Atriopeptins: A family of potent biologically active peptides derived from mammalian atria
Extracts of rat atria are potent stimulators of sodium and urine excretion, and relax vascular and intestinal smooth muscle preparations. The structures of six biologically active peptides obtained from atrial extracts are reported here. Ion exchange chromatography of a low molecular weight fraction...
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| Veröffentlicht in: | Biochemical and biophysical research communications 1984-04, Vol.120 (2), p.333-338 |
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| creator | Geller, D.M. Currie, M.G. Wakitani, K. Cole, B.R. Adams, S.P. Fok, K.F. Siegel, N.R. Eubanks, S.R. Galluppi, G.R. Needleman, P. |
| description | Extracts of rat atria are potent stimulators of sodium and urine excretion, and relax vascular and intestinal smooth muscle preparations. The structures of six biologically active peptides obtained from atrial extracts are reported here. Ion exchange chromatography of a low molecular weight fraction obtained by gel filtration of atrial extracts produced two natriuretic fractions: the first induced relaxation of intestinal smooth muscle strips only, whereas the second also relaxed vascular strips as well. From the first fraction four pure biologically active peptides obtained by reverse phase HPLC have been sequenced: the 21 amino acid peptide, designated atriopeptin I, and three homologs (des-ser
1-, des-ser
1-ser
2-, and des-ser
21-atriopeptin I). From the second fraction two pure biologically active peptides were obtained, which had C-terminal extensions of atriopeptin I: atriopeptins II (23 amino acid residues) and III (24 residues), having respectively phe-arg and phe-arg-tyr C-termini. These results suggest that this family of six peptides, sharing the same 17 membered ring formed by an internal cystine disulfide, is derived from a common high molecular weight precursor. |
| doi_str_mv | 10.1016/0006-291X(84)91258-0 |
| format | Article |
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1-, des-ser
1-ser
2-, and des-ser
21-atriopeptin I). From the second fraction two pure biologically active peptides were obtained, which had C-terminal extensions of atriopeptin I: atriopeptins II (23 amino acid residues) and III (24 residues), having respectively phe-arg and phe-arg-tyr C-termini. These results suggest that this family of six peptides, sharing the same 17 membered ring formed by an internal cystine disulfide, is derived from a common high molecular weight precursor.</description><identifier>ISSN: 0006-291X</identifier><identifier>EISSN: 1090-2104</identifier><identifier>DOI: 10.1016/0006-291X(84)91258-0</identifier><identifier>PMID: 6233969</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Amino Acid Sequence ; Animals ; Atrial Natriuretic Factor ; atrium ; Biological Assay ; Chickens ; Diuresis - drug effects ; Heart Atria - analysis ; Molecular Weight ; Muscle Contraction - drug effects ; Muscle Proteins - isolation & purification ; Muscle Proteins - pharmacology ; Muscle, Smooth - physiology ; Natriuresis - drug effects ; Rabbits ; Rats ; Space life sciences ; Structure-Activity Relationship</subject><ispartof>Biochemical and biophysical research communications, 1984-04, Vol.120 (2), p.333-338</ispartof><rights>1984</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c454t-fa2da638b1102e68361e7aa7e9c2103548017810534dd33cb3e9a67a2cbcc7223</citedby><cites>FETCH-LOGICAL-c454t-fa2da638b1102e68361e7aa7e9c2103548017810534dd33cb3e9a67a2cbcc7223</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/0006291X84912580$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3537,27901,27902,65306</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/6233969$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Geller, D.M.</creatorcontrib><creatorcontrib>Currie, M.G.</creatorcontrib><creatorcontrib>Wakitani, K.</creatorcontrib><creatorcontrib>Cole, B.R.</creatorcontrib><creatorcontrib>Adams, S.P.</creatorcontrib><creatorcontrib>Fok, K.F.