tryptophan/vefjadrep

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Inhibition of tumor necrosis factor-induced cell killing by tryptophan and indole.

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Cells sensitive to the cytocidal effect of tumor necrosis factor (TNF) were protected against this effect when growth in the presence of elevated concentrations of tryptophan. Several other indole derivatives also provided protection against TNF cytotoxicity. Most effective were indole itself and

Reversion of the antichlamydial effect of tumor necrosis factor by tryptophan and antibodies to beta interferon.

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Human recombinant tumor necrosis factor-alpha (TNF-alpha) inhibited the growth of Chlamydia trachomatis (L2/434/Bu) in HEp-2 cells. The effect was synergistic with that of gamma interferon (IFN-gamma). TNF-induced resistance to chlamydiae could be blocked with cycloheximide, suggesting that it

Tryptophan protects human melanoma cells against gamma-interferon and tumour necrosis factor-alpha: a unifying mechanism of action.

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The sensitivity and resistance of six human melanoma cell lines to gamma-interferon (gamma-IFN) and tumour necrosis factor-alpha (TNF-alpha) have been examined. Amelanotic cell lines were more sensitive to gamma-IFN and TNF-alpha than melanotic cells. The cytotoxicity of gamma-IFN and TNF-alpha

Tryptophan potentiation of the late cysteine preventive effects in carbon tetrachloride-induced necrosis.

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Carbon tetrachloride (CCl4) (1 ml/kg/ip) induces a very intense necrotic effect on rat liver at 24 hr after administration. Cysteine (950 mg/kg/po) given 6 h after CCl4 exerted a very weak preventive effect on CCl4-induced necrosis, while tryptophan (300 mg/kg/po) did not. When both aminoacids are

Mouse tumor necrosis factor-alpha increases brain tryptophan concentrations and norepinephrine metabolism while activating the HPA axis in mice.

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Endotoxin (LPS) administration has been shown to activate the hypothalamo-pituitary-adrenocortical (HPA) axis and increase cerebral catecholamine and indolamine metabolism and tryptophan concentrations. LPS stimulates the secretion of tumor necrosis factor-alpha (TNF-alpha) as well as interleukin-1

Two conserved tryptophan residues of tumor necrosis factor and lymphotoxin are not involved in the biological activity.

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Each of the two highly conserved tryptophan residues in hTNF (positions 28 and 114) was converted into phenylalanine by site-directed mutagenesis and the mutant proteins were partially purified. A cytotoxicity assay on mouse L929 cells showed only a slight reduction in biological activity, strongly

Tumour necrosis factor-alpha and lipopolysaccharide enhance interferon-induced tryptophan degradation and pteridine synthesis in human cells.

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The capacity of recombinant interferon-alpha, -beta and -gamma, of bacterial lipopolysaccharide and of recombinant tumour necrosis factor-alpha to induce indoleamine 2,3-dioxygenase and synthesis of pteridines was studied in human peripheral blood mononuclear cells, human macrophages and normal

Dietary tryptophan modulates intestinal immune response, barrier function, antioxidant status and gene expression of TOR and Nrf2 in young grass carp (Ctenopharyngodon idella).

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The present research evaluated the effects of dietary tryptophan (Trp) on growth performance, intestinal mucosal immune, barrier function and antioxidant capacity and gene expression of young grass carp (Ctenopharyngodon idella). Fish were fed six different experimental diets containing graded

Immunomodulatory effects of Turkish propolis: changes in neopterin release and tryptophan degradation.

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In most of the diseases which are considered to benefit from propolis, cellular immune reaction is activated, neopterin levels in body fluids are increased and enhanced tryptophan degradation is observed. In this study, the immunomodulatory effects of six Turkish propolis samples were evaluated by

Dynamic physiological and molecular changes in gastric ulcer healing achieved by melatonin and its precursor L-tryptophan in rats.

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Following induction of gastric ulcer in rats by serosal application of acetic acid, local mucosal necrosis ensues accompanied by a reduction in mucosal microcirculation and by almost immediate expression of inducible nitric oxide (NO) synthase (iNOS) and proinflammatory cytokines. Daily application

Possible role of cytokine-induced tryptophan degradation in anaemia of inflammation.

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Anaemia of inflammation (AI) is a frequent complication in patients suffering from chronic inflammatory disorders including infections, autoimmune and malignant disease. Cytokine imbalance with a shift towards T-helper (Th)1-type immune response seems to be important in the pathogenesis of this type

Association of human tumor necrosis factor-related apoptosis inducing ligand with membrane upon acidification.

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Tumor necrosis factor (TNF)-related apoptosis inducing ligand (TRAIL) has been known to induce tumor-specific apoptosis and to share the structural and functional characteristics with the proteins of TNF family. Recently, the crystal structure of human TRAIL showed that TRAIL is a homotrimeric

A synthetic tryptophan metabolite reduces hemorrhagic area and inflammation after pulmonary radiofrequency ablation in rabbit nonneoplastic lungs.

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OBJECTIVE The purpose of this study was to determine the effect of a synthetic tryptophan metabolite, tranilast [N-(3,4-dimethoxycinnamoyl)-anthranilic acid], on inflammatory and hemorrhagic areas after pulmonary radiofrequency ablation (RFA) in rabbits. METHODS Percutaneous RFA using a 17-gauge

Values of Cytokines and Tryptophan Metabolites over a 12 Weeks Time Course in Patients with Depression and Somatoform Disorder.

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Previous studies have suggested alterations in the kynurenine pathway as a major link between cytokine and neurotransmitter abnormalities in psychiatric disorders. Most of these studies used a cross-sectional case-control study design. However, knowledge is still lacking regarding the

NF-kappa B activation contributes to indoleamine dioxygenase transcriptional synergy induced by IFN-gamma and tumor necrosis factor-alpha.

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Interferon (IFN)-gamma-induced expression of indoleamine 2,3-dioxygenase (IDO), an enzyme that inhibits some pathogens by limiting tryptophan availability, is transcriptionally enhanced by tumor necrosis factor (TNF)-alpha. The expression of interferon responsive factor (IRF)-1, an IFN-gamma-induced

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