NDLI: Ultrastructural localization of tyrosine hydroxylase in noradrenergic neurons of brain.

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Ultrastructural localization of tyrosine hydroxylase in noradrenergic neurons of brain.

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Ultrastructural localization of tyrosine hydroxylase in noradrenergic neurons of brain.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Reis, D. J. Pickel, V. M. Joh, T. H.
Abstract	Tyrosine hydroxylase (EC 1.14.16.2), the enzyme catalyzing the rate-limiting step in catecholamine biosynthesis, was localized by electron microscopy within noradrenergic neurons of the nucleus locus coeruleus of the rat brain with a specific antibody to tyrosine hydroxylase labeled by the peroxidase-antiperoxidase immunohistochemical method. Labeled cell bodies and their processes were easily distinguished from unstained neuronal elements in the neuropil. The hydroxylase was only seen in the neuronal cytoplasm. Its distribution in processes was different from that in cell soma. In longitudinal sections of axons and dendrites, the peroxides reaction product appeared as fiber-like strands aligned parallel with the plasma membrane. In cross section, the labeled structures had a diameter of 220 A and exhibited an orderly distribution within the processes. The size and distribution of the peroxidase-stained structures suggest that they are neurotubules. In the perikarya, the cytoplasm was diffusely stained; the reaction was most intense on membranes of endoplasmic reticulum and Golgi apparatus, whereas lysosomes and mitochondria did not stain. The ultrastructural localization of tyrosine hydroxylase is consistent with biochemical data suggesting that the enzyme exists in different states in cell body and processes. The ultrastructural identification of enzymes subserving synthesis of neurotransmitters in central neurons and their processes may provide a useful tool in mapping the distribution of chemically specific synapses on identifiable neurons in brain.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	2
Volume Number	72
Language	English
Publisher	National Academy of Sciences
Publisher Date	1975-06-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Cerebral Ventricles Enzymology Tyrosine 3-Monooxygenase Animals Antigen-Antibody Reactions Ultrastructure Cytoplasm Endoplasmic Reticulum Histocytochemistry Immunologic Techniques Microscopy, Electron Mitochondria Neurons Peroxidases Immunology Research Support, U.S. Gov't, P.H.S. Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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