Estimating the Burden of T-Cell Lymphoma among Hispanic and Rural Patients

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A Lateral Flow Assay for Quantitative Detection of Amplified HIV-1 RNA

Although the accessibility of HIV treatment in developing nations has increased dramatically over the past decade, viral load testing to monitor the response of patients receiving therapy is often unavailable. Existing viral load technologies are often too expensive or resource-intensive for poor settings, and there is no appropriate HIV viral load test currently available at the point-of-care in low resource settings. Here, we present a lateral flow assay that employs gold nanoparticle probes and gold enhancement solution to detect amplified HIV RNA quantitatively. Preliminary results show that, when coupled with nucleic acid sequence based amplification (NASBA), this assay can detect concentrations of HIV RNA that match the clinically relevant range of viral loads found in HIV patients. The lateral flow test is inexpensive, simple and rapid to perform, and requires few resources. Our results suggest that the lateral flow assay may be integrated with amplification and sample preparation technologies to serve as an HIV viral load test for low-resource settings

Tumor Necrosis Factor Receptor–Associated Factor (Traf)2 Represses the T Helper Cell Type 2 Response through Interaction with Nfat-Interacting Protein (Nip45)

Recently we have identified a novel protein NIP45 (nuclear factor of activated T cells [NFAT]-interacting protein) which substantially augments interleukin (IL)-4 gene transcription. The provision of NIP45 together with NFAT and the T helper cell type 2 (Th2)-specific transcription factor c-Maf to cells normally refractory to IL-4 production, such as B cells or Th1 clones, results in substantial IL-4 secretion to levels that approximate those produced by primary Th2 cells. In studies designed to further our understanding of NIP45 activity, we have uncovered a novel facet of IL-4 gene regulation. We present evidence that members of the tumor necrosis factor receptor–associated factor (TRAF) family of proteins, generally known to function as adapter proteins that transduce signals from the tumor necrosis factor receptor superfamily, contribute to the repression of IL-4 gene transcription and that this effect is mediated through their interaction with NIP45

Regulation of heme oxygenase-1 mRNA deadenylation and turnover in NIH3T3 cells by nitrosative or alkylation stress-6

<p><b>Copyright information:</b></p><p>Taken from "Regulation of heme oxygenase-1 mRNA deadenylation and turnover in NIH3T3 cells by nitrosative or alkylation stress"</p><p>http://www.biomedcentral.com/1471-2199/8/116</p><p>BMC Molecular Biology 2007;8():116-116.</p><p>Published online 20 Dec 2007</p><p>PMCID:PMC2246143.</p><p></p>transcription and total RNA was extracted at the indicated times. HO-1 mRNA expression was monitored by northern blotting and normalized to GAPDH expression. The same blot was also probed for the expression of unstable CL100 mRNA.. Quantification shows the fitted decay lines, calculated from three independent experiments. Data points show the mean and standard errors. * p < 0.05 as compared the HO-1 mRNA remaining (% of initial) in untreated controls at the corresponding times. . NIH3T3 cells were treated with the indicated concentrations of DETA/NO for 6 h prior to the addition of AD, and the percentage of HO-1 mRNA remaining was quantified at the indicated time points.. Quantification shows the fitted decay lines, calculated from two independent experiments. Data points show the mean and standard errors. . In parallel experiments, cells were trypsinized immediately after the treatment or at 8 h and 24 h after treatment, followed by trypan blue staining. To estimate viability, the values were normalized to 100% at time 0 h in untreated controls. Quantification in panel E shows the mean and standard error of three independent experiments, except for 0.5 mM dose, which corresponds to one experiment. ** p < 0.01, * p < 0.05 as compared to untreated controls at the corresponding times

Regulation of heme oxygenase-1 mRNA deadenylation and turnover in NIH3T3 cells by nitrosative or alkylation stress-5

<p><b>Copyright information:</b></p><p>Taken from "Regulation of heme oxygenase-1 mRNA deadenylation and turnover in NIH3T3 cells by nitrosative or alkylation stress"</p><p>http://www.biomedcentral.com/1471-2199/8/116</p><p>BMC Molecular Biology 2007;8():116-116.</p><p>Published online 20 Dec 2007</p><p>PMCID:PMC2246143.</p><p></p>ylation. Residual full-length mRNA and the 3' end fragment carrying the poly(A) tail are indicated. FD represents the fully deadenylated 3' fragment of HO-1 mRNA. . The size of the poly(A) tail was estimated as for Fig. 5. . A fraction of the samples was used without further modification to assess the half-life of HO-1 mRNA. Quantification in panels B and C shows the fitted decay lines calculated from two independent experiments. Data points show the mean and standard errors

Regulation of heme oxygenase-1 mRNA deadenylation and turnover in NIH3T3 cells by nitrosative or alkylation stress-3

