CaRLO — Cancer Research Library Online

1

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PROPERTIES AND REGIONAL DISTRIBUTION OF HISTIDINE DECARBOXYLASE IN RAT BRAIN (1970)

Schwartz, J. C. ; Lampart, C. ; Rose, C.

Oxford, UK : Blackwell Publishing Ltd

Journal of neurochemistry 17 (1970), S. 0

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ISSN: 1471-4159

Source: Blackwell Publishing Journal Backfiles 1879-2005

Topics: Medicine

Notes: —Properties of the histamine-forming enzyme in rat brain were studied, utilizing a sensitive fluorometric assay. The optimum pH was related to substrate concentration and found to be6·4 at 10−2m-histidine; the apparent Km was about 4·10−4m; enzyme activity was inhibited by α-hydrazino -histidine and brocresine but was not affected by α-methyl DOPA or benzene. These different data suggest that the 'specific’histidine decarboxylase (EC 4.1.1.22)—and not the aromatic l-aminoacid decarboxylase—is involved. Determination of enzyme activity and histamine level in different areas of the rat brain revealed important regional differences, the two values being roughly parallel.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1111/j.1471-4159.1970.tb03722.x

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An alternative route for biosynthesis of methylhistamine: In vitro and in vivo formation through decarboxylation ofl-3-methylhistidine (1972)

Schwartz, J. C. ; Caillens, H. ; Rose, C.

Springer

Cellular and molecular life sciences 28 (1972), S. 904-905

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ISSN: 1420-9071

Source: Springer Online Journal Archives 1860-2000

Topics: Biology , Medicine

Notes: Résumé On a mis en évidence chez le Rat une formation de méthylhistamine-3H par décarboxylation de lal-3-méthylhistidine-3H. Cette réaction se produit in vitro et in vivo dans des tissus riches en histidine décarboxylase et elle est prévenue par un inhibiteur de cette enzyme. Les implications biologiques de l'existence de cette nouvelle voie métabolique sont envisagées.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1007/BF01924935

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3

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Daily Rhythms in Content and Utilization of Tyrosine in the Whole Mouse (1970)

ROSE, C. M. ; WURTMAN, R. J.

[s.l.] : Nature Publishing Group

Nature 226 (1970), S. 454-455

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ISSN: 1476-4687

Source: Nature Archives 1869 - 2009

Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics

Notes: [Auszug] Swiss mice (Type CD?I, from Charles River Breeding Laboratories) were subjected to periods of alternating light and darkness (light from 0900?2100 h) for at least 2 weeks. Approximately 50 foot candles of light were provided by 'Vita-Lite' bulbs (Duro-Test Manufacturing), whose emissions simulate ...

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1038/226454a0

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4

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Synthesis and release of3H-histamine in slices from rat brain (1974)

Verdiere, M. ; Rose, C. ; Schwartz, J. C.

Springer

Inflammation research 4 (1974), S. 184-185

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ISSN: 1420-908X

Source: Springer Online Journal Archives 1860-2000

Topics: Medicine

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1007/BF01970264

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HISTAMINE FORMATION IN RAT BRAIN IN VIVO: EFFECTS OF HISTIDINE LOADS (1972)

Schwartz, J. C. ; Lampart, C. ; Rose, C.

Oxford, UK : Blackwell Publishing Ltd

Journal of neurochemistry 19 (1972), S. 0

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ISSN: 1471-4159

Source: Blackwell Publishing Journal Backfiles 1879-2005

Topics: Medicine

Notes: Abstract— Administration of l-histidine at the rate of 500 mg/kg induced an increase of nearly 50 per cent in the level of histamine in rat brain which lasted several hours. The augmentation of histamine level was not significant 3 h after lower doses or after d-histidine α-methyl DOPA and Ro 4-4602 neither affected the cerebral level of histamine nor its elevation induced by l-histidine. Brocresine, a known histidine decarboxylase inhibitor not only prevented the effect of histidine load but also induced a prompt fall in the amine level. These results confirm those from earlier experiments in vitro indicating that histamine synthesis in rat brain depends on a specific decarboxylase (EC 4, 1.1.22) which is not normally saturated by the endogenous level of its substrate.When histamine levels were enhanced by histidine treatment, histidine decarboxylase activity, as evaluated on hypothalamus homogenates, was significantly reduced; intracisternal administration of cycloheximide, an inhibitor of protein synthesis, had similar effects. On the other hand, enzyme activity was not altered by the addition of histamine to hypothalamus homogenates. These results are compatible with the existence of a regulation mechanism of histidine decarboxylase involving repression by its end-product.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1111/j.1471-4159.1972.tb01394.x

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Histamine formation in rat brain during development (1971)

Schwartz, J-C. ; Lampart, C. ; Rose, C. ; [et al.]

Oxford, UK : Blackwell Publishing Ltd

Journal of neurochemistry 18 (1971), S. 0

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ISSN: 1471-4159

Source: Blackwell Publishing Journal Backfiles 1879-2005

Topics: Medicine

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1111/j.1471-4159.1971.tb03757.x

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