Amylin Agonists: A Novel Approach in the Treatment of Diabetes
Amylin is a peptide hormone that is cosecreted with insulin from the pancreatic beta-cell and is thus deficient in diabetic people. It inhibits glucagon secretion, delays gastric emptying, and acts as a satiety agent. Amylin replacement could therefore possibly improve glycemic control in some peopl...
Gespeichert in:
| Veröffentlicht in: | Diabetes (New York, N.Y.) N.Y.), 2004-12, Vol.53 (suppl 3), p.S233-S238 |
|---|---|
| Hauptverfasser: | , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | S238 |
|---|---|
| container_issue | suppl 3 |
| container_start_page | S233 |
| container_title | Diabetes (New York, N.Y.) |
| container_volume | 53 |
| creator | SCHMITZ, Ole BROCK, Birgitte RUNGBY, Jorgen |
| description | Amylin is a peptide hormone that is cosecreted with insulin from the pancreatic beta-cell and is thus deficient in diabetic people. It inhibits glucagon secretion, delays gastric emptying, and acts as a satiety agent. Amylin replacement could therefore possibly improve glycemic control in some people with diabetes. However, human amylin exhibits physicochemical properties predisposing the peptide hormone to aggregate and form amyloid fibers, which may play a part in beta-cell destruction in type 2 diabetes. This obviously makes it unsuitable for pharmacological use. A stable analog, pramlintide, which has actions and pharmacokinetic and pharmacodynamic properties similar to the native peptide, has been developed. The efficacy and safety of pramlintide administration has been tested in a vast number of clinical trials. Approximately 5,000 insulin-treated patients have received pramlintide and approximately 250 for > or =2 years. The aims of this review are to 1) briefly describe actions of amylin as demonstrated in animal and human models and 2) primarily review results from clinical trials with the amylin analog pramlintide. |
| doi_str_mv | 10.2337/diabetes.53.suppl_3.S233 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_pasca</sourceid><recordid>TN_cdi_pascalfrancis_primary_16322836</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>67100474</sourcerecordid><originalsourceid>FETCH-LOGICAL-c581t-4ac6f8230a0f6ef596a252cf7321f8751b0fb1113ab4ef13e0d45ac8d4ab50a23</originalsourceid><addsrcrecordid>eNp1kE1rGzEQhkVpiJ00f6GIQnNbRyOtpN0eCovTfIBJDnUgN6GVJXvDflXabfC_r4y3GAplDnOYZ2ZeHoQwkAVlTN5sKl3awYYFZ4sw9n2t2OJnnHxAc8hZnjAqXz-iOSFAE5C5nKGLEN4IISLWOZoB5wJykHP0vWj2ddXiYtu1VRjCN1zgp-63rXHR977TZofjdNhZvPZWD41tB9w5fDsF-ITOnK6DvZr6JXq5-7FePiSr5_vHZbFKDM9gSFJthMsoI5o4YR3PhaacGicZBZdJDiVxJQAwXabWAbNkk3Jtsk2qS040ZZfo-ng3Zvo12jCopgrG1rVubTcGJSQQkso0gl_-Ad-60bcxm6Ig0pwwKSOUHSHjuxC8dar3VaP9XgFRB8Hqr2DFmZoEq4PguPp5uj-Wjd2cFiejEfg6AToYXTuvW1OFEycYpRkTkYMjt6u2u_fK29PP_z7_A3g4mQ8</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>216490377</pqid></control><display><type>article</type><title>Amylin Agonists: A Novel Approach in the Treatment of Diabetes</title><source>MEDLINE</source><source>Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals</source><creator>SCHMITZ, Ole ; BROCK, Birgitte ; RUNGBY, Jorgen</creator><creatorcontrib>SCHMITZ, Ole ; BROCK, Birgitte ; RUNGBY, Jorgen</creatorcontrib><description>Amylin is a peptide hormone that is cosecreted with insulin from the pancreatic beta-cell and is thus deficient in diabetic people. It inhibits glucagon secretion, delays gastric emptying, and acts as a satiety agent. Amylin replacement could therefore possibly improve glycemic control in some people with diabetes. However, human amylin exhibits physicochemical properties predisposing the peptide hormone to aggregate and form amyloid fibers, which may play a part in beta-cell destruction in type 2 diabetes. This obviously makes it unsuitable for pharmacological use. A stable analog, pramlintide, which has actions and pharmacokinetic and pharmacodynamic properties similar to the native peptide, has been developed. The efficacy and safety of pramlintide administration has been tested in a vast number of clinical trials. Approximately 5,000 insulin-treated patients have received pramlintide and approximately 250 for > or =2 years. The aims of this review are to 1) briefly describe actions of amylin as demonstrated in animal and human models and 2) primarily review results from clinical trials with the amylin analog pramlintide.