Nuclear-cytoplasmic localization of acetyl coenzyme a synthetase-1 in the rat brain.
Acetyl coenzyme A synthetase-1 (AceCS1) catalyzes the synthesis of acetyl coenzyme A from acetate and coenzyme A and is thought to play diverse roles ranging from fatty acid synthesis to gene regulation. By using an affinity-purified antibody generated against an 18-mer peptide sequence of AceCS1 and a polyclonal antibody directed against recombinant AceCS1 protein, we examined the expression of AceCS1 in the rat brain. AceCS1 immunoreactivity in the adult rat brain was present predominantly in cell nuclei, with only light to moderate cytoplasmic staining in some neurons, axons, and oligodendrocytes. Some nonneuronal cell nuclei were very strongly immunoreactive, including those of some oligodendrocytes, whereas neuronal nuclei ranged from unstained to moderately stained. Both antibodies stained some neuronal cell bodies and axons, especially in the hindbrain. AceCS1 immunoreactivity was stronger and more widespread in the brains of 18-day-old rats than in adults, with increased expression in oligodendrocytes and neurons, including cortical pyramidal cells. Expression of AceCS1 was substantially up-regulated in neurons throughout the brain after controlled cortical impact injury. The strong AceCS1 expression observed in the nuclei of CNS cells during brain development and after injury is consistent with a role in nuclear histone acetylation and therefore the regulation of chromatin structure and gene expression. The cytoplasmic staining observed in some oligodendrocytes, especially during postnatal brain development, suggests an additional role in CNS lipid synthesis and myelination. Neuronal and axonal localization implicates AceCS1 in cytoplasmic acetylation reactions in some neurons.
Department of Anatomy, Molecular and Cell Biology Program and Neuroscience Program, Uniformed Services University of the Health Sciences, Bethesda, Maryland 20814, USA.
Prasanth S
PS
Ariyannur
John R
JR
Moffett
Chikkathur N
CN
Madhavarao
Peethambaran
P
Arun
Nisha
N
Vishnu
David M
DM
Jacobowitz
William C
WC
Hallows
John M
JM
Denu
Aryan M A
AM
Namboodiri
D000818:Animals; D015153:Blotting, Western; D001921:Brain / Q000033:anatomy & histology / Q000201:enzymology*; D001930:Brain Injuries / Q000201:enzymology; D002467:Cell Nucleus / Q000201:enzymology*; D002540:Cerebral Cortex / Q000293:injuries; D002846:Chromatography, Affinity; D003066:Coenzyme A Ligases / Q000096:biosynthesis*; D003593:Cytoplasm / Q000201:enzymology*; D004591:Electrophoresis, Polyacrylamide Gel; D005260:Female; D005904:Glial Fibrillary Acidic Protein / Q000378:metabolism; D007124:Immunoenzyme Techniques; D007150:Immunohistochemistry; D047468:Immunoprecipitation; D008297:Male; D008969:Molecular Sequence Data; D009412:Nerve Fibers / Q000201:enzymology; D009434:Neural Pathways / Q000166:cytology / Q000201:enzymology; D051381:Rats; D017207:Rats, Sprague-Dawley; D017208:Rats, Wistar
D005904:Glial Fibrillary Acidic Protein; D003066:Coenzyme A Ligases; C561832:Acsl1 protein, rat