Coamplification in Tumors ofKRAS2,Type 2 Inositol 1,4,5 Triphosphate Receptor Gene, and a Novel Human Gene,KRAG

Heighway, Jim; Betticher, Daniel; Hoban, Paul R.; Altermatt, Hans Jörg; Cowen, Rachel L.

doi:10.1006/geno.1996.0340

Cited by 31 publications

(24 citation statements)

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“…IP 3 R3 expression is also increased in MCF-7 cells induced to proliferate with estradiol (Szatkowski et al, 2010). An increase in IP 3 R2 expression together with KRas has been observed in non-small cell lung cancer (NSCLC) cells (Heighway et al, 1996). Given the differing properties of each IP 3 R isoform, this change in isoform composition following K-Ras deletion might have important consequences.…”

Section: Discussionmentioning

confidence: 99%

Oncogenic K-Ras suppresses IP3-dependent Ca2+ release through remodeling of IP3Rs isoform composition and ER luminal Ca2+ levels in colorectal cancer cell lines

Pierro

Cook

Foets

et al. 2014

Journal of Cell Science

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Section: Discussionmentioning

confidence: 99%

Oncogenic K-Ras suppresses IP3-dependent Ca2+ release through remodeling of IP3Rs isoform composition and ER luminal Ca2+ levels in colorectal cancer cell lines

Pierro

Cook

Foets

et al. 2014

Journal of Cell Science

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“…The exon structure of the cDNA clones was confirmed by PCR, and the 5Ј sequence was determined by direct analysis of biotinylated PCR products, as described previously (13). Sequencing analysis of the clones was performed using dye terminator cycling and analyzed on a 373A Stretch Fluorescent Automated sequencer (Applied Biosystems).…”

Section: Methodsmentioning

confidence: 99%

“…Northern Blotting-Adult human multiple tissue Northern blots (CLONTECH) containing 2 g of poly(A ϩ ) RNA per lane were probed with PCR-amplified probes representing the full-length cDNA (exons 1 to 3) of sarcospan (13).…”

Section: Methodsmentioning

confidence: 99%

Sarcospan, the 25-kDa Transmembrane Component of the Dystrophin-Glycoprotein Complex

Crosbie

Heighway

Venzke

et al. 1997

Journal of Biological Chemistry

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178

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The dystrophin-glycoprotein complex is a multisubunit protein complex that spans the sarcolemma and forms a link between the subsarcolemmal cytoskeleton and the extracellular matrix. Primary mutations in the genes encoding the proteins of this complex are associated with several forms of muscular dystrophy. Here we report the cloning and characterization of sarcospan, a unique 25-kDa member of this complex. Topology algorithms predict that sarcospan contains four transmembrane spanning helices with both N-and C-terminal domains located intracellularly. Phylogenetic analysis reveals that sarcospan's arrangement in the membrane as well as its primary sequence are similar to that of the tetraspan superfamily of proteins. Sarcospan co-localizes and co-purifies with the dystrophin-glycoprotein complex, demonstrating that it is an integral component of the complex. We also show that sarcospan expression is dramatically reduced in muscle from patients with Duchenne muscular dystrophy. This suggests that localization of sarcospan to the membrane is dependent on proper dystrophin expression. The gene encoding sarcospan maps to human chromosome 12p11.2, which falls within the genetic locus for congenital fibrosis of the extraocular muscle, an autosomal dominant muscular dystrophy.In skeletal muscle fibers, the dystrophin-glycoprotein complex (DGC) 1 (1-5) is located at the sarcolemma and is composed of both peripheral and integral membrane proteins. Collectively, these proteins provide a physical connection between the extracellular matrix and the intracellular cytoskeleton of muscle cells. Disruption of this linkage eventually progresses to muscle cell necrosis, as evidenced by the dystrophic muscle phenotypes that result from defects in several of the DGC components (for review, see Refs. 6 and 7). Although the DGC is known to be essential for normal muscle function, the precise role of this multi-protein complex remains to be determined.Purification of the DGC has led to the identification of many of its constituent polypeptides, which range in size from 25 kDa to over 400 kDa and include glycosylated as well as non-glycosylated proteins (1-4). Characterization of these proteins has increased our understanding of how the DGC is oriented in the sarcolemma and has provided clues to its function. In addition to dystrophin, the DGC consists of ␣/␤-dystroglycan, the sarcoglycans (␣, ␤, ␥, and ␦ subunits), and the syntrophins. While most of the "dystrophin-associated proteins" (DAPs) have been identified, one of them, a 25-kDa protein (also called A5) (1,(3)(4)(5), has remained an enigma.In the present work, we have determined the amino acid sequence of two peptides derived from 25DAP and have isolated the corresponding human cDNA. Previous analysis of the 25DAP indicated that it is an integral membrane protein, since it reacts strongly with a probe for protein hydrophobicity (4). We now report that 25DAP is a novel component of the DGC and is predicted to span the sarcolemma four times. This is unusual for integral membrane...