</description><identifier>ISSN: 0012-1797</identifier><identifier>EISSN: 1939-327X</identifier><identifier>DOI: 10.2337/diabetes.53.suppl_3.S233</identifier><identifier>PMID: 15561917</identifier><identifier>CODEN: DIAEAZ</identifier><language>eng</language><publisher>Alexandria, VA: American Diabetes Association</publisher><subject>Amyloid - agonists ; Amyloid - physiology ; Amyloid - therapeutic use ; Animals ; Binding sites ; Biological and medical sciences ; Clinical trials ; Clinical Trials as Topic ; Diabetes ; Diabetes Mellitus - drug therapy ; Diabetes. Impaired glucose tolerance ; Disease Models, Animal ; Endocrine pancreas. Apud cells (diseases) ; Endocrinopathies ; Etiopathogenesis. Screening. Investigations. Target tissue resistance ; Glucagon ; Glucose ; Glycated Hemoglobin A - drug effects ; Glycated Hemoglobin A - metabolism ; Humans ; Hypoglycemia ; Insulin - therapeutic use ; Insulin resistance ; Islet Amyloid Polypeptide ; Medical sciences ; Metabolism ; Peptides ; Physiology ; Signal transduction</subject><ispartof>Diabetes (New York, N.Y.), 2004-12, Vol.53 (suppl 3), p.S233-S238</ispartof><rights>2005 INIST-CNRS</rights><rights>Copyright American Diabetes Association Dec 2004</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c581t-4ac6f8230a0f6ef596a252cf7321f8751b0fb1113ab4ef13e0d45ac8d4ab50a23</citedby><cites>FETCH-LOGICAL-c581t-4ac6f8230a0f6ef596a252cf7321f8751b0fb1113ab4ef13e0d45ac8d4ab50a23</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>309,310,314,776,780,785,786,23909,23910,25118,27901,27902</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=16322836$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/15561917$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>SCHMITZ, Ole</creatorcontrib><creatorcontrib>BROCK, Birgitte</creatorcontrib><creatorcontrib>RUNGBY, Jorgen</creatorcontrib><title>Amylin Agonists: A Novel Approach in the Treatment of Diabetes</title><title>Diabetes (New York, N.Y.)</title><addtitle>Diabetes</addtitle><description>Amylin is a peptide hormone that is cosecreted with insulin from the pancreatic beta-cell and is thus deficient in diabetic people. It inhibits glucagon secretion, delays gastric emptying, and acts as a satiety agent. Amylin replacement could therefore possibly improve glycemic control in some people with diabetes. However, human amylin exhibits physicochemical properties predisposing the peptide hormone to aggregate and form amyloid fibers, which may play a part in beta-cell destruction in type 2 diabetes. This obviously makes it unsuitable for pharmacological use. A stable analog, pramlintide, which has actions and pharmacokinetic and pharmacodynamic properties similar to the native peptide, has been developed. The efficacy and safety of pramlintide administration has been tested in a vast number of clinical trials. Approximately 5,000 insulin-treated patients have received pramlintide and approximately 250 for > or =2 years. The aims of this review are to 1) briefly describe actions of amylin as demonstrated in animal and human models and 2) primarily review results from clinical trials with the amylin analog pramlintide.</description><subject>Amyloid - agonists</subject><subject>Amyloid - physiology</subject><subject>Amyloid - therapeutic use</subject><subject>Animals</subject><subject>Binding sites</subject><subject>Biological and medical sciences</subject><subject>Clinical trials</subject><subject>Clinical Trials as Topic</subject><subject>Diabetes</subject><subject>Diabetes Mellitus - drug therapy</subject><subject>Diabetes. Impaired glucose tolerance</subject><subject>Disease Models, Animal</subject><subject>Endocrine pancreas. Apud cells (diseases)</subject><subject>Endocrinopathies</subject><subject>Etiopathogenesis. Screening. Investigations. Target tissue resistance</subject><subject>Glucagon</subject><subject>Glucose</subject><subject>Glycated Hemoglobin A - drug effects</subject><subject>Glycated Hemoglobin A - metabolism</subject><subject>Humans</subject><subject>Hypoglycemia</subject><subject>Insulin - therapeutic use</subject><subject>Insulin resistance</subject><subject>Islet Amyloid Polypeptide</subject><subject>Medical