Tissue and subcellular distribution of CLIC1

Ulmasov, Barbara; Bruno, Jonathan; Woost, Philip G.; Edwards, John C.

doi:10.1186/1471-2121-8-8

Cited by 64 publications

(40 citation statements)

References 41 publications

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“…CLIC1 was originally identified as a nuclear chloride channel protein (NCC27) in a macrophage cell line, but since its discovery CLIC1 expression has been detected in many different tissues (17, 18). Despite its ubiquitous expression, CLIC1 has regularly been shown to be up-regulated in patients with malignant tumors of the brain, liver, lung, ovaries and gastro-intestinal tract and in many of these malignancies, CLIC1 expression correlates with aggressive disease and poor outcome (12, 19–22).…”

Section: Discussionmentioning

confidence: 99%

Relocation of CLIC1 Promotes Tumor Cell Invasion and Colonization of Fibrin

Gurski

Knowles

Basse

et al. 2015

Molecular Cancer Research

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Chloride intracellular channel 1 (CLIC1) has been shown to be up-regulated in various malignancies but its exact function remains unclear. Here, it is revealed that CLIC1 is critical for the stability of invadopodia in endothelial and tumor cells embedded in a 3-dimensional (3D) matrix of fibrin. Invadopodia stability was associated with the capacity of CLIC1 to induce stress fiber and fibronectin matrix formation following its β3 integrin (ITGB3)-mediated recruitment into invadopodia. This pathway, in turn, was relevant for fibrin colonization as well as slug (SNAI2) expression and correlated with a significant role of CLIC1 in metastasis in vivo. Mechanistically, a reduction of myosin light chain kinase (MYLK) in CLIC1- as well as β3 integrin-depleted cells suggests an important role of CLIC1 for integrin-mediated actomyosin dynamics in cells embedded in fibrin. Overall, these results indicate that CLIC1 is an important contributor to tumor invasion, metastasis and angiogenesis. Implications This study uncovers an important new function of CLIC1 in the regulation of cell-extracellular matrix interactions and ability of tumor cells to metastasize to distant organs.

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Section: Discussionmentioning

confidence: 99%

Relocation of CLIC1 Promotes Tumor Cell Invasion and Colonization of Fibrin

Gurski

Knowles

Basse

et al. 2015

Molecular Cancer Research

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“…The chromate uptake is mediated by the general anion channel band-3 protein (5) now understood as the chloride intracellular channel (CLIC) carrier proteins. The CLICs play important roles in various cellular functions (6). The (CLIC) proteins are small proteins related to the omega family of glutathione S-transferases (GSTs)(7).…”

Section: Transport Of Hexavalent Chromium Ion Through the Chloridmentioning

confidence: 99%

Review of Chromium (VI) Apoptosis, Cell-Cycle-Arrest, and Carcinogenesis

Chiu

Shi

Lee

et al. 2010

Journal of Environmental Science and Health, Part C

100

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Hexavalent chromium combines with glutathione in chloride intracellular channel carrier to form tetravalent and pentavelent chromium in plasma and organelle membranes. It also combines with NADH/NADPH to form pentavalent chromium in mitochondria. Tetravalent- and pentavalent- chromium (directly and indirectly) mediated DNA double strand breaks activate DNA damage signaling sensors: DNA-dependent-protein-kinase signals p53-dependent intrinsic mitochorndrial apoptosis, and ataxia-telangiectasia-mutated and ataxia-telangiectasia-Rad3-related signal cell-arrest for DNA repair. Tetravalent chromium may be the most potent species since it causes DNA breaks and somatic recombination, but not apoptosis. Upon further failure of apoptosis and senescence/DNA-repair, damaged cells may become immortal with loss-of-heterozygosity and genetic plasticity.

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“…We investigated this through indirect immunofluorescence of MCF10A monolayers treated with digitonin, which permeabilizes the plasma membrane and allows the selective extraction of cytosolic but not nuclear proteins (20,32). Maspin was fully extractable from the cytoplasm, suggesting that it is a soluble protein that is not associated with the cytoskeleton or any other cytoplasmic structure, and as expected, a fraction remained associated with the nucleus (Fig.…”

Section: Maspin Is Not Released From Cells On Addition Of a Conventiomentioning

confidence: 99%

Maspin (SERPINB5) Is an Obligate Intracellular Serpin

Teoh

Whisstock

Bird

2010

Journal of Biological Chemistry

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Maspin (SERPINB5) is a tumor suppressor lost in breast and prostate cancer whose molecular function is unknown. It is a non-inhibitory member of the clade B serpins suggested to play a role in a plethora of intracellular and extracellular settings, yet its normal cellular distribution has never been clarified. Here we investigate the distribution of maspin in non-transformed human epithelial cells. By indirect immunofluorescence, maspin has a nucleocytoplasmic distribution in breast (MCF10A) and prostate (RWPE-1) cells and, by immunoblotting and pulse-chase analyses, is neither glycosylated nor secreted. Cell surface biotinylation studies also show that maspin is not present at the cell surface. Differentiation of MCF10A cells into three-dimensional acini results in the redistribution of maspin from the nucleus to the cytoplasm but does not result in secretion. Addition of an efficient conventional signal peptide to maspin directs it into the secretory pathway and results in glycosylation but not secretion. We further show that maspin in the cytoplasm of MCF10A cells is a soluble monomeric protein that is not detectably associated with the cytoskeleton or other extractable components. Taken together, these results suggest that maspin is restricted to an intracellular, possibly nuclear, role in which it influences cell-matrix interactions indirectly. It is probably released only as a consequence of cell damage or necrosis.

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Tissue and subcellular distribution of CLIC1

Abstract: Background: CLIC1 is a chloride channel whose cellular role remains uncertain. The distribution of CLIC1 in normal tissues is largely unknown and conflicting data have been reported regarding the cellular membrane fraction in which CLIC1 resides.

Cited by 64 publications

References 41 publications

Relocation of CLIC1 Promotes Tumor Cell Invasion and Colonization of Fibrin

Relocation of CLIC1 Promotes Tumor Cell Invasion and Colonization of Fibrin

Review of Chromium (VI) Apoptosis, Cell-Cycle-Arrest, and Carcinogenesis

Maspin (SERPINB5) Is an Obligate Intracellular Serpin

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