Immunocytochemically defined interneuron populations in the hippocampus of mouse strains used in transgenic technology.
Transgenic mice are overtaking the role of model animals in neuroscience. They are used in developmental, anatomical, and physiological as well as experimental neurology. However, most results on the organization of the nervous system derive from the rat. The rat hippocampus and its neuronal elements have been thoroughly investigated, revealing remarkable functional and morphological diversity and specificity among hippocampal interneurons. Our aim was to examine the properties of distinct hippocampal interneuron populations, i.e., those immunoreactive for calcium-binding proteins (parvalbumin, calbindin, and calretinin), neuropeptides (cholecystokinin, neuropeptide Y, somatostatin, vasoactive intestinal polypeptide), and certain receptors (metabotropic glutamate receptor 1alpha, cannabinoid receptor type 1) in four strains of mice widely used in transgenic technology, and to compare their properties to those in the rat. Our data indicate that the distribution as well as the dendritic and axonal arborization of mouse interneurons immunoreactive for the different markers was identical in the examined mouse strains, and in most respects are similar to the features found in the rat. The postsynaptic targets of neurons terminating in the perisomatic (parvalbumin), proximal (calbindin), and distal (somatostatin) dendritic region, as well as on other interneurons (calretinin), also matched those found in the rat. However, a few significant differences could also be observed between the two species in addition to the already described immunoreactivity of mossy cells for calretinin: the absence of spiny calretinin-immunoreactive interneurons in the CA3 region, sparse contacts between calretinin-immunoreactive interneurons, and the axon staining for somatostatin and neuropil labeling for cholecystokinin. We can conclude that the morphofunctional classification of interneurons established in the rat is largely valid for mouse strains used in transgenic procedures.
Mátyás
Ferenc
F
Institute of Experimental Medicine, Hungarian Academy of Sciences, Budapest, Hungary.
Freund
Tamás F
TF
Gulyás
Attila I
AI
D000818:Animals; D064026:Calbindins; D002135:Calcium-Binding Proteins / Q000378:metabolism; D003433:Crosses, Genetic; D005260:Female; D006624:Hippocampus / Q000166:cytology* / Q000502:physiology; D007150:Immunohistochemistry / Q000379:methods; D007395:Interneurons / Q000166:cytology* / Q000502:physiology; D008297:Male; D051379:Mice; D008810:Mice, Inbred C57BL; D008808:Mice, Inbred CBA; D008822:Mice, Transgenic; D010320:Parvalbumins / Q000378:metabolism; D043882:Receptors, Cannabinoid / Q000032:analysis; D064030:S100 Calcium Binding Protein G / Q000378:metabolism; D005680:gamma-Aminobutyric Acid / Q000378:metabolism
D064026:Calbindins; D002135:Calcium-Binding Proteins; D010320:Parvalbumins; D043882:Receptors, Cannabinoid; D064030:S100 Calcium Binding Protein G; D005680:gamma-Aminobutyric Acid