sciences</subject><subject>Metabolism</subject><subject>Peptides</subject><subject>Physiology</subject><subject>Signal transduction</subject><issn>0012-1797</issn><issn>1939-327X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2004</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>8G5</sourceid><sourceid>BEC</sourceid><sourceid>BENPR</sourceid><sourceid>GUQSH</sourceid><sourceid>M2O</sourceid><recordid>eNp1kE1rGzEQhkVpiJ00f6GIQnNbRyOtpN0eCovTfIBJDnUgN6GVJXvDflXabfC_r4y3GAplDnOYZ2ZeHoQwkAVlTN5sKl3awYYFZ4sw9n2t2OJnnHxAc8hZnjAqXz-iOSFAE5C5nKGLEN4IISLWOZoB5wJykHP0vWj2ddXiYtu1VRjCN1zgp-63rXHR977TZofjdNhZvPZWD41tB9w5fDsF-ITOnK6DvZr6JXq5-7FePiSr5_vHZbFKDM9gSFJthMsoI5o4YR3PhaacGicZBZdJDiVxJQAwXabWAbNkk3Jtsk2qS040ZZfo-ng3Zvo12jCopgrG1rVubTcGJSQQkso0gl_-Ad-60bcxm6Ig0pwwKSOUHSHjuxC8dar3VaP9XgFRB8Hqr2DFmZoEq4PguPp5uj-Wjd2cFiejEfg6AToYXTuvW1OFEycYpRkTkYMjt6u2u_fK29PP_z7_A3g4mQ8</recordid><startdate>20041201</startdate><enddate>20041201</enddate><creator>SCHMITZ, Ole</creator><creator>BROCK, Birgitte</creator><creator>RUNGBY, Jorgen</creator><general>American Diabetes Association</general><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>3V.</scope><scope>7RV</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>88I</scope><scope>8AF</scope><scope>8AO</scope><scope>8C1</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>8G5</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BEC</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>GUQSH</scope><scope>HCIFZ</scope><scope>K9-</scope><scope>K9.</scope><scope>KB0</scope><scope>LK8</scope><scope>M0R</scope><scope>M0S</scope><scope>M1P</scope><scope>M2O</scope><scope>M2P</scope><scope>M7P</scope><scope>MBDVC</scope><scope>NAPCQ</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>Q9U</scope><scope>S0X</scope><scope>7X8</scope></search><sort><creationdate>20041201</creationdate><title>Amylin Agonists: A Novel Approach in the Treatment of Diabetes</title><author>SCHMITZ, Ole ; BROCK, Birgitte ; RUNGBY, Jorgen</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c581t-4ac6f8230a0f6ef596a252cf7321f8751b0fb1113ab4ef13e0d45ac8d4ab50a23</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2004</creationdate><topic>Amyloid - agonists</topic><topic>Amyloid - physiology</topic><topic>Amyloid - therapeutic use</topic><topic>Animals</topic><topic>Binding sites</topic><topic>Biological and medical sciences</topic><topic>Clinical trials</topic><topic>Clinical Trials as Topic</topic><topic>Diabetes</topic><topic>Diabetes Mellitus - drug therapy</topic><topic>Diabetes. Impaired glucose tolerance</topic><topic>Disease Models, Animal</topic><topic>Endocrine pancreas. Apud cells (diseases)</topic><topic>Endocrinopathies</topic><topic>Etiopathogenesis. Screening. Investigations. Target tissue resistance</topic><topic>Glucagon</topic><topic>Glucose</topic><topic>Glycated Hemoglobin A - drug effects</topic><topic>Glycated Hemoglobin A - metabolism</topic><topic>Humans</topic><topic>Hypoglycemia</topic><topic>Insulin - therapeutic use</topic><topic>Insulin resistance</topic><topic>Islet Amyloid Polypeptide</topic><topic>Medical sciences</topic><topic>Metabolism</topic><topic>Peptides</topic><topic>Physiology</topic><topic>Signal transduction</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>SCHMITZ, Ole</creatorcontrib><creatorcontrib>BROCK, Birgitte</creatorcontrib><creatorcontrib>RUNGBY, Jorgen</creatorcontrib><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>ProQuest Central (Corporate)</collection><collection>Nursing & Allied Health Database</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Medical Database (Alumni Edition)</collection><collection>Science Database (Alumni Edition)</collection><collection>STEM Database</collection><collection>ProQuest Pharma Collection</collection><collection>Public Health Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>Research Library (Alumni Edition)</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>eLibrary</collection><collection>ProQuest Central</collection><collection>Natural Science Collection</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>Research Library Prep</collection><collection>SciTech Premium Collection</collection><collection>Consumer Health Database (Alumni