<p><b>Copyright information:</b></p><p>Taken from "Regulation of heme oxygenase-1 mRNA deadenylation and turnover in NIH3T3 cells by nitrosative or alkylation stress"</p><p>http://www.biomedcentral.com/1471-2199/8/116</p><p>BMC Molecular Biology 2007;8():116-116.</p><p>Published online 20 Dec 2007</p><p>PMCID:PMC2246143.</p><p></p> To compensate for the differences in the starting amount of HO-1 mRNA between control and NO-treated cells where HO-1 mRNA is induced immediately after the SPER/NO treatment, 35 μg and 6 μg of total mRNA were used in a cleavage reaction from untreated controls and NO-treated samples, respectively. Residual full-length HO-1 mRNA and the 3' end fragment carrying the poly(A) tail are indicated. FD represents HO-1 mRNA that was fully deadenylated . . The upper boundary of the mRNA was set at a position below which 95–97% of the total HO-1 mRNA band area was included. The size of the poly(A) tail was estimated by comparing the migration of the upper bound to that of the FD (522-nt) and 623-nt size markers. . A fraction of the samples was used without further modification to assess the half-life of HO-1 mRNA by northern blotting. Quantification in panels B and C shows the fitted decay lines calculated from two independent experiments. Data points show the mean and standard errors

Regulation of heme oxygenase-1 mRNA deadenylation and turnover in NIH3T3 cells by nitrosative or alkylation stress-2

<p><b>Copyright information:</b></p><p>Taken from "Regulation of heme oxygenase-1 mRNA deadenylation and turnover in NIH3T3 cells by nitrosative or alkylation stress"</p><p>http://www.biomedcentral.com/1471-2199/8/116</p><p>BMC Molecular Biology 2007;8():116-116.</p><p>Published online 20 Dec 2007</p><p>PMCID:PMC2246143.</p><p></p>ction at the indicated time points. HO-1 mRNA was detected by northern blotting and normalized to GAPDH loading controls.. For each concentration in panel A, the fitted decay lines were calculated using data from three independent experiments and plotted. Data points show the mean and standard errors. . In parallel experiments viable cells (trypan blue-negative) were counted immediately after the treatment (time 0 h) and at 8 h and 24 h after treatment. The percentage of viable cells shown is relative to 100% cell number at time 0 h in untreated controls. The graph shows the mean and standard error of three independent experiments. * p < 0.05 as compared to untreated controls at the corresponding times

Regulation of heme oxygenase-1 mRNA deadenylation and turnover in NIH3T3 cells by nitrosative or alkylation stress-4

<p><b>Copyright information:</b></p><p>Taken from "Regulation of heme oxygenase-1 mRNA deadenylation and turnover in NIH3T3 cells by nitrosative or alkylation stress"</p><p>http://www.biomedcentral.com/1471-2199/8/116</p><p>BMC Molecular Biology 2007;8():116-116.</p><p>Published online 20 Dec 2007</p><p>PMCID:PMC2246143.</p><p></p>tively) were assayed for HO-1 mRNA deadenylation. Residual full-length mRNA and the 3' end fragment carrying the poly(A) tail are indicated. FD represents a fully deadenylated 3' fragment of HO-1 mRNA. . The size of the poly(A) tail was estimated as for Fig. 5. . A fraction of these samples was used without further modification to assess the half-life of HO-1 mRNA. Quantification in panels B and C shows the fitted decay lines calculated from two independent experiments. Data points show the mean and standard errors

Regulation of heme oxygenase-1 mRNA deadenylation and turnover in NIH3T3 cells by nitrosative or alkylation stress-0

<p><b>Copyright information:</b></p><p>Taken from "Regulation of heme oxygenase-1 mRNA deadenylation and turnover in NIH3T3 cells by nitrosative or alkylation stress"</p><p>http://www.biomedcentral.com/1471-2199/8/116</p><p>BMC Molecular Biology 2007;8():116-116.</p><p>Published online 20 Dec 2007</p><p>PMCID:PMC2246143.</p><p></p>transcription and total RNA was extracted at the indicated times. HO-1 mRNA expression was monitored by northern blotting and normalized to GAPDH expression. The same blot was also probed for the expression of unstable CL100 mRNA.. Quantification shows the fitted decay lines, calculated from three independent experiments. Data points show the mean and standard errors. * p < 0.05 as compared the HO-1 mRNA remaining (% of initial) in untreated controls at the corresponding times. . NIH3T3 cells were treated with the indicated concentrations of DETA/NO for 6 h prior to the addition of AD, and the percentage of HO-1 mRNA remaining was quantified at the indicated time points.. Quantification shows the fitted decay lines, calculated from two independent experiments. Data points show the mean and standard errors. . In parallel experiments, cells were trypsinized immediately after the treatment or at 8 h and 24 h after treatment, followed by trypan blue staining. To estimate viability, the values were normalized to 100% at time 0 h in untreated controls. Quantification in panel E shows the mean and standard error of three independent experiments, except for 0.5 mM dose, which corresponds to one experiment. ** p < 0.01, * p < 0.05 as compared to untreated controls at the corresponding times