Title

Comparison of acetylcholinesterase and choline acetyltransferase staining patterns in the optic tectum of the goldfish carassius auratus: A histochemical and immunocytochemical analysis

Document Type

Article

Abstract

Although the optic tectum of nonmammalian vertebrates has been extensively studied anatomically, there is little information about the identification of neuro-transmitters and the enzymes critical to their synthesis. Choline acetyltransferase (Ch AT), the enzyme responsible for acetylcholine synthesis, is presently regarded as the most reliable marker for cholinergic neurons, and its localization within putative cholinergic neurons has been made possible by the development of antibodies specific to ChAT. We have compared the immunocytochemical localization of ChAT to the histochemical staining of acetylcholinesterase (AChE) in the goldfish optic tectum. Goldfish brains reacted with the monoclonal antibody AB8 to ChAT have revealed that: (1) type XIV neurons are the only ChAT-positive cells in the tectum, and there are approximately 15,000 such cells per tectal hemisphere; (2) these neurons and other ChAT-con-taining afferent fibers form bands of label which correspond to those seen after AChE staining, and (3) many AChE-stained neurons do not contain ChAT. The immunohisto-chemical localization of ChAT has provided a direct method for determining the localization and organization of putative cholinergic structures in the optic tectum of goldfish. Future studies may elucidate the relationship of these cholinergic systems to the retinotectal projections, as there is close correspondence between AChE and ChAT location and the retinotectal termination patterns. © 1987 S. Karger AG, Basel.

Keywords

Acetylcholinesterase, Choline acetyltransferase, Cholinergic neurons, Immunohistochemistry, Optic tectum

Publication Date

1-1-1987

Publication Title

Brain, Behavior and Evolution

ISSN

00068977

Volume

30

Issue

3-4

First Page

143

Last Page

159

PubMed ID

3311287

Digital Object Identifier (DOI)

10.1159/000118643

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