title: Trans-synaptic increase in RNA coding for tyrosine hydroxylase in a rat sympathetic ganglion.
abstract: To begin examining molecular mechanisms underlying trans-synaptic regulation, tyrosine hydroxylase (TH) and its messenger RNA (mRNA) were examined in the superior cervical sympathetic ganglion (SCG) of adult rats. Basal levels of TH mRNA were detectable in control ganglia by RNA dot hybridization, using the 32P nick translated PstI-KpnI restriction fragment of pTH.4 as a probe. Reserpine induced a 3-fold rise in TH activity per microgram protein, and a simultaneous 3-fold increase in ganglion TH mRNA. As expected, ganglion decentralization (denervation) prevented the trans-synaptic induction of TH. In addition, decentralization prevented the increase in TH mRNA, suggesting that the increase in message was dependent on trans-synaptic stimulation. Northern blot analysis indicated that the cDNA (complementary DNA) probe hybridized to a single band of approximately 1900 nucleotides, which was the same size in all ganglia. Our observations indicate that induction of TH is associated with a trans-synaptic increase in mRNA coding for the enzyme. Consequently, trans-synaptic increases in impulse activity may induce TH by increasing neuronal levels of TH mRNA in the SCG.
authors.forename: I B
authors.initials: IB
authors.lastname: Black
authors.forename: D M
authors.initials: DM
authors.lastname: Chikaraishi
authors.forename: E J
authors.initials: EJ
authors.lastname: Lewis
mesh_terms: D000818:Animals; D004247:DNA / Q000032:analysis; D004790:Enzyme Induction; D005260:Female; D005728:Ganglia, Sympathetic / Q000201:enzymology*; D008297:Male; D009693:Nucleic Acid Hybridization; D012333:RNA, Messenger / Q000032:analysis*; D051381:Rats; D011919:Rats, Inbred Strains; D012110:Reserpine / Q000494:pharmacology; D013569:Synapses / Q000502:physiology*; D009435:Synaptic Transmission; D014446:Tyrosine 3-Monooxygenase / Q000096:biosynthesis*
chemical_list: D012333:RNA, Messenger; D012110:Reserpine; D004247:DNA; D014446:Tyrosine 3-Monooxygenase