Incorporation of radioactivity from labeled serotonin and tryptamine into acid-insoluble material from subcellular fractions of brain.  I.  Nature of the substrate

Alivisatos, Spyridon G.A.; Ungar, Frieda

doi:10.1021/bi00841a035

Cited by 59 publications

(11 citation statements)

References 31 publications

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“…The conversion of tryptamine into ITCA reported in the present work occurs in a two-step reaction ( Fig. reaction (step 1 and step 2) at pH 7.0 which is in good agreement with the results of Alivisatos and Ungar ( 1968) for the incorporation of indoleamine into soluble material. On the other hand, we observed that step 2 of the reaction, namely the condensation of IAAL with L-cysteine, proceeds rapidly in basic media, yielding ITCA which absorbed at 276 nm.…”

Section: Discussionsupporting

confidence: 91%

“…The rate of condensation increased on raising the pH and was unaffected by heat denaturation. Thus, the second step of the reaction showed strong similarities with the incorporation of indoleamine into nonextractable material (Alivisatos and Ungar, 1968) and with the reaction of IAAL with brain tissue observed by Nilsson and Tottmar (1985).…”

Section: Discussionsupporting

confidence: 63%

“…It has been reported that tryptamine was metabolized in the brain or liver into "pigment" (Pugh and Quastel, 1937;Blaschko and Hellmann, 1953;Nakai, 1958) and into soluble and insoluble "incorporated material" (Alivisatos and Ungar, 1968) via IAAL as an intermediate compound. The incorporation into soluble material (extractable with chloroform/methanol, 2: 1) was enzyme catalyzed, showing a pH optimum at pH 7.0.…”

Section: Discussionmentioning

confidence: 99%

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Formation of a New Biogenic Aldehyde Adduct by Incubation of Tryptamine with Rat Brain Tissue

Susilo

Damm

Rommelspacher

1988

Journal of Neurochemistry

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Tryptamine was degraded by incubation with rat brain homogenate to an unknown product. The reaction was stimulated by the nonionic detergents Triton X-100 and Lubrol PX and less by the zwitterionic detergent 3-[(3-cholamidopropyl)dimethylammonio]1-propanesulfonate (CHAPS). The same results were obtained with pig brain and bovine brain. The monoamine oxidase inhibitor pargyline inhibited the reaction strongly, indicating the participation of the enzyme on the reaction. Addition of 17,000 g supernatant from rat brain homogenate increased the formation effectively whereas phospholipids or chloroform/methanol (7:3) extract from the 17,000 g supernatant showed only little or no effect. Chromatographic and electrophoretic properties as well as the chemical reaction of the product with specific reagents suggest that the compound consists of an indole part and an amino acid part. The product could be identified by fast atom bombardment mass spectrometry and by comparison with the synthetic substance (4R)-2-(3-indolylmethyl)-1,3-thiazolidine-4-carboxylic acid. It is formed by the enzymatic oxidation of tryptamine producing indole-3-acetaldehyde which spontaneously cyclizes with free L-cysteine from the tissue. The results suggest that the reaction of biogenic aldehydes with brain macromolecules may proceed via an analogous reaction.

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Section: Discussionsupporting

confidence: 91%

Section: Discussionsupporting

confidence: 63%

Section: Discussionmentioning

confidence: 99%

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Formation of a New Biogenic Aldehyde Adduct by Incubation of Tryptamine with Rat Brain Tissue

Susilo

Damm

Rommelspacher

1988

Journal of Neurochemistry

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“…It may also be that any attempt to increase their overall concentrations, e.g., by inhibiting ALDH, above the detection limit of the assays presently available would only result in an increased amount of aldehyde bound to various biomolecules, and not in a higher level of free aldehyde. Such a view is supported by studies in vivo by Alivisatos and Ungar (1968), Alivisatos and Tabakoff (1973), and Alivisatos et al (1970). They injected rats or mice with ['4C]tryptamine, ['4C]tryptophan, or [I4C]5-HT and found decreased incorporation of radioactivity to brain membranes in animals given an MA0 inhibitor and increased incorporation in animals given pentobarbital or acetaldehyde, two substances capable of inhibiting the degradation of biogenic aldehydes.…”

Section: Preparation Of Biogenic Aldehydesmentioning

confidence: 90%

Biogenic Aldehydes in Brain: On Their Preparation and Reactions with Rat Brain Tissue

