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Immunocytochemical colocalization of histamine, histidine decarboxylase, 5-hydroxytryptamine and tyrosine hydroxylase in the superior cervical ganglion of the rat
Authors:H. Pä  ivä  rinta, O. Hä  ppö    , T. H. Joh, H. Steinbusch, T. Watanabe  P. Panula
Affiliation:(1) Department of Anatomy, University of Helsinki, Siltavuorenpenger 20 A, 00170 Helsinki, Finland;(2) Department of Neurology, Laboratory of Molecular Neurobiology, Cornell University Medical College, 1300 York Avenue, 10021 New York, N.Y., USA;(3) Department of Pharmacology, Free University, 1081 BT Amsterdam, The Netherlands;(4) Department of Pharmacology II, Osaka University School of Medicine, 3-57, Nakanoshima 4, Kita-ku, 530 Osaka, Japan
Abstract:Summary The coexistence of histamine, histidine decarboxylase (the enzyme synthesizing histamine), 5-hydroxytryptamine and tyrosine hydroxylase (the rate-limiting enzyme in catecholamine synthesis), was studied in the rat superior cervical ganglion with the indirect immunofluorescence method. Possible colocalization was examined by staining consecutive sections with two different antibodies, or alternatively in the same section by eluting the first antibody with a mild solution containing potassium permanganate and sulphuric acid, and by staining the same section with another antibody. It was shown that tyrosine hydroxylase immunoreactivity was found both in large principal nerve cells and in small cells, which on the basis of their size and high nucleus—cytoplasm ratio corresponded to small intensely fluorescent (SIF) cells. Histamine, histidine decarboxylase and 5-hydroxytryptamine immunoreactivities were observed only in SIF cells. Those SIF cells which were immunoreactive for histamine, histidine decarboxylase or 5-hydroxytryptamine also contained tyrosine hydroxylase immunoreactivity. On the other hand, all tyrosine hydroxylase-immunoreactive SIF cells were also immunoreactive for histidine decarboxylase or 5-hydroxytryptamine. Some of the SIF cells, which were non-reactive for histamine, were immunoreactive for tyrosine hydroxylase.
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