An improved colorimetric assay for cell proliferation and viability utilizing the tetrazolium salt XTT

Roehm, Neal W.; Rodgers, George H.; Hatfield, Stephen; Glasebrook, Andrew L.

doi:10.1016/0022-1759(91)90114-u

Cited by 907 publications

(584 citation statements)

References 10 publications

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“…17 The cytotoxicity against MonoMac6 cells was determined in an 2,3-bis(2-methoxy-4-nitro-5-sulfophenyl)-2H-tetrazolium-5-carboxanilide sodium-based cell viability assay. 18 The 972-bp human CXCL10 promoter (À875 to +97 relative to the transcription start site) was cloned into the pGL4 basic vector (Promega, Mannheim, Germany) to generate the hCXCL10 promoter-driven luciferase reporter plasmid. The plasmid pRL-EF1a for normalizing transfection efficiency was obtained from Promega.…”

Section: Biological Assaysmentioning

confidence: 99%

Ganodermycin, a novel inhibitor of CXCL10 expression from Ganoderma applanatum

et al. 2011

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CXCL10 (inducible protein-10) is a highly inducible chemoattractant, which contributes to the recruitment of inflammatory cells, such as macrophages and T-lymphocytes, and thereby has important roles in chronic inflammatory conditions. In a search for new inhibitors of CXCL10 expression in MonoMac6 cells, a novel compound, designated as Ganodermycin, was isolated from fermentations of the basidiomycete Ganoderma applanatum. The structure was determined by a combination of spectroscopic techniques. Ganodermycin inhibited the lipopolysaccharide (LPS)/interferon (IFN)-c-induced CXCL10 promoter activity in transiently transfected MonoMac6 cells in a dose-dependent manner with IC 50 values of 15-20 lg ml À1 (53-71 lM). Ganodermycin also reduced LPS/IFN-c-induced CXCL10 protein synthesis and excretion.

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Section: Biological Assaysmentioning

confidence: 99%

Ganodermycin, a novel inhibitor of CXCL10 expression from Ganoderma applanatum

et al. 2011

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“…31 Cells were plated in 96-well microtiter plates at densities of 2 Â 10 3 -6 Â 10 3 cells per well in 100 ml of medium. At 24 h after the cells were plated, 50-ml aliquots of medium containing varying concentrations of Ad-PTEN or Ad-Luc were added to each well, or cells were exposed to varying doses of IR after 30 minutes of exposure to 100-ml aliquots of medium containing varying concentrations of caffeine.…”

Section: Xtt Assaymentioning

confidence: 99%

Adenovirus-mediated PTEN treatment combined with caffeine produces a synergistic therapeutic effect in colorectal cancer cells

et al. 2003

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The tumor suppressor phosphatase and tensin homologue deleted from chromosome 10 (PTEN) gene is a negative regulator of the phosphatidylinositol-3-kinase (PI3K)/protein kinase B (Akt/PKB) signaling pathway. Overexpression of PTEN in cancer cells results in cell-cycle arrest and cell death through inhibition of PI3K. Caffeine, a xanthine analogue, is well known to enhance the cytocidal and growth-inhibitory effects of DNA-damaging agents such as radiation, UV light, and anticancer agents on tumor cells by abrogating DNA-damage checkpoints through inhibition of ataxia-telangiectasia-mutated (ATM), and ATM and Rad3-related (ATR) kinase activity. In this study, we demonstrate that treatment with a combination of adenovirus-mediated transfer of PTEN (Ad-PTEN) and caffeine synergistically suppressed cell growth and induced apoptosis in colorectal cancer cells but not in normal colorectal fibroblast cells. This synergistic effect was induced through abrogation of G 2 /M arrest, downregulation of the Akt pathway, and modulation of the p44/42MAPK pathway. Thus, combined treatment with Ad-PTEN and caffeine is a potential therapy for colorectal cancer.

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“…The migration responses to LN were tested with controls in the same assay. After an incubation of 3 hours at 37˚C in a humidified 5% CO 2 atmosphere, the number of cells that migrated through the filter into lower wells was quantified with a non-radioactive, colorimetric assay system using XTT (Roche) (Roehm et al, 1991). XTT with phenazine methosulfate (PMS) was added in each well after removal of inserts and incubated for 5 hours at 37˚C.…”

Section: In Vitro Cell Migration Assaysmentioning

confidence: 99%

Laminin-1-induced migration of multiple myeloma cells involves the high-affinity 67 kD laminin receptor

Broek¹,

Vanderkerken²,

Greef³

et al. 2001

Br J Cancer

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SummaryThe 67 kD laminin receptor (67LR) binds laminin-1 (LN), major component of the basement membrane, with high affinity. In this study, we demonstrated that human multiple myeloma cell lines (HMCL) and murine 5T2MM cells express 67LR. CD38 bright+ plasma cells in fresh multiple myeloma (MM) bone marrow (BM) samples showed weaker 67LR expression, but expression increased after direct exposure to a BM endothelial cell line (4LHBMEC). LN stimulated the in vitro migration of 3 HMCL (MM5.1, U266 and MMS.1), primary MM cells and the murine 5T2MM cells. 67LR has been shown to mediate the actions of LN through binding to CDPGYIGSR, a 9 amino acid sequence from the B1 chain of LN. MM cell migration was partially blocked by peptide 11, a synthetic nonapeptide derived from this amino sequence and also by a blocking antiserum against 67LR. Co-injection of peptide 11 with 5T2MM cells in a murine in vivo model of MM resulted in a decreased homing of 5T2MM cells to the BM compartment. In conclusion, LN acts as a chemoattractant for MM cells by interaction with 67LR. This interaction might be important during extravasation of circulating MM cells.

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An improved colorimetric assay for cell proliferation and viability utilizing the tetrazolium salt XTT

Cited by 907 publications

References 10 publications

Ganodermycin, a novel inhibitor of CXCL10 expression from Ganoderma applanatum

Ganodermycin, a novel inhibitor of CXCL10 expression from Ganoderma applanatum

Adenovirus-mediated PTEN treatment combined with caffeine produces a synergistic therapeutic effect in colorectal cancer cells

Laminin-1-induced migration of multiple myeloma cells involves the high-affinity 67 kD laminin receptor

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