Edition)</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Nursing & Allied Health Database (Alumni Edition)</collection><collection>ProQuest Biological Science Collection</collection><collection>Consumer Health Database</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Research Library</collection><collection>Science Database</collection><collection>Biological Science Database</collection><collection>Research Library (Corporate)</collection><collection>Nursing & Allied Health Premium</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central China</collection><collection>ProQuest Central Basic</collection><collection>SIRS Editorial</collection><collection>MEDLINE - Academic</collection><jtitle>Diabetes (New York, N.Y.)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>SCHMITZ, Ole</au><au>BROCK, Birgitte</au><au>RUNGBY, Jorgen</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Amylin Agonists: A Novel Approach in the Treatment of Diabetes</atitle><jtitle>Diabetes (New York, N.Y.)</jtitle><addtitle>Diabetes</addtitle><date>2004-12-01</date><risdate>2004</risdate><volume>53</volume><issue>suppl 3</issue><spage>S233</spage><epage>S238</epage><pages>S233-S238</pages><issn>0012-1797</issn><eissn>1939-327X</eissn><coden>DIAEAZ</coden><abstract>Amylin is a peptide hormone that is cosecreted with insulin from the pancreatic beta-cell and is thus deficient in diabetic people. It inhibits glucagon secretion, delays gastric emptying, and acts as a satiety agent. Amylin replacement could therefore possibly improve glycemic control in some people with diabetes. However, human amylin exhibits physicochemical properties predisposing the peptide hormone to aggregate and form amyloid fibers, which may play a part in beta-cell destruction in type 2 diabetes. This obviously makes it unsuitable for pharmacological use. A stable analog, pramlintide, which has actions and pharmacokinetic and pharmacodynamic properties similar to the native peptide, has been developed. The efficacy and safety of pramlintide administration has been tested in a vast number of clinical trials. Approximately 5,000 insulin-treated patients have received pramlintide and approximately 250 for > or =2 years. The aims of this review are to 1) briefly describe actions of amylin as demonstrated in animal and human models and 2) primarily review results from clinical trials with the amylin analog pramlintide.</abstract><cop>Alexandria, VA</cop><pub>American Diabetes Association</pub><pmid>15561917</pmid><doi>10.2337/diabetes.53.suppl_3.S233</doi><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0012-1797 |
| ispartof | Diabetes (New York, N.Y.), 2004-12, Vol.53 (suppl 3), p.S233-S238 |
| issn | 0012-1797 1939-327X |
| language | eng |
| recordid | cdi_pascalfrancis_primary_16322836 |
| source | MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals |
| subjects | Amyloid - agonists Amyloid - physiology Amyloid - therapeutic use Animals Binding sites Biological and medical sciences Clinical trials Clinical Trials as Topic Diabetes Diabetes Mellitus - drug therapy Diabetes. Impaired glucose tolerance Disease Models, Animal Endocrine pancreas. Apud cells (diseases) Endocrinopathies Etiopathogenesis. Screening. Investigations. Target tissue resistance Glucagon Glucose Glycated Hemoglobin A - drug effects Glycated Hemoglobin A - metabolism Humans Hypoglycemia Insulin - therapeutic use Insulin resistance Islet Amyloid Polypeptide Medical sciences Metabolism Peptides Physiology Signal transduction |
| title | Amylin Agonists: A Novel Approach in the Treatment of Diabetes |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-02-02T05%3A44%3A30IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_pasca&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Amylin%20Agonists:%20A%20Novel%20Approach%20in%20the%20Treatment%20of%20Diabetes&rft.jtitle=Diabetes%20(New%20York,%20N.Y.)&rft.au=SCHMITZ,%20Ole&rft.date=2004-12-01&rft.volume=53&rft.issue=suppl%203&rft.spage=S233&rft.epage=S238&rft.pages=S233-S238&rft.issn=0012-1797&rft.eissn=1939-327X&rft.coden=DIAEAZ&rft_id=info:doi/10.2337/diabetes.53.suppl_3.S233&rft_dat=%3Cproquest_pasca%3E67100474%3C/proquest_pasca%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=216490377&rft_id=info:pmid/15561917&rfr_iscdi=true |