title: Chemoarchitectonic subdivisions of the songbird septum and a comparative overview of septum chemical anatomy in jawed vertebrates.
abstract: Available data demonstrate that the avian septal region shares a number of social behavior functions and neurochemical features in common with mammals. However, the structural and functional subdivisions of the avian septum remain largely unexplored. In order to delineate chemoarchitectural zones of the avian septum, we prepared a large dataset of double-, triple-, and quadruple-labeled material in a variety of songbird species (finches and waxbills of the family Estrildidae and a limited number of emberizid sparrows) using antibodies against 10 neuropeptides and enzymes. Ten septal zones were identified that were placed into lateral, medial, caudocentral, and septohippocampal divisions, with the lateral and medial divisions each containing multiple zones. The distributions of numerous immunoreactive substances in the lateral septum closely match those of mammals (i.e., distributions of met-enkephalin, vasotocin, galanin, calcitonin gene-related peptide, tyrosine hydroxylase, vasoactive intestinal polypeptide, substance P, corticotropin-releasing factor, and neuropeptide Y), enabling detailed comparisons with numerous chemoarchitectonic zones of the mammalian lateral septum. Our septohippocampal and caudocentral divisions are topographically comparable to the mammalian septohippocampal and septofimbrial nuclei, respectively, although additional data will be required to establish homology. The present data also demonstrate the presence of a medial septal nucleus that is histochemically comparable to the medial septum of mammals. The avian medial septum is clearly defined by peptidergic markers and choline acetyltransferase immunoreactivity. These findings should provide a useful framework for functional and comparative studies, as they suggest that many features of the septum are highly conserved across vertebrate taxa.
authors.affiliation: Psychology Department, University of California, San Diego, La Jolla, California 92093, USA. jgoodson@ucsd.edu
authors.forename: James L
authors.initials: JL
authors.lastname: Goodson
authors.forename: Andrew K
authors.initials: AK
authors.lastname: Evans
authors.forename: Laura
authors.initials: L
authors.lastname: Lindberg
mesh_terms: D000818:Animals; D001127:Arginine Vasopressin / Q000378:metabolism; D015740:Calcitonin Gene-Related Peptide / Q000378:metabolism; D002795:Choline O-Acetyltransferase / Q000378:metabolism; D004744:Enkephalin, Methionine / Q000378:metabolism; D005260:Female; D019004:Galanin / Q000378:metabolism; D007150:Immunohistochemistry / Q000379:methods; D008297:Male; D009434:Neural Pathways / Q000033:anatomy & histology / Q000378:metabolism; D009474:Neurons / Q000378:metabolism*; D009478:Neuropeptide Y / Q000378:metabolism; D020665:Septum of Brain / Q000166:cytology* / Q000378:metabolism*; D020308:Songbirds; D013045:Species Specificity; D013373:Substance P / Q000378:metabolism; D014446:Tyrosine 3-Monooxygenase / Q000378:metabolism; D014660:Vasoactive Intestinal Peptide / Q000378:metabolism; D014828:Vocalization, Animal
chemical_list: D009478:Neuropeptide Y; D001127:Arginine Vasopressin; D013373:Substance P; D014660:Vasoactive Intestinal Peptide; D004744:Enkephalin, Methionine; D019004:Galanin; D014446:Tyrosine 3-Monooxygenase; D002795:Choline O-Acetyltransferase; D015740:Calcitonin Gene-Related Peptide