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Immunohistochemical analysis of a novel dehydroepiandrosterone sulfotransferase-like protein in Drosophila neural circuits
- Source :
- Biochemical and Biophysical Research Communications. 367:14-20
- Publication Year :
- 2008
- Publisher :
- Elsevier BV, 2008.
-
Abstract
- Sulfotransferase (ST)-catalyzed sulfation plays an important role in various neuronal functions such as homeostasis of catecholamine neurotransmitters and hormones. Drosophila is a popular model for the study of memory and behavioral manifestations because it is able to mimic the intricate neuroregulation and recognition in humans. However, there has been no evidence indicating that cytosolic ST(s) is(are) present in Drosophila. The aim of this study is to investigate whether or not cytosolic ST(s) is(are) expressed in the Drosophila nervous system. Immunoblot analysis demonstrated the presence of dehydroepiandrosterone (DHEA) ST-like protein in Drosophila brain and a sensitive fluorometric assay revealed its sulfating activity toward DHEA. Immunohistochemical staining demonstrated this DHEA ST-like protein to be abundant in specific neurons as well as in several bundles of nerve fibers in Drosophila. Clarification of a possible link between ST and a neurotransmitter-mediated effect may eventually aid in designing approaches for alleviating neuronal disorders in humans.
- Subjects :
- Nervous system
medicine.medical_specialty
Sulfotransferase
Neuroregulation
Biophysics
Dehydroepiandrosterone
Biology
Models, Biological
Biochemistry
Catalysis
Catecholamines
Sulfation
Memory
Internal medicine
medicine
Animals
Homeostasis
Humans
Molecular Biology
Neuropharmacology
Neurons
Neurotransmitter Agents
Neurodegenerative Diseases
Cell Biology
Immunohistochemistry
Hormones
Cell biology
medicine.anatomical_structure
Endocrinology
Catecholamine
Drosophila
Sulfotransferases
medicine.drug
Subjects
Details
- ISSN :
- 0006291X
- Volume :
- 367
- Database :
- OpenAIRE
- Journal :
- Biochemical and Biophysical Research Communications
- Accession number :
- edsair.doi.dedup.....1abe864a6ced477b54b7b7ed11d30c02
- Full Text :
- https://doi.org/10.1016/j.bbrc.2007.12.082