4.1 Article

Immunocytochemical Localization of Calcium-binding Proteins, Calbindin D28K-, Calretinin-, and Parvalbumin-containing Neurons in the Dog Visual Cortex

Journal

ZOOLOGICAL SCIENCE
Volume 28, Issue 9, Pages 694-702

Publisher

ZOOLOGICAL SOC JAPAN
DOI: 10.2108/zsj.28.694

Keywords

calcium-binding proteins; visual cortex; immunocytochemistry; localization; gamma-aminobutyric acid

Categories

Funding

  1. Korea Research Foundation [KRF 2006-311-E00370]
  2. National Research Foundation of Korea [2006-311-E00370] Funding Source: Korea Institute of Science & Technology Information (KISTI), National Science & Technology Information Service (NTIS)

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Although the dog is widely used to analyze the function of the brain, it is not known whether the distribution of calcium-binding proteins reflects a specific pattern in the visual cortex. The distribution of neurons containing calcium-binding proteins, calbindin D28K, calretinin, and parvalbumin in adult dog visual cortex were studied using immunocytochemistry. We also compared this labeling to that of gamma-aminobutyric acid (GABA). Calbindin D28K-immunoreactive (IR) neurons were predominantly located in layer II/III. Calretinin-and parvalbumin-IR neurons were located throughout the layers with the highest density in layers II/III and IV. The large majority of calbindin D28K-IR neurons were multipolar stellate cells. The majority of the calretinin-IR neurons were vertical fusiform cells with long processes traveling perpendicular to the pial surface. And the large majority of parvalbumin-IR neurons were multipolar stellate and round/oval cells. More than 90% of the calretinin-and parvalbumin-IR neurons were double-labeled with GABA, while approximately 66% of the calbindin D28K-IR neurons contained GABA. This study elucidates the neurochemical structure of calcium-binding proteins. These data will be informative in appreciating the functional significance of different laminar distributions of calcium-binding proteins between species and the differential vulnerability of calcium-binding proteins-containing neurons, with regard to calcium-dependent excitotoxic procedures.

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