Nilsson

Tottmar

1987

Journal of Neurochemistry

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When 1 mM serotonin, dopamine, or norepinephrine was incubated with a monoamine oxidase preparation (mitochondrial membranes) in the presence of 4 mM sodium bisulfite, 85-95% of the amines were oxidized to the corresponding aldehydes. In the absence of bisulfite, the recoveries were only approximately 30%, and dark colored products were formed during the incubations. The aldehydes derived from tyramine, octopamine, methoxytyramine, and normetanephrine were also prepared by the use of this method. The bisulfite-aldehyde compounds were stable during storage at -20 degrees C. Bisulfite-free aldehyde solutions were made by diethylether extraction. When the aldehydes derived from dopamine or serotonin were incubated with rat brain homogenates, they were found to disappear in an aldehyde dehydrogenase- and aldehyde reductase-independent manner. The disappearance of the latter aldehyde was more pronounced, and the results indicated that this aldehyde may react with both proteins and phospholipids.

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“…Although 5-OH-IAA itself has not previously been reported to have any regulatory role, 5-hydroxytryptamine is a neutrotransmitter (37), has been implicated in behavioral phenotypes (38)(39)(40)(41)(42)(43)(44), and is a precursor of the hormone melatonin (45). The aldehyde derived from this amine is also considered to have biological activity (46)(47)(48)(49).…”

mentioning

confidence: 99%

Metabolite gene regulation of the L-arabinose operon in Escherichia coli with indoleacetic acid and other indole derivatives.

Kline¹,

Brown²,

Bankaitis³

et al. 1980

Proc. Natl. Acad. Sci. U.S.A.

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The ability of indole derivatives to facilitate RNA polymerase transcription of the L-arabinose operon in Escherichia coli was shown to require the catabolite activator protein (CAP) as well as the araC gene product. Adenosine 3',5'-monophosphate (cAMP) was not obligatory for araBAD transcription when the cells were grown in the presence of 1 mM indole-3-acetic acid or in the presence of indole-3-acetamide, indole-3-propionic acid, indole-3-butyric acid, or 5-hydroxyindole-3-acetic acid. However, these indole derivatives were unable to circumvent the cAMP requirement for the induction of the lactose and the maltose operons. Catabolite repression occurred when glucose was added to cells grown in the presence of L-arabinose and 1 mM indoleacetic acid or 1 mM cAMP. This effect was reversed at higher concentrations of indoleacetic acid or cAMP. The induction and the catabolite repression phenomena were quantitated by measuring the differential rate of synthesis of L-arabinose isomerase (the araA gene product). These results indicated that indole metabolites from various living systems may regulate gene expression and may be involved in "metabolite gene regulation."The induction of the L-arabinose regulon-araBAD, araE, and araF-in Escherichia coli requires the protein product (P2) of the araC gene, the catabolite activator protein (CAP), and adenosine 3',5'-monophosphate (cAMP) (1-8). Hence, mutants with an inactive product for the crp gene (the gene coding for CAP), the araC gene, or the cya gene (the gene coding for adenylate cyclase) are unable to utilize L-arabinose as a carbon source.The existence of araCl mutants that can circumvent the requirement for cAMP in the induction of the L-arabinose operon (2) and the complexity of various regulatory interlocks (9-11) led to the idea that low molecular weight metabolites other than the ubiquitous cAMP and guanosine 3',5'-monophosphate might function at the genetic level in cell regulation. Recently, we demonstrated with cya deletion strains of E. coli (12) that specific concentrations of imidazoleacetic acid, a compound structurally related to the amino acid histidine, could circumvent the necessity for cAMP in the induction of the araBAD structural genes. In addition, preliminary evidence indicated that a metabolite of tryptophan, indole-3-acetic acid (IAA), could function in the "metabolite gene regulation" of eukaryotic cells and various genera of bacteria. *

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Incorporation of radioactivity from labeled serotonin and tryptamine into acid-insoluble material from subcellular fractions of brain. I. Nature of the substrate

Cited by 59 publications

References 31 publications

Formation of a New Biogenic Aldehyde Adduct by Incubation of Tryptamine with Rat Brain Tissue

Formation of a New Biogenic Aldehyde Adduct by Incubation of Tryptamine with Rat Brain Tissue

Biogenic Aldehydes in Brain: On Their Preparation and Reactions with Rat Brain Tissue

Metabolite gene regulation of the L-arabinose operon in Escherichia coli with indoleacetic acid and other indole derivatives.

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