Receptors on phaeochromocytoma cells for two members of the PP-fold family — NPY and PP
Pancreatic polypeptide (PP) and neuropeptide Y (NPY) belong to a family of regulatory peptides which hold a distinct tertiary structure, the PP-fold, even in dilute aqueous solution. High-affinity receptors, specific for both PP and NPY, are described on the rat phaeochromocytoma cell line, PC-12. T...
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| Veröffentlicht in: | FEBS letters 1987-12, Vol.225 (1), p.209-214 |
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| creator | Schwartz, Thue W. Sheikh, Søren P. O'Hare, Mairead M.T. |
| description | Pancreatic polypeptide (PP) and neuropeptide Y (NPY) belong to a family of regulatory peptides which hold a distinct tertiary structure, the PP-fold, even in dilute aqueous solution. High-affinity receptors, specific for both PP and NPY, are described on the rat phaeochromocytoma cell line, PC-12. The binding of [
125I-Tyr
36]PP to PC-12 cells was inhibited by concentrations of unlabeled PP which correspond to physiological concentrations of the hormone, 10
−11-10
−9 mol/1. The affinity of the receptor for the neuropeptide, NPY, was 10
2-times lower than that of the PP receptor. C-terminal fragments of both PP (PP
24–36) and NPY (NPY
13–36) were between 10
2 - and 10
3-times less potent in displacing the radiolabeled 36-amino-acid peptides from their respective receptors. It is concluded that PC-12 cells are suited for structure-function studies of the PP-fold peptides and studies on the cellular events following cellular binding of PP-fold peptides. |
| doi_str_mv | 10.1016/0014-5793(87)81159-6 |
| format | Article |
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125I-Tyr
36]PP to PC-12 cells was inhibited by concentrations of unlabeled PP which correspond to physiological concentrations of the hormone, 10
−11-10
−9 mol/1. The affinity of the receptor for the neuropeptide, NPY, was 10
2-times lower than that of the PP receptor. C-terminal fragments of both PP (PP
24–36) and NPY (NPY
13–36) were between 10
2 - and 10
3-times less potent in displacing the radiolabeled 36-amino-acid peptides from their respective receptors. It is concluded that PC-12 cells are suited for structure-function studies of the PP-fold peptides and studies on the cellular events following cellular binding of PP-fold peptides.</description><identifier>ISSN: 0014-5793</identifier><identifier>EISSN: 1873-3468</identifier><identifier>DOI: 10.1016/0014-5793(87)81159-6</identifier><identifier>PMID: 2826239</identifier><identifier>CODEN: FEBLAL</identifier><language>eng</language><publisher>Amsterdam: Elsevier B.V</publisher><subject>3-Dimensional peptide structure ; Adrenal Gland Neoplasms - metabolism ; Animals ; Binding, Competitive ; Biological and medical sciences ; Cell receptors ; Cell structures and functions ; Fundamental and applied biological sciences. Psychology ; Iodine Radioisotopes ; Kinetics ; Molecular and cellular biology ; Monoiodotyrosine ; neuropeptide ; Neuropeptide Y ; Neuropeptide Y - metabolism ; pancreatic peptide ; Pancreatic polypeptide ; Pancreatic Polypeptide - metabolism ; PC-12 cell ; Peptide Fragments - metabolism ; Pheochromocytoma - metabolism ; pheochromocytoma cells ; Rats ; Receptors, Gastrointestinal Hormone - metabolism ; Receptors, Neuropeptide Y ; Receptors, Neurotransmitter - metabolism ; Tumor Cells, Cultured</subject><ispartof>FEBS letters, 1987-12, Vol.225 (1), p.209-214</ispartof><rights>1987</rights><rights>FEBS Letters 225 (1987) 1873-3468 © 2015 Federation of European Biochemical Societies</rights><rights>1988 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4416-c2b3421595629e1d1dcc1f035d7ffa821fb1d727755ff08db5f65c5ec8c463c53</citedby><cites>FETCH-LOGICAL-c4416-c2b3421595629e1d1dcc1f035d7ffa821fb1d727755ff08db5f65c5ec8c463c53</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/0014579387811596$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>314,776,780,3536,27903,27904,65309</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=7778135$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/2826239$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Schwartz, Thue W.