title: Patterns of phosphorylated tyrosine hydroxylase vary with song production in female starlings.
abstract: Vocal signal production in male songbirds is well studied, but the neural correlates of female song production are poorly understood. In European starlings, females sing to defend nesting resources, and song can be considered agonistically motivated. Across vertebrates catecholamines strongly influence motivated, agonistic social behaviors. The present study was designed to provide insight into a possible role for catecholamine activity in territorial song in female starlings. We presented females that were defending nest-cavities with an unfamiliar female and assessed song production. We then measured immunolabeling for phosphorylated tyrosine hydroxylase (pTH-ir), the rate-limiting enzyme for catecholamine synthesis, in brain regions in which catecholamines stimulate agonistic behavior. Females that sang had higher pTH-ir in the caudomedial ventral tegmental area and the lateral septum than females that did not sing. Furthermore, the number of songs produced correlated positively with pTH-ir in the medial preoptic nucleus. Phosphorylation of TH is thought to occur after catecholamine release, so these results link increased catecholamine activity in several brain regions governing agonistic behavior to territorial song production in females.
authors.affiliation: 426 Birge Hall, University of Wisconsin-Madison, Department of Zoology, 430 Lincoln Drive, Madison, WI 53706, USA,. Electronic address: jme29@cornell.edu.
authors.forename: Jesse M S
authors.initials: JM
authors.lastname: Ellis
authors.affiliation: 426 Birge Hall, University of Wisconsin-Madison, Department of Zoology, 430 Lincoln Drive, Madison, WI 53706, USA,. Electronic address: LVRiters@wisc.edu.
authors.forename: Lauren V
authors.initials: LV
authors.lastname: Riters
mesh_terms: D000818:Animals; D001921:Brain / Q000201:enzymology*; D005260:Female; D007150:Immunohistochemistry; D010766:Phosphorylation; D010784:Photomicrography; D046749:Starlings; D014446:Tyrosine 3-Monooxygenase / Q000378:metabolism*; D014828:Vocalization, Animal / Q000502:physiology*
chemical_list: D014446:Tyrosine 3-Monooxygenase