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. 1975 Feb;72(2):659–663. doi: 10.1073/pnas.72.2.659

Ultrastructural localization of tyrosine hydroxylase in noradrenergic neurons of brain.

V M Pickel, T H Joh, D J Reis
PMCID: PMC432374  PMID: 235760

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.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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