Characteristics of tryptophan accumulation by glial cells

Bauman, Annie; Bourgoin, S.; Benda, P; Głowiński, J.; Hamon, Michel

doi:10.1016/0006-8993(74)90144-9

Cited by 45 publications

(4 citation statements)

References 19 publications

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“…The present results show that tryptophan is accumulated in membrane vesicles derived from synaptosomes by an Na+-gradient-dependent system analogous to those previously described €or other amino acids in similar preparations (Kanner, 1978; Kanner and Sharon, 1978; Arag6n et al, 1981;Marviz6n et al, 1981). The process has features similar to those seen in cruder preparations such as brain slices, glial cells (Bauman et al, 1974), or synaptosomes (Knapp and Mandell, 1973; Mandell and Knapp, 1977). The vesicles were preloaded with KCI medium and incubated for 30 s as described in Experimental Procedures in the presence of 5 pLM-~-[G-~H]trypt~phan and the indicated additions in the NaCl medium or the KCI medium.…”

Section: Discussionsupporting

confidence: 85%

Tryptophan Transport into Plasma Membrane Vesicles Derived from Rat Brain Synaptosomes

Herrero

Aragón

Giménez

et al. 1983

Journal of Neurochemistry

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Tryptophan uptake by membrane vesicles derived from rat brain was investigated. The uptake is dependent on the Na+ gradient [Na+] outside greater than [Na+] inside, and is maximal when both Na+ and Cl- are present. The uptake represents transport into an osmotically active space and not a binding artifact, as indicated by the effect of increasing the medium osmolarity. The uptake of tryptophan is stimulated by a membrane potential (interior negative) as demonstrated by the effects of the ionophores valinomycin and carbonyl cyanide m-chlorophenylhydrazone and anions with different permeabilities. Kinetic data show that tryptophan is accumulated by two systems with different affinities. Ouabain, an inhibitor of Na+,K+-activated ATPase, does not affect tryptophan transport. The uptake of tryptophan is inhibited by high concentrations of phenylalanine, tyrosine, leucine, and 3,4-dihydroxyphenylalanine.

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Section: Discussionsupporting

confidence: 85%

Tryptophan Transport into Plasma Membrane Vesicles Derived from Rat Brain Synaptosomes

Herrero

Aragón

Giménez

et al. 1983

Journal of Neurochemistry

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“…The kinetic parameters of leucine uptake by components I and I1 were the same under both conditions. Bauman et al (1974) also reported low and high K, values of Na+-independent tryptophan uptake by C6 glial cells.…”

Section: Discussionmentioning

confidence: 83%

Triiodothyronine Is a High‐Affinity Inhibitor of Amino Acid Transport System L₁ in Cultured Astrocytes

Blondeau

Beslin

Chantoux

et al. 1993

Journal of Neurochemistry

103

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The relationship between the transport of thyroid hormones and that of amino acids was examined by measuring the uptake of amino acids that are characteristic substrates of systems L, A, and N, and the effect of 3,3',5-triiodo-L-thyronine (T3) on this uptake, in cultured astrocytes. Tryptophan and leucine uptakes were rapid, Na(+)-independent, and efficiently inhibited by T3 (half-inhibition at approximately 2 microM). Two Na(+)-independent L-like systems (L1 and L2), common to leucine and aromatic amino acids, were characterized kinetically. System L2 had a low affinity for leucine and tryptophan (Km = 0.3-0.9 mM). The high-affinity system L1 (Km approximately 10 microM for both amino acids) was competitively inhibited by T3 with a Ki of 2-3 microM (close to the T3 transport Km). Several T3 analogues inhibited system L1 and the T3 transport system similarly. Glutamine uptake and alpha-(methylamino)isobutyric acid uptake were, respectively, two and 200 times lower than tryptophan and leucine uptakes. T3 had little effect on the uptakes of glutamine and alpha -(methylamino)isobutyric acid. The results indicate that the T3 transport system and system L1 are related.

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“…arpAT transport specificity and tissue distribution gives few clues about its physiology. In the brain, sodium-independent low and high affinity components of L-Tyr, L-DOPA, and L-Trp transport have been identified (56,57). The low affinity component is consistent with arpAT expression.…”

Section: Comparative Analysis Of the Evolution Of Arpat Inmentioning

confidence: 60%

Identification and Functional Characterization of a Novel Low Affinity Aromatic-preferring Amino Acid Transporter (arpAT)

Fernández

Torrents

Zorzano

et al. 2005

Journal of Biological Chemistry

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Characteristics of tryptophan accumulation by glial cells

Cited by 45 publications

References 19 publications

Tryptophan Transport into Plasma Membrane Vesicles Derived from Rat Brain Synaptosomes

Tryptophan Transport into Plasma Membrane Vesicles Derived from Rat Brain Synaptosomes

Triiodothyronine Is a High‐Affinity Inhibitor of Amino Acid Transport System L₁ in Cultured Astrocytes

Identification and Functional Characterization of a Novel Low Affinity Aromatic-preferring Amino Acid Transporter (arpAT)

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Characteristics of tryptophan accumulation by glial cells

Cited by 45 publications

References 19 publications

Tryptophan Transport into Plasma Membrane Vesicles Derived from Rat Brain Synaptosomes

Tryptophan Transport into Plasma Membrane Vesicles Derived from Rat Brain Synaptosomes

Triiodothyronine Is a High‐Affinity Inhibitor of Amino Acid Transport System L1 in Cultured Astrocytes

Identification and Functional Characterization of a Novel Low Affinity Aromatic-preferring Amino Acid Transporter (arpAT)

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Triiodothyronine Is a High‐Affinity Inhibitor of Amino Acid Transport System L₁ in Cultured Astrocytes