Distribution of Tryptophan in Erythrocytes, Leukocytes and Thrombocytes, and Its Binding to Plasma Albumin

Baumann, Pierre; Perey, M; Laurian, S.; Grasset, François; Steck, Andreas; Gaillard, Jean‐Michel

doi:10.1007/978-3-7091-2243-3_15

Cited by 5 publications

(4 citation statements)

References 21 publications

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“…Our results show that after 1 h of incubation at 37 °C the ratio between intracellular and plasma 14C-tryptophan is the same as the ratio found by Baumann et al [1979] between endogenous intracellular and total plasma tryptophan. The fact that this ratio remains much lower than 1, in contrast to tyrosine, suggests that the free fraction of tryptophan can only cross the cell membrane.…”

Section: Discussionsupporting

confidence: 71%

L-Tyrosine and L-Tryptophan Transport in Red Blood Cells in Normal Subjects

Widmer¹,

Gaillard²,

Tissot³

1986

Neuropsychobiology

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Blood cells may be used as a model in the central transport mechanisms of amino acids, precursors of amines, implicated in some hypotheses of psychiatric diseases. In a previous paper, we showed a deficit of tyrosine transport by red cells incubated in the plasma of depressed patients. In the present study, we have investigated the interaction of these peripheral transport mechanisms for tyrosine and tryptophan with other amino acid transports, such as the L and ASC systems, and the role of sodium ions in the extracellular medium. We also describe the inhibition induced by incubation at a low temperature, and a probable role of the membrane viscosity. The interest of incubating the cells in their own plasma, in order to have physiological conditions, is also discussed.

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Section: Discussionsupporting

confidence: 71%

L-Tyrosine and L-Tryptophan Transport in Red Blood Cells in Normal Subjects

Widmer¹,

Gaillard²,

Tissot³

1986

Neuropsychobiology

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“…Hence insulin secretion (or carbohydrate consumption) normally elevates the plasma Trp ratio (Fernstrom and Wurtman, 1971;Wurtman et al, 1981;Fernstrom et al, 1979) while its absence tends to lower the ratio. The reduction in fasting plasma Trp levels observed when non-obese subjects consumed the PSMF diet may have resulted in part from a persistent elevation in plasma NEFA, secondary to diet-induced insulinopenia, which could have displaced the amino acid from albumin (Baumann et al, 1979). Our observations suggest that supplemental Trp might be useful for restoring the plasma Trp ratio to normal in subjects on PSMF diets, especially when the ratio is already diminished by obesity.…”

Section: Discussionmentioning

confidence: 56%

The treatment of obesity by carbohydrate deprivation suppresses plasma tryptophan and its ratio to other large neutral amino acids

Héraïef¹,

Burckhardt²,

Mauron

et al. 1983

J. Neural Transmission

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We measured plasma concentrations of tryptophan (Trp) and the other large neutral amino acids (LNAA) in 6 control and 7 obese subjects before and after they consumed a low-carbohydrate "protein-sparing modified fast" (PSMF) diet; LNAA levels in control subjects were also assessed after supplemental oral Trp. Consumption of the PSMF diet by non-obese subjects, or obesity per se, caused major reductions in the ratio of the plasma Trp concentration to the summed plasma concentrations of the other LNAA (i.e., the "plasma Trp ratio"), and may thus have diminished brain serotonin synthesis. Administration of even 2 g of supplemental Trp did not elevate the plasma Trp ratio beyond the normal range observed previously in subjects consuming carbohydrate-containing meals.

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“…Like RBCs, platelets do not have a nucleus but contain granules of chemotactic molecules, fibrinogen, coagulation factors, tubules to form canalicular structures, and mitochondria to support their transformation upon activation. The role of blood cells in the transport of amino acid L‐tryptophan highlighted that tryptophan is present in and transported by platelets (Baumann et al, 1979). Mitochondria and associated NAD(P)H and FAD regulate platelet function (Galeotti et al, 1970; Rodrigues et al, 2011).…”

Section: Source Of Autofluorescence Of Bloodmentioning

confidence: 99%

Autofluorescence of blood and its application in biomedical and clinical research

Shrirao

Schloss

Fritz

et al. 2021

Biotech & Bioengineering

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Autofluorescence of blood has been explored as a label free approach for detection of cell types, as well as for diagnosis and detection of infection, cancer, and other diseases.Although blood autofluorescence is used to indicate the presence of several physiological abnormalities with high sensitivity, it often lacks disease specificity due to use of a limited number of fluorophores in the detection of several abnormal conditions. In addition, the measurement of autofluorescence is sensitive to the type of sample, sample preparation, and spectroscopy method used for the measurement. Therefore, while current blood autofluorescence detection approaches may not be suitable for primary clinical diagnosis, it certainly has tremendous potential in developing methods for large scale screening that can identify high risk groups for further diagnosis using highly specific diagnostic tests. This review discusses the source of blood autofluorescence, the role of spectroscopy methods, and various applications that have used autofluorescence of blood, to explore the potential of blood autofluorescence in biomedical research and clinical applications.

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Distribution of Tryptophan in Erythrocytes, Leukocytes and Thrombocytes, and Its Binding to Plasma Albumin

Cited by 5 publications

References 21 publications

<i>L</i>-Tyrosine and <i>L</i>-Tryptophan Transport in Red Blood Cells in Normal Subjects

<i>L</i>-Tyrosine and <i>L</i>-Tryptophan Transport in Red Blood Cells in Normal Subjects

The treatment of obesity by carbohydrate deprivation suppresses plasma tryptophan and its ratio to other large neutral amino acids

Autofluorescence of blood and its application in biomedical and clinical research

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