Activation of ganglionic tyrosine hydroxylase by peptides of the secretin-glucagon family: Structure-function studies

@article{Schwarzschild1989ActivationOG,
  title={Activation of ganglionic tyrosine hydroxylase by peptides of the secretin-glucagon family: Structure-function studies},
  author={M. Schwarzschild and W. Vale and A. Corigliano-Murphy and J. Pisano and R. Zigmond},
  journal={Neuroscience},
  year={1989},
  volume={31},
  pages={159-167}
}
The hydroxylation of tyrosine to dopa is the rate-limiting reaction in catecholamine biosynthesis. It has been previously reported that secretin, vasoactive intestinal peptide and peptide histidine isoleucine amide, all members of the secretin-glucagon family of peptides, increase dopa synthesis in superior cervical ganglia in vitro. We report here that two other members of this peptide family, rat growth hormone-releasing factor and helodermin H38, a component of Gila monster venom, also… Expand
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