A new molecular form of PYY: Structural characterization of human PYY(3–36) and PYY(1–36)

@article{Eberlein1989ANM,
  title={A new molecular form of PYY: Structural characterization of human PYY(3–36) and PYY(1–36)},
  author={Gert A. Eberlein and Viktor E. Eysselein and M Schaeffer and Peter Layer and Daniel Grandt and Harald Goebell and Wolfgang Niebel and Mike T. Davis and Terry D. Lee and John E. Shively and Joseph R. Reeve},
  journal={Peptides},
  year={1989},
  volume={10},
  pages={797-803}
}
PYY(1-36) is the major form of PYY in rat distal small intestine: Quantification using high-resolution mass spectrometry
Processing and metabolism of peptide-YY: pivotal roles of dipeptidylpeptidase-IV, aminopeptidase-P, and endopeptidase-24.11.
TLDR
The relative levels of the three membrane peptidases at different tissue locations and on different cell types may play a pivotal role in postsecretory processing and metabolism of PYY to receptor-selective agonists or inactive metabolites.
Novel generation of hormone receptor specificity by amino terminal processing of peptide YY.
Mass spectrometry-assisted confirmation of the inability of dipeptidyl peptidase-4 to cleave goldfish peptide YY(1–36) and the lack of anorexigenic effects of peptide YY(3–36) in goldfish (Carassius auratus)
TLDR
The novel results indicate that DPP4 is unable to cleave goldfish PYY(1–36) to PYY[3–36] in vitro, and confirms a previously held hypothesis that D PP4 is Unable to Cleave fish PYY (1– 36) that contains N-terminal proline–proline residues.
Structural and functional characterization of peptide YY on feeding in Schizothorax davidi.
TLDR
The full-length cDNA sequence of PYY in S. davidi is identified for the first time and it is suggested that it might function as a satiety factor in S .
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References

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Syntheses and receptor affinities of partial sequences of peptide YY (PYY).
TLDR
This investigation has resulted in identifying the receptor binding region of PYY, which may prove useful in designing agonistic and antagonistic peptides not only for PYY but also for other structurally related hormones such as NPY.
Characterization of peptide YY receptors in the brain.
TLDR
The identity in the size of NPY and PYY receptors together with their similarities in binding properties including regional distribution and peptide specificity, indicate that NPYand PYY regulate brain function through interaction at a common receptor site.
Molecular structure of mammalian neuropeptide Y: analysis by molecular cloning and computer-aided comparison with crystal structure of avian homologue.
TLDR
It is suggested that neuropeptide preserves a compact tertiary structure characterized by extensive hydrophobic interactions between an N- terminal polyproline-II-like helix and a C-terminal alpha-helix.
Cloning, characterization, and DNA sequence of a human cDNA encoding neuropeptide tyrosine.
In vitro translation of the RNA isolated from a human pheochromocytoma demonstrated that this tumor contained a mRNA encoding a 10.5-kDa protein, which was immunoprecipitated with antiserum raised
Isolation and characterization of peptide YY (PYY), a candidate gut hormone that inhibits pancreatic exocrine secretion.
  • K. Tatemoto
  • Biology, Chemistry
    Proceedings of the National Academy of Sciences of the United States of America
  • 1982
TLDR
PYY has been found to strongly inhibit both secretin- and cholecystokinin-stimulated pancreatic secretion in the anesthetized cat and is proposed to form a new peptide family together with the pancreatic polypeptide.
Isolation of two novel candidate hormones using a chemical method for finding naturally occurring polypeptides
TLDR
A chemical detection system based on fragmentation of peptides in tissue extracts followed by identification of certain of these peptide fragments having distinct chemical features is proposed and several previously unknown peptide amides in porcine upper small intestinal tissues are found.
Neuropeptide Y: complete amino acid sequence of the brain peptide.
  • K. Tatemoto
  • Biology, Chemistry
    Proceedings of the National Academy of Sciences of the United States of America
  • 1982
TLDR
Neuropeptide Y has a high degree of sequence homology with peptide YY, the newly isolated porcine intestinal peptide, and pancreatic polypeptides, and it is proposed that neuropeptid Y, peptideYY, and pancreptide are members of a newly recognized peptide family.
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