Identification and characterization of CRG-L2, a new marker for liver tumor development

Graveel, Carrie R.; Harkins-Perry, Sarah R; Acevedo, Luis G.; Farnham, Peggy J.

doi:10.1038/sj.onc.1206309

Cited by 17 publications

(18 citation statements)

References 19 publications

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“…Fold enrichment values were used to obtain the list of candidates with >1.5-fold change and a P value of 0. RNA expression analysis was performed by Hierarchical Clustering using Genesis 1.7.2 software, 4 with the average linkage clustering as agglomeration rule (13). All of the genes from the Illumina platform were used for the clustering analysis.…”

Section: Methodsmentioning

confidence: 99%

“…In attempts to characterize molecular changes that occur during the development of HCC, several previous studies have compared RNA expression levels in normal versus tumor liver using techniques such as directed analysis of the expression of candidate genes, serial analysis of gene expression assays, differential display, and hybridization of cDNA arrays (2)(3)(4)(5)(6)(7)(8). Gene expression alterations involving loss of checkpoint control have been commonly observed (see ref.…”

Section: Introductionmentioning

confidence: 99%

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Analysis of the Mechanisms Mediating Tumor-Specific Changes in Gene Expression in Human Liver Tumors

Acevedo

Bieda

Green³

et al. 2008

Cancer Research

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There is widespread interest in efficient characterization of differences between tumor and normal samples. Here, we show an effective methodology for genome-scale characterization of tumors. Using matched normal and tumor samples from liver cancer patients, as well as non-cancer-related normal liver tissue, we first determined changes in gene expression as monitored on RNA expression arrays. We identified several hundred mRNAs that were consistently changed in the tumor samples. To characterize the mechanisms responsible for creation of the tumor-specific transcriptome, we performed chromatin immunoprecipitation on microarray experiments to assay binding of RNA polymerase II, H3me3K27, and H3me3K9 and DNA methylation in 25,000 promoter regions. These experiments identified changes in active and silenced regions of the genome in the tumor cells.

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Section: Methodsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Analysis of the Mechanisms Mediating Tumor-Specific Changes in Gene Expression in Human Liver Tumors

Acevedo

Bieda

Green³

et al. 2008

Cancer Research

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“…The C-terminal half of this protein was named the olfactomedin domain. Regions similar to the olfactomedin domain were subsequently found in a variety of proteins from different tissues and species ranging from sea urchin to human [2][3][4][5][6][7][8][9]. Some of the olfactomedin domain-containing proteins are membrane proteins.…”

Section: Introductionmentioning

confidence: 99%

Optimedin induces expression of N-cadherin and stimulates aggregation of NGF-stimulated PC12 cells

Lee

Tomarev

2007

Experimental Cell Research

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Optimedin, also known as olfactomedin 3, belongs to a family of olfactomedin domain-containing proteins. It is expressed in neural tissues and Pax6 is involved in the regulation of its promoter. To study possible effects of optimedin on the differentiation of neural cells, we produced stably transfected PC12 cell lines expressing optimedin under a tetracycline-inducible promoter. Cells expressing high levels of optimedin showed higher growth rates and stronger adhesion to the collagen extracellular matrix as compared with control PC12 cells. After stimulation with nerve growth factor (NGF), optimedin-expressing cells demonstrated elevated levels of N-cadherin, β-catenin, α-catenin, and occludin as compared with stimulated, control PC12 cells. Expression of optimedin induced Ca 2+ -dependent aggregation of NGF-stimulated PC12 cells and this aggregation was blocked by the expression of N-cadherin siRNA. Expression of optimedin also changed the organization of the actin cytoskeleton and inhibited neurite outgrowth in NGF-stimulated PC12 cells. We suggest that expression of optimedin stimulates the formation of adherent and tight junctions on the cell surface and this may play an important role in the differentiation of the brain and retina through the modulation of cytoskeleton organization, cell-cell adhesion and migration.