</creatorcontrib><creatorcontrib>Siegel, N.R.</creatorcontrib><creatorcontrib>Eubanks, S.R.</creatorcontrib><creatorcontrib>Galluppi, G.R.</creatorcontrib><creatorcontrib>Needleman, P.</creatorcontrib><title>Atriopeptins: A family of potent biologically active peptides derived from mammalian atria</title><title>Biochemical and biophysical research communications</title><addtitle>Biochem Biophys Res Commun</addtitle><description>Extracts of rat atria are potent stimulators of sodium and urine excretion, and relax vascular and intestinal smooth muscle preparations. The structures of six biologically active peptides obtained from atrial extracts are reported here. Ion exchange chromatography of a low molecular weight fraction obtained by gel filtration of atrial extracts produced two natriuretic fractions: the first induced relaxation of intestinal smooth muscle strips only, whereas the second also relaxed vascular strips as well. From the first fraction four pure biologically active peptides obtained by reverse phase HPLC have been sequenced: the 21 amino acid peptide, designated atriopeptin I, and three homologs (des-ser
1-, des-ser
1-ser
2-, and des-ser
21-atriopeptin I). From the second fraction two pure biologically active peptides were obtained, which had C-terminal extensions of atriopeptin I: atriopeptins II (23 amino acid residues) and III (24 residues), having respectively phe-arg and phe-arg-tyr C-termini. These results suggest that this family of six peptides, sharing the same 17 membered ring formed by an internal cystine disulfide, is derived from a common high molecular weight precursor.</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Atrial Natriuretic Factor</subject><subject>atrium</subject><subject>Biological Assay</subject><subject>Chickens</subject><subject>Diuresis - drug effects</subject><subject>Heart Atria - analysis</subject><subject>Molecular Weight</subject><subject>Muscle Contraction - drug effects</subject><subject>Muscle Proteins - isolation & purification</subject><subject>Muscle Proteins - pharmacology</subject><subject>Muscle, Smooth - physiology</subject><subject>Natriuresis - drug effects</subject><subject>Rabbits</subject><subject>Rats</subject><subject>Space life sciences</subject><subject>Structure-Activity Relationship</subject><issn>0006-291X</issn><issn>1090-2104</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1984</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkEFrFTEQx4Mo9Vn9Bgo5iR62zSTZbOJBeBSrhYKXCqWXkE1mJbK7WZN9hX578_oePdZTmMxv_sP8CHkP7AwYqHPGmGq4gdtPWn42wFvdsBdkA8ywhgOTL8nmCXlN3pTyhzEAqcwJOVFcCKPMhtxt1xzTgssa5_KFbungpjg-0DTQJa04r7SPaUy_o3dj_XZ-jfdIH_mAhQbMtQ50yGmik5smN0Y3U1dD3VvyanBjwXfH95T8uvx2c_Gjuf75_epie9142cq1GRwPTgndAzCOSgsF2DnXofH1CtFKzaDTwFohQxDC9wKNU53jvve-41ycko-H3CWnvzssq51i8TiObsa0K1bXYK06-C8IQreSma6C8gD6nErJONglx8nlBwvM7t3bvVi7F2u1tI_uLatjH475u37C8DR0lF37Xw99rDbuI2ZbfMTZY4gZ_WpDis8v-AfJy5Nk</recordid><startdate>19840430</startdate><enddate>19840430</enddate><creator>Geller, D.M.</creator><creator>Currie, M.G.</creator><creator>Wakitani, K.</creator><creator>Cole, B.R.</creator><creator>Adams, S.P.</creator><creator>Fok, K.F.</creator><creator>Siegel, N.R.</creator><creator>Eubanks, S.R.</creator><creator>Galluppi, G.R.</creator><creator>Needleman, P.</creator><general>Elsevier Inc</general><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>7QL</scope><scope>C1K</scope><scope>7X8</scope></search><sort><creationdate>19840430</creationdate><title>Atriopeptins: A family of potent biologically active peptides derived from mammalian atria</title><author>Geller, D.M. ; Currie, M.G. ; Wakitani, K. ; Cole, B.R. ; Adams, S.P. ; Fok, K.F. ; Siegel, N.R. ; Eubanks, S.R. ; Galluppi, G.R. ; Needleman, P.