenting cells such as macrophages and dendritic cells is well documented, which explains its designation as ‘dendritic cell-heparin integrin ligand’ (DC-HIL) [21].…”

Section: Gpnmb Is Involved In Physiological Processes In Normal Tissuesmentioning

confidence: 99%

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Glycoprotein Non-Metastatic Melanoma Protein B (GPNMB) and Cancer: A Novel Potential Therapeutic Target

Taya

Hammes

2018

Steroids

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Glycoprotein non-metastatic melanoma protein B (GPNMB) is a transmembrane protein enriched on the cell surface of cancer cells, including melanoma, glioblastoma, and triple-negative breast cancer. There is growing evidence identifying GPNMB as a tumor-promoter; however, despite its biological and clinical significance, the molecular mechanisms engaged by GPNMB to promote tumorigenesis are not well understood. GPNMB promotes aggressive behaviors such as tumor cell proliferation, migration, and invasion. The extracellular domain of GPNMB shed from the cell surface interacts with integrins to facilitate in the recruitment of immune-suppressive and pro-angiogenic cells to the tumor microenvironment, thereby enhancing tumor migration and invasion. GPNMB also modulates receptor tyrosine kinases and integrin signaling in a cell autonomous fashion, leading to downstream kinase signaling that in turn triggers the expression and secretion of tumorigenic factors such as matrix metalloproteinases (MMPs) and cytokines. Therefore, GPNMB exerts its pro-tumorigenic role both intracellularly and in a paracrine fashion through shedding its extracellular domain. This review highlights the importance of GPNMB in cancer progression and discusses molecular mediators of GPNMB-induced tumor growth and invasion.

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Section: Gpnmb Structure and Functionmentioning

confidence: 99%

Section: Gpnmb Is Involved In Physiological Processes In Normal Tissuesmentioning

confidence: 99%

Glycoprotein Non-Metastatic Melanoma Protein B (GPNMB) and Cancer: A Novel Potential Therapeutic Target

Taya

Hammes

2018

Steroids

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“…3,4 Furthermore, GPNMB overexpression has been observed in many cancers, such as metastatic prostate cancer, glioma, and hepatocellular carcinoma. 5,6 In terms of glioma, GPNMB was recently identified to be aberrantly overexpressed in human glioma tissue. 3 As a potential molecular therapeutic target, GPNMB was selected to perform molecular targeting therapy for GPNMB-expressing gliomas by antibody-mediated delivery of cytotoxic agents.…”

Section: Introductionmentioning

confidence: 99%

Glycoprotein non-metastaticmelanoma protein B promotes glioma motility and angiogenesis through the Wnt/β-catenin signaling pathway

Bao

Wang

et al. 2016

Exp Biol Med (Maywood)

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Glioma is a common tumor with high mortality and poor overall survival. However, the regulatory mechanisms of glioma tumorigenesis and glioma cell motility are completely unknown. Here, we investigated the role of glycoprotein non-metastatic melanoma protein B in glioma. The expression of glycoprotein non-metastatic melanoma protein B is observed to be aberrantly regulated in glioma tissues and cells, and high levels of glycoprotein non-metastatic melanoma protein B present an inverse correlation with the survival of glioma patients. Compared with the control, glycoprotein non-metastatic melanoma protein B inhibition significantly retarded the proliferation and migration of human glioma cells. The tube formation ability of HBMECs induced by glioma cells was also remarkably reduced by glycoprotein non-metastatic melanoma protein B silencing. Increased levels of VEGF-C and TEM7 were down-regulated by the suppression of glycoprotein non-metastatic melanoma protein B in glioma cells. Additionally, the activity of MMP-2/3/9 was assessed in glioma cells using Western blotting and gelatin zymography assay; their activities were strongly decreased following the suppression of glycoprotein non-metastatic melanoma protein B. Further studies suggested that canonical Wnt/b-catenin pathway was activated, but was inactivated by glycoprotein non-metastatic melanoma protein B suppression in glioma cells.In conclusion, we demonstrate that glycoprotein non-metastatic melanoma protein B might be an inducer for glioma and could enhance matrix metalloproteinase activity through Wnt/b-catenin pathway to contribute to glioma tumorigenesis. This may represent a new understanding for malignant glioma.

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“…For example, the receptor tyrosine protein kinase ERBB2 (also known as HER2) is expressed in only twofold excess in breast cancer relative to normal tissue 41 , whereas CD30 is expressed in 3.3-fold and 4.4-fold excess in Hodgkin's lymphoma 42 and anaplastic large cell lymphoma 43 , respectively. Transmembrane protein NMB is similarly present in fourfold excess in melanoma relative to healthy tissue 44,45 . Other examples of receptors that are commonly overexpressed in certain types of cancer include hepatocyte growth factor receptor (encoded by MET) 46,47 , luteinizing hormone-releasing hormone receptor 48 and epidermal growth factor (EGF) receptor 49 .…”

mentioning

confidence: 99%

Principles in the design of ligand-targeted cancer therapeutics and imaging agents

Srinivasarao

Galliford

Low

2015

Nat Rev Drug Discov

557

488

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Most cancer drugs are designed to interfere with one or more events in cell proliferation or survival. As healthy cells may also need to proliferate and avoid apoptosis, anticancer agents can be toxic to such cells. To minimize these toxicities, strategies have been developed wherein the therapeutic agent is targeted to tumour cells through conjugation to a tumour-cell-specific small-molecule ligand, thereby reducing delivery to normal cells and the associated collateral toxicity. This Review describes the major principles in the design of ligand-targeted drugs and provides an overview of ligand-drug conjugates and ligand-imaging-agent conjugates that are currently in development.

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Gpnmb/osteoactivin, an attractive target in cancer immunotherapy

Cited by 52 publications

References 35 publications

Glycoprotein Non-Metastatic Melanoma Protein B (GPNMB) and Cancer: A Novel Potential Therapeutic Target

Glycoprotein Non-Metastatic Melanoma Protein B (GPNMB) and Cancer: A Novel Potential Therapeutic Target

Glycoprotein non-metastaticmelanoma protein B promotes glioma motility and angiogenesis through the Wnt/β-catenin signaling pathway

Principles in the design of ligand-targeted cancer therapeutics and imaging agents

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