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“…These five genes are frequently associated with tumorigenesis. For example, KRAG is expressed in lung and ovarian carcinoma cells, 55 but its functional role has not been described in these tumors. RRAS2 is frequently overexpressed in squamous carcinoma cells 56 and in esophageal 57 and breast carcinomas.…”

Section: Btf3 In Pancreatic Cancermentioning

confidence: 99%

Basic transcription factor 3 (BTF3) regulates transcription of tumor-associated genes in pancreatic cancer cells

Kusumawidjaja

Kayed

Giese

et al. 2007

Cancer Biology & Therapy

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Basic transcription factor 3 (BTF3) acts as a transcription factor and modulator of apoptosis, and is differentially expressed in colorectal cancer and glioblastomas. In the present study, the expression of BTF3, as well as its role in apoptosis and gene transcription, was analyzed in pancreatic ductal adenocarcinoma (PDAC). QRT-PCR, immunohistochemistry, immunoblotting, and immunofluorescence analyses were carried out to investigate BTF3 mRNA/protein expression and localization. BTF3 silencing in pancreatic cancer cells was performed using specific siRNA molecules. Functional analyses were carried out using cell growth assays, apoptosis assays, and DNA array analysis. BTF3 and BTF3a exhibited 1.3-fold and 4.6-fold increased median mRNA levels in PDAC tissues, compared to normal pancreatic tissues. BTF3 localized mainly in the cytoplasm and nuclei of tubular complexes and pancreatic cancer cells. Pancreatic cancer cell lines expressed the mRNA and protein of BTF3a (27 kDa) and BTF3b (22 kDa) isoforms. BTF3 silencing using specific siRNA molecules did not influence apoptosis induced by chemotherapy or radiotherapy. In contrast, BTF3 silencing resulted in down-regulation of several cancer-associated genes, including EPHB2, ABL2, HPSE2 and ATM, and up-regulation of KRAG, RRAS2, NFk-B, MRVI1, MADCAM1 and others. In conclusion, BTF3 is overexpressed in PDAC, where it acts as a transcriptional regulator rather than a direct modulator of apoptosis.

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Coamplification in Tumors ofKRAS2,Type 2 Inositol 1,4,5 Triphosphate Receptor Gene, and a Novel Human Gene,KRAG

Cited by 31 publications

References 1 publication

Oncogenic K-Ras suppresses IP3-dependent Ca2+ release through remodeling of IP3Rs isoform composition and ER luminal Ca2+ levels in colorectal cancer cell lines

Oncogenic K-Ras suppresses IP3-dependent Ca2+ release through remodeling of IP3Rs isoform composition and ER luminal Ca2+ levels in colorectal cancer cell lines

Sarcospan, the 25-kDa Transmembrane Component of the Dystrophin-Glycoprotein Complex

Basic transcription factor 3 (BTF3) regulates transcription of tumor-associated genes in pancreatic cancer cells

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