title: Expression of ecto-nucleoside triphosphate diphosphohydrolase3 (NTPDase3) in the female rat brain during postnatal development.
abstract: Nucleoside triphosphate diphosphohydrolase3 (NTPDase3) is membrane-bound ecto-enzyme which hydrolyzes extracellular ATP, thus modulating the function of purinergic receptors and the pattern of purinergic signaling. Here we analyzed the developmental expression of NTPDase3 in female hypothalamus, cerebral cortex and hippocampal formation at different postnatal ages (PD7-PD90) by qRT-PCR and immunohistochemistry. In hypothalamus and hippocampus, a similar developmental profile was seen: NTPDase3 gene expression was stable during postnatal development and increased in adults. In the cortex, upregulation of NTPDase3 mRNA expression was seen at PD15 and further increase was evidenced in adults. Immunohistochemical analysis at PD7 revealed faint neuronal NTPDase3 localization in a dorsal hypothalamus. The immunoreactivity (ir) gradually increased in PD15 and PD20, in clusters of cells in the lateral, ventral and dorsomedial hypothalamus. Furthermore, in PD20 animals, NTPDase3-ir was detected on short fibers in the posterior hypothalamic area, while in PD30 the fibers appeared progressively longer and markedly varicose. In adults, the strongest NTPDase3-ir was observed in collections of cells in dorsomedial hypothalamic nucleus, dorsal and lateral hypothalamus and in several thalamic areas, whereas the varicose fibers traversed entire diencephalon, particularly paraventricular thalamic nucleus, ventromedial and dorsomedial hypothalamic nuclei, the arcuate nucleus and the prefornical part of the lateral hypothalamus. The presumably ascending NTPDase3-ir fibers were first observed in PD20; their density and the varicose appearance increased until the adulthood. Prominent enhancement of NTPDase3-ir in the hypothalamus coincides with age when animals acquire diurnal rhythms of sleeping and feeding, supporting the hypothesis that this enzyme may be involved in regulation of homeostatic functions.
authors.affiliation: Department of Molecular Biology and Endocrinology, VINČA Institute of Nuclear Sciences, University of Belgrade, Belgrade, Serbia. Electronic address: istanojevic@vinca.rs.
authors.forename: Ivana
authors.initials: I
authors.lastname: Grković
authors.affiliation: Institute for Biological Research "Siniša Stanković," University of Belgrade, Belgrade, Serbia.
authors.forename: Ivana
authors.initials: I
authors.lastname: Bjelobaba
authors.affiliation: Department of Molecular Biology and Endocrinology, VINČA Institute of Nuclear Sciences, University of Belgrade, Belgrade, Serbia.
authors.forename: Nataša
authors.initials: N
authors.lastname: Mitrović
authors.affiliation: Institute for Biological Research "Siniša Stanković," University of Belgrade, Belgrade, Serbia.
authors.forename: Irena
authors.initials: I
authors.lastname: Lavrnja
authors.affiliation: Department of Molecular Biology and Endocrinology, VINČA Institute of Nuclear Sciences, University of Belgrade, Belgrade, Serbia.
authors.forename: Dunja
authors.initials: D
authors.lastname: Drakulić
authors.affiliation: Department of Molecular Biology and Endocrinology, VINČA Institute of Nuclear Sciences, University of Belgrade, Belgrade, Serbia.
authors.forename: Jelena
authors.initials: J
authors.lastname: Martinović
authors.affiliation: Department of Molecular Biology and Endocrinology, VINČA Institute of Nuclear Sciences, University of Belgrade, Belgrade, Serbia.
authors.forename: Miloš
authors.initials: M
authors.lastname: Stanojlović
authors.affiliation: Department of Molecular Biology and Endocrinology, VINČA Institute of Nuclear Sciences, University of Belgrade, Belgrade, Serbia.
authors.forename: Anica
authors.initials: A
authors.lastname: Horvat
authors.affiliation: Institute for Physiology and Biochemistry, Faculty of Biology, University of Belgrade, Belgrade, Serbia.
authors.forename: Nadežda
authors.initials: N
authors.lastname: Nedeljković
mesh_terms: D000375:Aging / Q000378:metabolism; D000818:Animals; D001921:Brain / Q000201:enzymology / Q000254:growth & development; D001923:Brain Chemistry; D005247:Feeding Behavior / Q000502:physiology; D005260:Female; D018507:Gene Expression Regulation, Developmental / Q000235:genetics*; D015971:Gene Expression Regulation, Enzymologic / Q000235:genetics*; D007031:Hypothalamus / Q000201:enzymology / Q000254:growth & development; D009412:Nerve Fibers / Q000201:enzymology; D011755:Pyrophosphatases / Q000096:biosynthesis* / Q000235:genetics*; D012333:RNA, Messenger / Q000096:biosynthesis / Q000235:genetics; D051381:Rats; D017208:Rats, Wistar; D012890:Sleep / Q000502:physiology; D013347:Subcellular Fractions / Q000201:enzymology
chemical_list: D012333:RNA, Messenger; D011755:Pyrophosphatases; C439652:nucleoside-triphosphate diphosphohydrolase 3
keywords: Ecto-nucleoside triphosphate diphosphohydrolase (NTPDase3); Feeding/sleeping behavior; Hypothalamus; Postnatal development; Varicose fibers