High impact information on PYY

• The extremely high degree of homology to the peptide YY gene, in both coding and especially noncoding regions, suggests that the seminalplasmin gene has arisen by a very recent gene duplication of the bovine peptide YY gene [1].
• The rank order of potency for inhibition of tyrosine hydroxylase activity is NPY > or = [Leu31,Pro34]NPY > or = peptide YY > NPY2-36 > NPY13-36 > NPY18-36 > or = NPY26-36 >> NPY1-30, suggesting a NPY-Y1 receptor subtype [2].
• Immunocytochemical evidence for a substance related to the bovine pancreatic polypeptide-peptide YY group of peptides in the human fetal gastrointestinal tract [3].
• Unlabeled NPY or PYY, but not BPP, HPP and APP, inhibited labeling of [125I]NPY to the 50 kDa protein band [4].
• The unexpected presence of MENK8 in all glandular regions of the stomach and PYY in the small intestine was also noted [5].

Biological context of PYY

• NPY, Y1RL, and PYY displayed a concentration that inhibits the specific binding by 50% IC50 (nM) values of 4.06 +/- 1.66 (n = 4), 2.94 +/- 0.75 (n = 5), and 18.36 +/- 10.36 (n = 3), respectively [6].

Anatomical context of PYY

• The study indicates a modulatory role for NPY, PYY and bPP in synaptic interactions within the enteric nervous system [7].
• Saturation and competition binding data with PYY, NPY-(18-36) and NPY itself fit with a single class of sites: for the radioligand KD = 1.4 +/- 0.5 nM, Bmax = 434 +/- 180 fmol/mg protein in frontal cortex, KD = 0.7 +/- 0.2 nM, Bmax = 267 +/- 50 fmol/mg protein in hippocampus [8].

Associations of PYY with chemical compounds

• 4. The results suggest that NPY, PYY and bPP, but not aPP, act presynaptically to inhibit acetylcholine release from myenteric neurones of the gastric corpus, thereby suppressing fEPSPs [7].

References