A Method for Analysis of Gene Expression Patterns

Chalifour, Lorraine E.; Fahmy, Roger G.; Holder, Emma; Hutchinson, E. W.; Osterland, C. K.; Schipper, H.; Wang, E.

doi:10.1006/abio.1994.1045

Cited by 35 publications

(17 citation statements)

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“…Siot Bot hybridization rnRNA levels were assessed using a novel. slot-blot hybridization assay developed by Chalifour et al (1994). This method involved 5 steps: 1) generation of the flIst strand cDNA.…”

Section: Gel Electrophoresis and Immunoblottingmentioning

confidence: 99%

“…During the formation of semiquinones, neurotoxic superoxide anion and H 2 0 2 are also generated (Kalyanaraman et al, 1984(Kalyanaraman et al, , 1985. In support of this free radical hypothesis of hypothalamic damage, it has been shown that dietary supplementation with the potent antioxidants a-tocopherol (Desjardins et al, 1992) or 21-aminosleroids (Schipper et al, 1994) reduces EV-induced damage to the arcuate nucleus. As in the case of the peripheral sex steroid target tissues, many periventricular glia contain estrogen receptors (Lee, 1982;Stopa et al, 1989;Langub and Watson, 1992).…”

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confidence: 99%

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Differential effects of cysteamine on heat shock protein induction and cytoplasmic granulation in astrocytes and glioma cells

Chopra¹,

Chalifour²,

Schipper³

1995

Molecular Brain Research

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Section: Gel Electrophoresis and Immunoblottingmentioning

confidence: 99%

mentioning

confidence: 99%

Differential effects of cysteamine on heat shock protein induction and cytoplasmic granulation in astrocytes and glioma cells

Chopra¹,

Chalifour²,

Schipper³

1995

Molecular Brain Research

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“…In the present study, we tried to identify the gene that is involved in b-HIVS-induced apoptosis to clarify the molecular mechanisms of apoptosis. Gene-expression arrays have recently been developed as highly effective tools for the profiling of gene expression (Chalifour et al, 1994;Schena et al, 1995), and we used such arrays in our search for apoptosis-promoting genes whose expression is regulated by b-HIVS. Our analysis indicated that expression of a gene for a polo-like kinase 1 (PLK1) was significantly suppressed by b-HIVS in U937 and HL60 cells.…”

Section: Introductionmentioning

confidence: 99%

β-Hydroxyisovalerylshikonin induces apoptosis in human leukemia cells by inhibiting the activity of a polo-like kinase 1 (PLK1)

et al. 2003

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b-Hydroxyisovalerylshikonin (b-HIVS), which was isolated from the plant, Lithospermum radix, induces apoptosis in various lines of human tumor cells. To identify genes involved in b-HIVS-induced apoptotic process, we performed cDNA array analysis and found that b-HIVS suppresses the expression of the gene for a polo-like kinase 1 (PLK1) that is involved in control of the cell cycle. When U937 and HL60 cells were treated with 10 À6 m b-HIVS for 0.5 h, both the amount of PLK1 itself and the kinase activity of this enzyme were decreased. By contrast, Bcr-Abl-positive K562 cells were resistant to the induction of apoptosis by b-HIVS and this compound did not suppress the kinase activity of PLK1 in these cells. However, simultaneous treatment of K562 cells with both b-HIVS and STI571, which selectively inhibits the protein tyrosine kinase (PTK) activity of Bcr-Abl, strongly induced apoptosis. Moreover, b-HIVS increased the inhibitory effect of STI571 on PTK activity. Treatment of K562 cells with antisense oligodeoxynucleotides (ODNs) specific for PLK1 sensitized these cells to the b-HIVS-induced fragmentation of DNA. These results suggest that suppression of the activity of PLK1 via inhibition of tyrosine kinase activity by b-HIVS might play a critical role in the induction of apoptosis.