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c454t-fa2da638b1102e68361e7aa7e9c2103548017810534dd33cb3e9a67a2cbcc7223</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1984</creationdate><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Atrial Natriuretic Factor</topic><topic>atrium</topic><topic>Biological Assay</topic><topic>Chickens</topic><topic>Diuresis - drug effects</topic><topic>Heart Atria - analysis</topic><topic>Molecular Weight</topic><topic>Muscle Contraction - drug effects</topic><topic>Muscle Proteins - isolation & purification</topic><topic>Muscle Proteins - pharmacology</topic><topic>Muscle, Smooth - physiology</topic><topic>Natriuresis - drug effects</topic><topic>Rabbits</topic><topic>Rats</topic><topic>Space life sciences</topic><topic>Structure-Activity Relationship</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Geller, D.M.</creatorcontrib><creatorcontrib>Currie, M.G.</creatorcontrib><creatorcontrib>Wakitani, K.</creatorcontrib><creatorcontrib>Cole, B.R.</creatorcontrib><creatorcontrib>Adams, S.P.</creatorcontrib><creatorcontrib>Fok, K.F.</creatorcontrib><creatorcontrib>Siegel, N.R.</creatorcontrib><creatorcontrib>Eubanks, S.R.</creatorcontrib><creatorcontrib>Galluppi, G.R.</creatorcontrib><creatorcontrib>Needleman, P.</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Environmental Sciences and Pollution Management</collection><collection>MEDLINE - Academic</collection><jtitle>Biochemical and biophysical research communications</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Geller, D.M.</au><au>Currie, M.G.</au><au>Wakitani, K.</au><au>Cole, B.R.</au><au>Adams, S.P.</au><au>Fok, K.F.</au><au>Siegel, N.R.</au><au>Eubanks, S.R.</au><au>Galluppi, G.R.</au><au>Needleman, P.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Atriopeptins: A family of potent biologically active peptides derived from mammalian atria</atitle><jtitle>Biochemical and biophysical research communications</jtitle><addtitle>Biochem Biophys Res Commun</addtitle><date>1984-04-30</date><risdate>1984</risdate><volume>120</volume><issue>2</issue><spage>333</spage><epage>338</epage><pages>333-338</pages><issn>0006-291X</issn><eissn>1090-2104</eissn><abstract>Extracts of rat atria are potent stimulators of sodium and urine excretion, and relax vascular and intestinal smooth muscle preparations. The structures of six biologically active peptides obtained from atrial extracts are reported here. Ion exchange chromatography of a low molecular weight fraction obtained by gel filtration of atrial extracts produced two natriuretic fractions: the first induced relaxation of intestinal smooth muscle strips only, whereas the second also relaxed vascular strips as well. From the first fraction four pure biologically active peptides obtained by reverse phase HPLC have been sequenced: the 21 amino acid peptide, designated atriopeptin I, and three homologs (des-ser
1-, des-ser
1-ser
2-, and des-ser
21-atriopeptin I). From the second fraction two pure biologically active peptides were obtained, which had C-terminal extensions of atriopeptin I: atriopeptins II (23 amino acid residues) and III (24 residues), having respectively phe-arg and phe-arg-tyr C-termini. These results suggest that this family of six peptides, sharing the same 17 membered ring formed by an internal cystine disulfide, is derived from a common high molecular weight precursor.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>6233969</pmid><doi>10.1016/0006-291X(84)91258-0</doi><tpages>6</tpages></addata></record> |
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| ispartof | Biochemical and biophysical research communications, 1984-04, Vol.120 (2), p.333-338 |
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| source | MEDLINE; Elsevier ScienceDirect Journals Complete |
| subjects | Amino Acid Sequence Animals Atrial Natriuretic Factor atrium Biological Assay Chickens Diuresis - drug effects Heart Atria - analysis Molecular Weight Muscle Contraction - drug effects Muscle Proteins - isolation & purification Muscle Proteins - pharmacology Muscle, Smooth - physiology Natriuresis - drug effects Rabbits Rats Space life sciences Structure-Activity Relationship |
| title | Atriopeptins: A family of potent biologically active peptides derived from mammalian atria |
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