Ser(13)-phosphorylated PYY from porcine intestine with a potent biological activity
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 I...
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| Veröffentlicht in: | FEBS letters 2001-03, Vol.492 (1-2), p.119-122 |
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| container_title | FEBS letters |
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| creator | Chen, Z Eriste, E Jonsson, A P Norberg, A Nepomuceno, D Lovenberg, T W Bergman, T Efendic, S Jörnvall, H Sillard, R |
| description | 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. |
| doi_str_mv | 10.1016/S0014-5793(01)02234-7 |
| format | Article |
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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.</description><identifier>ISSN: 0014-5793</identifier><identifier>DOI: 10.1016/S0014-5793(01)02234-7</identifier><identifier>PMID: 11248248</identifier><language>eng</language><publisher>England</publisher><subject>Amino Acid Sequence ; Animals ; Cyclic AMP - metabolism ; Humans ; Intestinal Mucosa - metabolism ; Peptide YY - chemistry ; Peptide YY - metabolism ; Phosphorylation ; Sequence Analysis, Protein ; Sequence Homology, Amino Acid ; Serine - metabolism ; Swine ; Tumor Cells, Cultured</subject><ispartof>FEBS letters, 2001-03, Vol.492 (1-2), p.119-122</ispartof><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27901,27902</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/11248248$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Chen, Z</creatorcontrib><creatorcontrib>Eriste, E</creatorcontrib><creatorcontrib>Jonsson, A P</creatorcontrib><creatorcontrib>Norberg, A</creatorcontrib><creatorcontrib>Nepomuceno, D</creatorcontrib><creatorcontrib>Lovenberg, T W</creatorcontrib><creatorcontrib>Bergman, T</creatorcontrib><creatorcontrib>Efendic, S</creatorcontrib><creatorcontrib>Jörnvall, H</creatorcontrib><creatorcontrib>Sillard, R</creatorcontrib><title>Ser(13)-phosphorylated PYY from porcine intestine with a potent biological activity</title><title>FEBS letters</title><addtitle>FEBS Lett</addtitle><description>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.</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Cyclic AMP - metabolism</subject><subject>Humans</subject><subject>Intestinal Mucosa - metabolism</subject><subject>Peptide YY - chemistry</subject><subject>Peptide YY - metabolism</subject><subject>Phosphorylation</subject><subject>Sequence Analysis, Protein</subject><subject>Sequence Homology, Amino Acid</subject><subject>Serine - metabolism</subject><subject>Swine</subject><subject>Tumor Cells, Cultured</subject><issn>0014-5793</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2001</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNo9UMtKAzEUzUKxtfoJSlbSLkbznMwspfgCQaG66GpIMndsZF4mqdK_N2IV7uG-zjlcLkJnlFxSQvOrFSFUZFKVfE7ogjDGRaYO0PR_PEHHIbyT1Be0PEITSpkoUkzRagV-TvkiGzdDSPC7Vkeo8fN6jRs_dHgcvHU9YNdHCPGn-nJxg3VaROgjNm5ohzdndYu1je7Txd0JOmx0G-B0n2fo9fbmZXmfPT7dPSyvH7ORERWzklLOgZUMZK0E01YpQ6StuREMmFGgmZCFlTo3xghomDBUci1o0SSdFXyGLn59Rz98bNN1VeeChbbVPQzbUKm8TL65TMTzPXFrOqir0btO-1319wb-DdvJXks</recordid><startdate>20010309</startdate><enddate>20010309</enddate><creator>Chen, Z</creator><creator>Eriste, E</creator><creator>Jonsson, A P</creator><creator>Norberg, A</creator><creator>Nepomuceno, D</creator><creator>Lovenberg, T W</creator><creator>Bergman, T</creator><creator>Efendic, S</creator><creator>Jörnvall, H</creator><creator>Sillard, R</creator><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>7X8</scope></search><sort><creationdate>20010309</creationdate><title>Ser(13)-phosphorylated PYY from porcine intestine with a potent biological activity</title><author>Chen, Z ; Eriste, E ; Jonsson, A P ; Norberg, A ; Nepomuceno, D ; Lovenberg, T W ; Bergman, T ; Efendic, S ; Jörnvall, H ; Sillard, R</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-p207t-91133e292e5d742ac77b05cd3b42e2b7ea2458c5a6bbb4ef24b153a418f33ec43</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2001</creationdate><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Cyclic AMP - metabolism</topic><topic>Humans</topic><topic>Intestinal Mucosa - metabolism</topic><topic>Peptide YY - chemistry</topic><topic>Peptide YY - metabolism</topic><topic>Phosphorylation</topic><topic>Sequence Analysis, Protein</topic><topic>Sequence Homology, Amino Acid</topic><topic>Serine - metabolism</topic><topic>Swine</topic><topic>Tumor Cells, Cultured</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Chen, Z</creatorcontrib><creatorcontrib>Eriste, E</creatorcontrib><creatorcontrib>Jonsson, A P</creatorcontrib><creatorcontrib>Norberg, A</creatorcontrib><creatorcontrib>Nepomuceno, D</creatorcontrib><creatorcontrib>Lovenberg, T W</creatorcontrib><creatorcontrib>Bergman, T</creatorcontrib><creatorcontrib>Efendic, S</creatorcontrib><creatorcontrib>Jörnvall, H</creatorcontrib><creatorcontrib>Sillard, R</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>MEDLINE - Academic</collection><jtitle>FEBS letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Chen, Z</au><au>Eriste, E</au><au>Jonsson, A P</au><au>Norberg, A</au><au>Nepomuceno, D</au><au>Lovenberg, T W</au><au>Bergman, T</au><au>Efendic, S</au><au>Jörnvall, H</au><au>Sillard, R</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Ser(13)-phosphorylated PYY from porcine intestine with a potent biological activity</atitle><jtitle>FEBS letters</jtitle><addtitle>FEBS Lett</addtitle><date>2001-03-09</date><risdate>2001</risdate><volume>492</volume><issue>1-2</issue><spage>119</spage><epage>122</epage><pages>119-122</pages><issn>0014-5793</issn><abstract>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.</abstract><cop>England</cop><pmid>11248248</pmid><doi>10.1016/S0014-5793(01)02234-7</doi><tpages>4</tpages></addata></record> |
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| ispartof | FEBS letters, 2001-03, Vol.492 (1-2), p.119-122 |
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| source | Wiley Free Content; MEDLINE; Wiley Online Library Journals Frontfile Complete; Elsevier ScienceDirect Journals; EZB-FREE-00999 freely available EZB journals; Alma/SFX Local Collection |
| subjects | Amino Acid Sequence Animals Cyclic AMP - metabolism Humans Intestinal Mucosa - metabolism Peptide YY - chemistry Peptide YY - metabolism Phosphorylation Sequence Analysis, Protein Sequence Homology, Amino Acid Serine - metabolism Swine Tumor Cells, Cultured |
| title | Ser(13)-phosphorylated PYY from porcine intestine with a potent biological activity |
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