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PubMed2001

Decomposition of protein tryptophan fluorescence spectra into log-normal components. III. Correlation between fluorescence and microenvironment parameters of individual tryptophan residues.

In our previous paper (Reshetnyak, Ya. K., and E. A. Burstein. 2001. Biophys. J. 81:1710-1734) we confirmed the existence of five statistically discrete classes of emitting tryptophan fluorophores in proteins. The differences in fluorescence properties of tryptophan residues of these five classes reflect differences in interactions of excited states of tryptophan fluorophores with their microenvironment in proteins. Here we present a system of describing physical and structural parameters of microenvironments of tryptophan residues based on analysis of atomic crystal structures of proteins. The application of multidimensional statistical methods of cluster and discriminant analyses for the set of microenvironment parameters of 137 tryptophan residues of 48 proteins with known three-dimensional structures allowed us to 1) demonstrate the discrete nature of ensembles of structural parameters of tryptophan residues in proteins; 2) assign spectral components obtained after decomposition of tryptophan fluorescence spectra to individual tryptophan residues; 3) find a correlation between spectroscopic and physico-structural features of the microenvironment; and 4) reveal differences in structural and physical parameters of the microenvironment of tryptophan residues belonging to various spectral classes.

Analysis of Variance↗

PubMed1997

Mouse strain and source of L-tryptophan affects hepatic nuclear tryptophan binding.

This study describes that the affinity for specific L-tryptophan binding to hepatic nuclei in vitro is markedly decreased in NZBWF1 mice in comparison to that in Swiss mice. Also, the hepatic nuclei of NZBWF1 mice have a significantly decreased binding response in vitro to Showa Denko L-tryptophan (implicated in the eosinophilia-myalgia syndrome) or to its contaminants, 1,1'-ethylidenebis(tryptophan) or 3-phenylamino-L-alanine, when each is added to control, non-implicated L-tryptophan compared with hepatic nuclei of Swiss mice. Enhanced hepatic protein synthesis induced by tube-feeding control L-tryptophan is much less in NZBWF1 mice than in Swiss mice. Tube-feeding of Showa Denko L-tryptophan induced less stimulation of hepatic protein synthesis than did control L-tryptophan in Swiss mice but essentially none in NZBWF1 mice. NZBWF1 mice have a genetically altered response to L-tryptophan which may prove to be useful is studying the role of L-tryptophan in health and in disease.

Alanine↗

PubMed2001

Influence of tryptophan supplementation of soy-based infant formulas on protein quality and on blood and brain tryptophan and brain serotonin in the rat model.

A 2-wk feeding study with weanling rats was conducted to investigate the effects of tryptophan supplementation of soy-based infant formulas on protein quality and on the levels of blood and brain tryptophan and brain serotonin and 5-HIAA (5-hydroxyindole-3-acetic acid), a metabolite of serotonin. The powder and liquid concentrate forms of soy-based infant formulas obtained from four manufacturers were tested. The tryptophan contents of the test soy-based formulas (10.0-12.3 mg/g protein) were considerably lower compared to those of human milk (17-19 mg/g protein). The infant formulas were fed as the sole source of protein in diets containing 8% protein, 20% fat, 5% cellulose and adequate amounts of minerals and vitamins. In general, supplementation of the diets containing test formulas with graded levels of L-tryptophan (0.1 or 0.2%) had no effect on protein quality indices based on rat growth such as PER (protein efficiency ratio), NPR (net protein ratio) and relative NPR (RNPR), but resulted in significant (p < 0.05) increases in the concentrations of tryptophan in the plasma and brain, and serotonin and 5-HIAA in brain of rats. The increased concentrations of brain tryptophan and 5-hydroxyindoles (serotonin + 5-HIAA) in rats fed tryptophan-supplemented formulas compared to those fed unsupplemented formulas support the need for further research to investigate the influence of tryptophan supplementation of soy-based infant formulas on tryptophan metabolites and their potential related effects on sleep latency and neurobehavioral developments in infants.

Animals↗

PubMed2003

Total plasma l-tryptophan, free l-tryptophan and competing amino acid levels in a homicidal male adolescent with conduct disorder.

OBJECTIVE: Several studies have shown abnormal findings in human serotonin metabolism, such as increased total plasma l-tryptophan and free l-tryptophan levels among habitually violent antisocial offenders. It is not clear if these increased l-tryptophan levels are associated with adult antisocial personality disorder (ASP) or history of substance abuse, or if these levels are already present in adolescent subjects with conduct disorder (CD). METHOD: Total plasma and free l-tryptophan and competing amino acids (CAAs) were measured in a 15-year-old adolescent offender, who was convicted for two homicides, and in 10 healthy male controls of similar age and body mass index (BMI). RESULTS: In the juvenile offender, plasma total l-tryptophan/CAA was 84% and free l-tryptophan/CAA 143% higher than average mean among controls. CONCLUSION: From this very aggressive boy with CD, findings of free l- and total l-tryptophan/CAA values were similar to those of habitually violent adult ASP offenders. As severe CDs in adolescence tend to develop into adults with ASP, increased l-tryptophan/CAA and free l-tryptophan/CAA values may serve as early indicators for the development of habitually violent adult offenders.

