C-terminal modifications of neuropeptide Y and its analogs leading to selectivity for the mouse brain receptor over the porcine spleen receptor

@article{Krstenansky1990CterminalMO,
  title={C-terminal modifications of neuropeptide Y and its analogs leading to selectivity for the mouse brain receptor over the porcine spleen receptor},
  author={John L Krstenansky and Thomas J. Owen and Marguerite H. Payne and S. A. Shatzer and Stephen H. Buck},
  journal={Neuropeptides},
  year={1990},
  volume={17},
  pages={117-120}
}
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Centrally truncated neuropeptide Y analog acts as an agonist for Y1 receptors on SK-N-MC cells
Activation of neuropeptide Y1 and neuropeptide Y2 receptors by substituted and truncated neuropeptide Y analogs: identification of signal epitopes.
Evaluation of truncated neuropeptide Y analogues with modifications of the tyrosine residue in position 1 on Y1, Y2 and Y3 receptor sub-types.
Design of the Y1-receptor-selective cyclic peptide based on the C-terminal sequence of neuropeptide Y.
TLDR
Four cyclic peptides which are mimics of the C-terminal region of human neuropeptide Y (NPY) on the basis of the structural model of NPY exhibited significantly higher affinity for the Y1-receptor than the corresponding C- terminate linear fragment, NPY Ac-28-36.
Characterization of neuropeptide Y (NPY) receptors in human cerebral arteries with selective agonists and the new Y1 antagonist BIBP 3226
TLDR
It is concluded that Y1 receptors exclusively, mediate the NPY‐induced contraction in human cerebral arteries and BIBP 3226 is a potent and competitive antagonist of this Y1‐mediated vasoconstriction.
Chapter 6 – The importance of various parts of the NPY molecule for receptor recognition
Neuropeptide Y-related peptides and their receptors--are the receptors potential therapeutic drug targets?
TLDR
It has been appreciated that NPY may also be an important messenger in its own right , perhaps particularly in the brain, where NP Y has been frequently used to study cotransmission, particularly in its relation to the "classical" neurotransmitter norepinephrine.
Activity of centrally truncated analogues of neuropeptide Y at Y1 and Y2 receptor subtypes in vivo
Benextramine-neuropeptide Y (NPY) binding site interactions: Characterization of 3H-NPY binding site heterogeneity in rat brain
Multiple neuropeptide Y receptors are involved in cardiovascular regulation. Peripheral and central mechanisms.
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References

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TLDR
It is concluded that [Leu31, Pro34]NPY is a specific Y1 receptor agonist and that the analog or variants of it can be useful in delineating the physiological importance of Y1 receptors.
Y1 and Y2 receptors for neuropeptide Y
Centrally truncated and stabilized porcine neuropeptide Y analogs: design, synthesis, and mouse brain receptor binding.
TLDR
It is proposed that the central region of pNPY serves a structural role in the peptide and is not involved in direct receptor interaction.
125I-neuropeptide Y and 125I-peptide YY bind to multiple receptor sites in rat brain.
TLDR
It is proposed that rat brain contains a minor population of high affinity NPY binding sites with an intermediate dissociation rate and no sensitivity to Gpp(NH)p, a nonhydrolyzable analog of GTP.
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Data is presented supporting the unexpected finding of two fragments of NPY, NPY17-36 and NPT18-36 with substantial hypotensive action in vivo, which suggests that both NPY and NPY 18-36 assume an ordered conformation upon reaching the lipid rich receptor environment.
Synthesis and hypertensive activity of neuropeptide Y fragments and analogues with modified N- or C-termini or D-substitutions.
TLDR
Data indicate that an essentially full-length, C-terminally amidated NPY structure is required for the hypertensive activity observed in conscious rats upon intraarterial administration of NPY and NPY analogues.
Evidence for different pre- and post-junctional receptors for neuropeptide Y and related peptides
Neuropeptide Y receptor in pig spleen: binding characteristics, reduction of cyclic AMP formation and calcium antagonist inhibition of vasoconstriction.
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TLDR
The results suggest the existence of three distinct types of tachykinin receptors: SP-P, SP-E, and SP-K.
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