</creatorcontrib><creatorcontrib>Sheikh, Søren P.</creatorcontrib><creatorcontrib>O'Hare, Mairead M.T.</creatorcontrib><title>Receptors on phaeochromocytoma cells for two members of the PP-fold family — NPY and PP</title><title>FEBS letters</title><addtitle>FEBS Lett</addtitle><description>Pancreatic polypeptide (PP) and neuropeptide Y (NPY) belong to a family of regulatory peptides which hold a distinct tertiary structure, the PP-fold, even in dilute aqueous solution. High-affinity receptors, specific for both PP and NPY, are described on the rat phaeochromocytoma cell line, PC-12. The binding of [
125I-Tyr
36]PP to PC-12 cells was inhibited by concentrations of unlabeled PP which correspond to physiological concentrations of the hormone, 10
−11-10
−9 mol/1. The affinity of the receptor for the neuropeptide, NPY, was 10
2-times lower than that of the PP receptor. C-terminal fragments of both PP (PP
24–36) and NPY (NPY
13–36) were between 10
2 - and 10
3-times less potent in displacing the radiolabeled 36-amino-acid peptides from their respective receptors. It is concluded that PC-12 cells are suited for structure-function studies of the PP-fold peptides and studies on the cellular events following cellular binding of PP-fold peptides.</description><subject>3-Dimensional peptide structure</subject><subject>Adrenal Gland Neoplasms - metabolism</subject><subject>Animals</subject><subject>Binding, Competitive</subject><subject>Biological and medical sciences</subject><subject>Cell receptors</subject><subject>Cell structures and functions</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Iodine Radioisotopes</subject><subject>Kinetics</subject><subject>Molecular and cellular biology</subject><subject>Monoiodotyrosine</subject><subject>neuropeptide</subject><subject>Neuropeptide Y</subject><subject>Neuropeptide Y - metabolism</subject><subject>pancreatic peptide</subject><subject>Pancreatic polypeptide</subject><subject>Pancreatic Polypeptide - metabolism</subject><subject>PC-12 cell</subject><subject>Peptide Fragments - metabolism</subject><subject>Pheochromocytoma - metabolism</subject><subject>pheochromocytoma cells</subject><subject>Rats</subject><subject>Receptors, Gastrointestinal Hormone - metabolism</subject><subject>Receptors, Neuropeptide Y</subject><subject>Receptors, Neurotransmitter - metabolism</subject><subject>Tumor Cells, Cultured</subject><issn>0014-5793</issn><issn>1873-3468</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1987</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkM-O0zAQxi0EWroLbwCSDwgth0Bsx39yQYLVFpBWUCE47Mly7LFqlMTFTln1xkPwhDwJcVv1CJwsz_ebmW8-hJ6Q-iWpiXhV16SpuGzZpZIvFCG8rcQ9tCBKsoo1Qt1HixPyEJ3n_K2e_4q0Z-iMKiooaxfo9jNY2EwxZRxHvFkbiHad4hDtboqDwRb6PmMfE57uIh5g6KCgHk9rwKtV5WPvsDdD6Hf4989f-OPqFpvRzdIj9MCbPsPj43uBvi6vv1y9r24-vftw9eamsk1DRGVpxxo6m-eCtkAccdYSXzPupPdGUeI74iSVknPva-U67gW3HKyyjWCWswv0_DB3k-L3LeRJDyEX22aEuM1aSqX4fO4_QdIoIckebA6gTTHnBF5vUhhM2mlS6xK9LrnqkqtWUu-j16Xt6XH-thvAnZqOWc_6s6NusjW9T2a0IZ8wORslrNyzPGB3oYfdf63Wy-u3tAilruS-Wvy8PgyCOf0fAZLONsBowYUEdtIuhr8f9AdyF7Jh</recordid><startdate>19871210</startdate><enddate>19871210</enddate><creator>Schwartz, Thue W.</creator><creator>Sheikh, Søren P.</creator><creator>O'Hare, Mairead M.T.</creator><general>Elsevier B.V</general><general>Elsevier</general><scope>6I.</scope><scope>AAFTH</scope><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>8FD</scope><scope>FR3</scope><scope>M7Z</scope><scope>P64</scope><scope>7X8</scope></search><sort><creationdate>19871210</creationdate><title>Receptors on phaeochromocytoma cells for two members of the PP-fold family — NPY and PP</title><author>Schwartz, Thue W. ; Sheikh, Søren P. ; O'Hare, Mairead M.T.