Adolescent↗

PubMed1997

Tryptophan and carcinogenesis: review and update on how tryptophan may act.

This review covers the historical developments of the consideration that tryptophan may influence the induction of cancer in experimental studies. Studies relating to stimulatory effects, as well as to inhibitory effects, of tryptophan or tryptophan-related compounds are described. Also the effects of pyrolysis products of tryptophan on carcinogenesis are covered. In consideration that new L-tryptophan-related contaminants may be involved in a recently described human disease, a description is given of the eosinophilia-myalgia syndrome, which has been attributed to the ingestion of L-tryptophan-containing related contaminants. Whether these new L-tryptophan-related contaminants alone or together with L-tryptophan may prove to be carcinogenic remains to be determined. Lastly, recent developments relating to regulatory effects of L-tryptophan on liver metabolism are reviewed and then considered as possibly playing a role in carcinogenesis.

Animals↗

PubMed1987

States of tryptophan residues in castor bean hemagglutinin: the perturbing effects of solvents on tryptophans in hemagglutinin and its complexes as analyzed by UV-difference spectroscopy.

The states of tryptophan residues in castor bean hemagglutinin (CBH) were analyzed by solvent perturbation studies employing ultraviolet difference spectroscopy. Eight out of 22 tryptophan residues in CBH were exposed to ethylene glycol and glycerol, suggesting that the remaining 14 tryptophan residues are buried in the interior of the CBH molecule. The fraction of tryptophan residues accessible to the perturbant decreased with increase in the molecular size of the perturbant, and only 2 tryptophan residues were exposed to polyethylene glycol 600. Upon binding with raffinose, 2 tryptophan residues were shielded from the perturbing effect of the solvent, and binding of lactose reduced the number of tryptophan residues accessible to the perturbant by 1 mol per mol of protein. Binding of galactose, however, did not change the accessibility of tryptophan to the perturbant. On the other hand, the accessibility of tyrosine to the perturbant remained unchanged after binding with raffinose and lactose, suggesting that tyrosine is not directly involved in the saccharide binding of CBH. Based on these results, it is proposed that one tryptophan residue at the saccharide-binding site on each B-chain of CBH lies on the surface of the protein molecule and is located at a subsite which is accessible to a glucopyranoside moiety in the lactose molecule or a glycopyranosyl-fructofuranosyl moiety in the raffinose molecule, whereas such a residue is not present at the galactopyranoside-recognition site.

Lectins↗

PubMed1985

Increased total activity in the rat after L-tryptophan plus the monoamine oxidase-A inhibitor amiflamine but not after L-tryptophan plus clorgyline.

The effect of pretreatment with either saline or the monoamine oxidase-A inhibitors clorgyline and amiflamine upon the total activity, locomotion and rearing behaviour of the rat induced by various doses of the monoamine precursor L-tryptophan was studied by use of automated activity boxes. Amiflamine (2.5 and 5.0 mg kg-1, i.p.) increased in a dose-dependent manner total activity and to a lesser extent, locomotion when given 60 min before L-tryptophan (100 mg kg-1, i.p.). The increased activity was seen after amiflamine plus either 25 or 75 mg kg-1 L-tryptophan. Rearing behaviour was not affected. Analysis of 5-hydroxytryptamine (5-HT) and its deaminated metabolite 5-hydroxyindoleacetic acid (5-HIAA) by high performance liquid chromatography with electrochemical detection indicated that in both frontal cortex and hypothalamus, amiflamine (at both doses) increased 5-HT and reduced 5-HIAA concentrations. Combination of amiflamine with L-tryptophan (100 mg kg-1, i.p.) resulted in a higher 5-HT concentration being found than after amiflamine alone. L-Tryptophan treatment alone did not change 5-HT concentrations but increased 5-HIAA concentrations. Clorgyline, at a dose of either 1 or 5 mg kg-1 i.p. plus L-tryptophan (25 or 100 mg kg-1, i.p.) did not increase total activity, locomotion or behaviour. A number of possible explanations for the differences in the behavioural effects of clorgyline and amiflamine when given with L-tryptophan are discussed. It is concluded that in addition to monoamine oxidase-A inhibition, other pharmacological effects of the drugs, such as 5-HT release (amiflamine) and inhibition of tryptophan hydroxylation (clorgyline) may be of importance in determining the magnitude of the increase in activity when the compounds are given together with L-tryptophan.