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“…Cultures of Synechocystis sp. strain PCC 6803 that had been exposed to a variety of nutritional and environmental conditions (Table 1) were surveyed for the presence of mRNA encoding SynPPP1 or SynPPM3 using an adaptation of the array technique of Chalifour et al (6). As can be seen in Fig.…”

Section: Resultsmentioning

confidence: 99%

“…The levels of mRNA derived from ORFs sll1033 and sll1387 were determined by the array method of Chalifour et al (6). Briefly, oligonucleotide probes, ϳ400 to 600 nucleotides in length, were prepared by PCR amplification of genomic DNA.…”

Section: Materials Purchased Materials Included [␥-mentioning

confidence: 99%

The Protein Phosphatases of Synechocystis sp. Strain PCC 6803: Open Reading Frames sll1033 and sll1387 Encode Enzymes That Exhibit both Protein-Serine and Protein-Tyrosine Phosphatase Activity In Vitro

Potters

Shi

et al. 2005

J Bacteriol

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The open reading frames (ORFs) encoding two potential protein-serine/threonine phosphatases from the cyanobacterium Synechocystis sp. strain PCC 6803 were cloned and their protein products expressed in Escherichia coli cells. The product of ORF sll1033, SynPPM3, is a homologue of the PPM family of proteinserine/threonine phosphatases found in all eukaryotes as well as many members of the Bacteria. Surprisingly, the recombinant protein phosphatase dephosphorylated phosphotyrosine-as well as phosphoserine-containing proteins in vitro. While kinetic analyses indicate that the enzyme was more efficient at dephosphorylating the latter, replacement of Asp 608 by asparagine enhanced activity toward a phosphotyrosine-containing protein fourfold. The product of ORF sll1387, SynPPP1, is the sole homolog of the PPP family of protein phosphatases encoded by the genome of Synechocystis sp. strain PCC 6803. Like many other bacterial PPPs, the enzyme dephosphorylated phosphoserine-and phosphotyrosine-containing proteins with comparable efficiencies. However, while previously described PPPs from prokaryotic organisms required the addition of exogenous metal ion cofactors, such as Mg 2؉ or Mn 2؉, for activity, recombinantly produced SynPPP1 displayed near-maximal activity in the absence of added metals. Inductively coupled plasma mass spectrometry indicated that recombinant SynPPP1 contained significant quantities, 0.32 to 0.44 mol/mole total, of Mg and Mn. In this respect, the cyanobacterial enzyme resembled eukaryotic members of the PPP family, which are metalloproteins. mRNA encoding SynPPP1 or SynPPM3 could be detected in cells grown under many, but not all, environmental conditions.Examination of the current library of genome sequences indicates that many bacteria possess open reading frames (ORFs) encoding known or potential protein-serine/threonine/ tyrosine kinases and phosphatases (30,46,49). However, our current body of knowledge concerning the functional properties and physiologic roles of these enzymes remains disappointingly fragmentary (23). The genome of the cyanobacterium Synechocystis sp. strain PCC 6803 (22), for example, encodes 15 potential protein-serine/threonine/tyrosine kinases and 12 potential protein-serine/threonine/tyrosine phosphatases (46, 49). However, the catalytic capabilities of only nine of these deduced intermediaries of signal transduction, one-third of the total, have been experimentally assessed to date. Intriguingly, while all six of the predicted protein kinases characterized thus far displayed the ability to phosphorylate themselves and/or exogenous proteins in vitro (19-21, 26, 45), only two of the three potential protein phosphatases behaved as initially predicted. Specifically, while the PPM family protein phosphatases PphA (16,41) and IcfG (SynPPM1) (45) exhibited robust protein phosphatase activity, the product of ORF slr0946, initially annotated as a low-molecular-weight protein-tyrosine phosphatase, was discovered to be an arsenate reductase (33).The predominant source of protein-...

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A Method for Analysis of Gene Expression Patterns

Cited by 35 publications

References 0 publications

Differential effects of cysteamine on heat shock protein induction and cytoplasmic granulation in astrocytes and glioma cells

Differential effects of cysteamine on heat shock protein induction and cytoplasmic granulation in astrocytes and glioma cells

β-Hydroxyisovalerylshikonin induces apoptosis in human leukemia cells by inhibiting the activity of a polo-like kinase 1 (PLK1)

The Protein Phosphatases of Synechocystis sp. Strain PCC 6803: Open Reading Frames sll1033 and sll1387 Encode Enzymes That Exhibit both Protein-Serine and Protein-Tyrosine Phosphatase Activity In Vitro

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