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Ser 13 ‐phosphorylated PYY from porcine intestine with a potent biological activity
Author(s) -
Chen Zheng-wang,
Eriste Elo,
Jonsson Andreas P.,
Norberg Åke,
Nepomuceno Diane,
Lovenberg Timothy W.,
Bergman Tomas,
Efendic Suad,
Jörnvall Hans,
Sillard Rannar
Publication year - 2001
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(01)02234-7
Subject(s) - peptide yy , neuropeptide y receptor , phosphorylation , chemistry , receptor , forskolin , peptide , endocrinology , medicine , gastrointestinal hormone , mole , peptide hormone , microbiology and biotechnology , biology , neuropeptide , biochemistry
We have isolated a posttranslationally modified form of peptide YY (PYY) from porcine intestine and shown by MALDI‐TOF and electrospray tandem mass spectrometry that it is phosphorylated at Ser 13 . Phospho‐PYY exhibits high affinity for binding to neuropeptide Y (NPY) receptors Y1, Y2 and Y5. The IC 50 values with the Y1, Y2, and Y5 receptor subtypes were for NPY 2.4, 3.1, and 3.3 nM, for PYY 2.3, 0.94, and 3.2 nM, and for phospho‐PYY 4.6, 2.2, and 5.5 nM, respectively. Phospho‐PYY potently inhibits forskolin‐stimulated cAMP accumulation in SK‐N‐MC cells with an IC 50 value of 0.5 nM compared to 0.15 nM for non‐phosphorylated PYY. The finding of phosphorylation of PYY is unusual among hormonal peptides, and emphasizes the importance of direct protein analysis of gene products.