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4416-c2b3421595629e1d1dcc1f035d7ffa821fb1d727755ff08db5f65c5ec8c463c53</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1987</creationdate><topic>3-Dimensional peptide structure</topic><topic>Adrenal Gland Neoplasms - metabolism</topic><topic>Animals</topic><topic>Binding, Competitive</topic><topic>Biological and medical sciences</topic><topic>Cell receptors</topic><topic>Cell structures and functions</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Iodine Radioisotopes</topic><topic>Kinetics</topic><topic>Molecular and cellular biology</topic><topic>Monoiodotyrosine</topic><topic>neuropeptide</topic><topic>Neuropeptide Y</topic><topic>Neuropeptide Y - metabolism</topic><topic>pancreatic peptide</topic><topic>Pancreatic polypeptide</topic><topic>Pancreatic Polypeptide - metabolism</topic><topic>PC-12 cell</topic><topic>Peptide Fragments - metabolism</topic><topic>Pheochromocytoma - metabolism</topic><topic>pheochromocytoma cells</topic><topic>Rats</topic><topic>Receptors, Gastrointestinal Hormone - metabolism</topic><topic>Receptors, Neuropeptide Y</topic><topic>Receptors, Neurotransmitter - metabolism</topic><topic>Tumor Cells, Cultured</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Schwartz, Thue W.</creatorcontrib><creatorcontrib>Sheikh, Søren P.</creatorcontrib><creatorcontrib>O'Hare, Mairead M.T.</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>Biochemistry Abstracts 1</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>FEBS letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Schwartz, Thue W.</au><au>Sheikh, Søren P.</au><au>O'Hare, Mairead M.T.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Receptors on phaeochromocytoma cells for two members of the PP-fold family — NPY and PP</atitle><jtitle>FEBS letters</jtitle><addtitle>FEBS Lett</addtitle><date>1987-12-10</date><risdate>1987</risdate><volume>225</volume><issue>1</issue><spage>209</spage><epage>214</epage><pages>209-214</pages><issn>0014-5793</issn><eissn>1873-3468</eissn><coden>FEBLAL</coden><abstract>Pancreatic polypeptide (PP) and neuropeptide Y (NPY) belong to a family of regulatory peptides which hold a distinct tertiary structure, the PP-fold, even in dilute aqueous solution. High-affinity receptors, specific for both PP and NPY, are described on the rat phaeochromocytoma cell line, PC-12. The binding of [
125I-Tyr
36]PP to PC-12 cells was inhibited by concentrations of unlabeled PP which correspond to physiological concentrations of the hormone, 10
−11-10
−9 mol/1. The affinity of the receptor for the neuropeptide, NPY, was 10
2-times lower than that of the PP receptor. C-terminal fragments of both PP (PP
24–36) and NPY (NPY
13–36) were between 10
2 - and 10
3-times less potent in displacing the radiolabeled 36-amino-acid peptides from their respective receptors. It is concluded that PC-12 cells are suited for structure-function studies of the PP-fold peptides and studies on the cellular events following cellular binding of PP-fold peptides.</abstract><cop>Amsterdam</cop><pub>Elsevier B.V</pub><pmid>2826239</pmid><doi>10.1016/0014-5793(87)81159-6</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | FEBS letters, 1987-12, Vol.225 (1), p.209-214 |
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| language | eng |
| recordid | cdi_proquest_miscellaneous_77885826 |
| source | MEDLINE; Elsevier ScienceDirect Journals; EZB-FREE-00999 freely available EZB journals; Alma/SFX Local Collection |
| subjects | 3-Dimensional peptide structure Adrenal Gland Neoplasms - metabolism Animals Binding, Competitive Biological and medical sciences Cell receptors Cell structures and functions Fundamental and applied biological sciences. Psychology Iodine Radioisotopes Kinetics Molecular and cellular biology Monoiodotyrosine neuropeptide Neuropeptide Y Neuropeptide Y - metabolism pancreatic peptide Pancreatic polypeptide Pancreatic Polypeptide - metabolism PC-12 cell Peptide Fragments - metabolism Pheochromocytoma - metabolism pheochromocytoma cells Rats Receptors, Gastrointestinal Hormone - metabolism Receptors, Neuropeptide Y Receptors, Neurotransmitter - metabolism Tumor Cells, Cultured |
| title | Receptors on phaeochromocytoma cells for two members of the PP-fold family — NPY and PP |
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