Animals↗

PubMed1971

Influences of various amino acids on tryptophan-mediated control of the tryptophan biosynthetic enzymes in Escherichia coli.

Lysates of Escherichia coli Ymel obtained from cultures grown in the absence of tryptophan in minimal medium supplemented with 0.1% casein hydrolysate show an approximate fivefold increase in steady-state specific activity of both anthranilate synthetase and tryptophan synthetase A protein relative to cultures grown in nonsupplemented medium. In the presence of repressing levels of exogenous tryptophan, growth of cultures in casein hydrolysate-supplemented medium results in a noncoordinate enhancement of repression of 10-fold for anthranilate synthetase and twofold for tryptophan synthetase A protein. Similar, but less pronounced, effects are shown for strain W3110. Strains possessing tryptophan regulator gene mutations do not exhibit this first effect, but do yield an approximate twofold decrease in specific activity of both enzymes when grown in medium supplemented with tryptophan and casein hydrolysate. A stimulation of derepression of both enzymes in strain Ymel equivalent to that induced by casein hydrolysate can be reproduced by growth in minimal medium supplemented with threonine, phenylalanine, tyrosine, serine, glutamic acid, and glutamine. Doubling time in this medium is not significantly different from that in minimal medium. An enhancement of repression which partially mimics that observed on growth in medium supplemented with tryptophan plus casein hydrolysate is obtained when Ymel is grown on medium supplemented with tryptophan plus methionine. Threonine or phenylalanine plus tyrosine as separate medium supplements are independently capable of producing a 1.4-fold or 3.4-fold stimulation, respectively, but in combination only the phenylalanine plus tyrosine effect is manifested unless serine and glutamic acid or glutamine are included. Our data show that expression of the tryptophan biosynthetic enzymes can be significantly influenced in vivo as a result of growth in medium supplemented with a variety of amino acids.

Amino Acids↗

PubMed2002

Dynamic diversity of the tryptophan pathway in chlamydiae: reductive evolution and a novel operon for tryptophan recapture.

BACKGROUND: Complete genomic sequences of closely related organisms, such as the chlamydiae, afford the opportunity to assess significant strain differences against a background of many shared characteristics. The chlamydiae are ubiquitous intracellular parasites that are important pathogens of humans and other organisms. Tryptophan limitation caused by production of interferon-gamma by the host and subsequent induction of indoleamine dioxygenase is a key aspect of the host-parasite interaction. It appears that the chlamydiae have learned to recognize tryptophan depletion as a signal for developmental remodeling. The consequent non-cultivable state of persistence can be increasingly equated to chronic disease conditions. RESULTS: The genes encoding enzymes of tryptophan biosynthesis were the focal point of this study. Chlamydophila psittaci was found to possess a compact operon containing PRPP synthase, kynureninase, and genes encoding all but the first step of tryptophan biosynthesis. All but one of the genes exhibited translational coupling. Other chlamydiae (Chlamydia trachomatis, C. muridarum and Chlamydophila pneumoniae) lack genes encoding PRPP synthase, kynureninase, and either lack tryptophan-pathway genes altogether or exhibit various stages of reductive loss. The origin of the genes comprising the trp operon does not seem to have been from lateral gene transfer. CONCLUSIONS: The factors that accommodate the transition of different chlamydial species to the persistent (chronic) state of pathogenesis include marked differences in strategies deployed to obtain tryptophan from host resources. C. psittaci appears to have a novel mechanism for intercepting an early intermediate of tryptophan catabolism and recycling it back to tryptophan. In effect, a host-parasite metabolic mosaic has evolved for tryptophan recycling.

Bacterial Proteins↗

PubMedDate not supplied

Absorption rates of L-tryptophan, L-methionine, and L-methionyl-L-tryptophan by rat intestine in vitro and in vivo.

The absorption rates of L-tryptophan, L-methionine, and L-methionyl-L-tryptophan were determined by both the everted sac and the tied loop method with rat intestines. In the everted sac method, high concentrations of L-tryptophan or L-methionyl-L-tryptophan caused anomalous inhibition of absorption of L-tryptophan and L-methionine. The rates of absorption of both L-tryptophan and L-methionyl-L-tryptophan decreased markedly at concentrations higher than 2-3mM. This inhibition was not observed in the tied loop method. Chromatographic, electrophoretic, and microscopic studies suggested that such decreases in absorption rate were caused mainly by decomposition of L-tryptophan to some basic incubation products containing tryptamine with consequent damage to the mucosal surface of everted sacs during long-term incubation. In the tied loop method, L-methionyl-L-tryptophan was absorbed more rapidly than either of the constituent amino acids in equimolar mixture.

Animals↗

PubMed1974