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“…Olfactomedin domain was originally identified in a glycoprotein isolated from the olfactory epithelium of frogs (71) and subsequently was found in a group of proteins forming a family of olfactomedin domaincontaining proteins. The family of olfactomedin domain-containing proteins includes both secreted and membrane-bound proteins that each exhibit a characteristic distribution in different tissues (4,10,27,30,44,51,58,78,79). Most of the glaucomacausing mutations in myocilin are located in the olfactomedin domain (1,2,18,19,24,72).…”

mentioning

confidence: 99%

Myocilin Is a Modulator of Wnt Signaling

Kwon

Lee

et al. 2009

Molecular and Cellular Biology

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It is well documented that mutations in the MYOCILINGlaucoma is a leading cause of blindness in the world. Primary open-angle glaucoma is the most common form of glaucoma. It will affect more than 60 million and blind about 4.5 million people worldwide by the year 2010 (62). It is now well established that a genetic component may contribute to glaucoma, and several glaucoma-associated genes have been identified. The first-identified and the most-studied gene is MYOCILIN (MYOC), which is highly expressed in and secreted by the trabecular meshwork (1,19,72,75,77,78), one of the key components of the eye aqueous humor outflow system. Dominant mutations in MYOC may lead to juvenile openangle glaucoma and are found in 3 to 4% of patients with primary open-angle glaucoma (18,19). The encoded protein, myocilin, belongs to a family of glycosylated proteins containing a C-terminal olfactomedin domain (57,90,91). Olfactomedin domain was originally identified in a glycoprotein isolated from the olfactory epithelium of frogs (71) and subsequently was found in a group of proteins forming a family of olfactomedin domaincontaining proteins. The family of olfactomedin domain-containing proteins includes both secreted and membrane-bound proteins that each exhibit a characteristic distribution in different tissues (4,10,27,30,44,51,58,78,79). Most of the glaucomacausing mutations in myocilin are located in the olfactomedin domain (1,2,18,19,24,72).Besides the trabecular meshwork and sclera (1, 77), high levels of MYOC were observed in the ciliary body (1, 13, 39), iris (89), retinal pigment epithelium/choroid (78, 88), and optic nerve (74). Low levels of MYOC expression were detected in several nonocular tissues (75). Myocilin, being a secreted protein, was also found in the aqueous humor, an intraocular fluid responsible for the supply of nutrients and for removal of metabolites from the avascular tissues of the eye anterior segment (63, 65). Some mutations in the MYOC gene lead to the inhibition of mutated myocilin secretion. Secretion of wildtype myocilin also can be reduced or blocked in the presence of mutated myocilin (22,36,52). It has been suggested that the intracellular accumulation of myocilin aggregates is deleterious to the trabecular meshwork cells, resulting in the deterioration of their function and subsequent elevation of intraocular pressure (IOP) (38,49).Although the MYOC gene has been studied for more than 10 years, the functions of myocilin protein are still not well understood (19,75). Biochemical data indicate that myocilin may interact with several intracellular and extracellular matrix proteins (16,37,48,61,73,78), although the biological significance of such interactions is not clear. The absence of openangle glaucoma in an elderly woman homozygous for the Arg46Stop mutation (45), as well as the absence of glaucoma in people hemizygous for MYOC (87), suggests that the loss of functional myocilin is not critical for the development of glaucoma or for normal eye functioning. These observations are supporte...

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Identification and characterization of CRG-L2, a new marker for liver tumor development

Cited by 17 publications

References 19 publications

Analysis of the Mechanisms Mediating Tumor-Specific Changes in Gene Expression in Human Liver Tumors

Analysis of the Mechanisms Mediating Tumor-Specific Changes in Gene Expression in Human Liver Tumors

Optimedin induces expression of N-cadherin and stimulates aggregation of NGF-stimulated PC12 cells

Myocilin Is a Modulator of Wnt Signaling

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