A Superactive Insulin: [B 10-aspartic Acid]Insulin(Human)
The genetic basis for a case of familial hyperproinsulinemia has been elucidated recently. It involves a single point mutation in the proinsulin gene resulting in the substitution of aspartic acid for histidine-10 of the B chain of insulin. We have synthesized a human insulin analogue, [AspB10]insul...
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| Veröffentlicht in: | Proc. Natl. Acad. Sci. U.S.A.; (United States) 1987-09, Vol.84 (18), p.6408-6411 |
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| creator | Schwartz, Gerald P. Burke, G. Thompson Katsoyannis, Panayotis G. |
| description | The genetic basis for a case of familial hyperproinsulinemia has been elucidated recently. It involves a single point mutation in the proinsulin gene resulting in the substitution of aspartic acid for histidine-10 of the B chain of insulin. We have synthesized a human insulin analogue, [AspB10]insulin, corresponding to the mutant proinsulin and evaluated its biological activity. [AspB10]Insulin displayed a binding affinity to insulin receptors in rat liver plasma membranes that was 534 ± 146% relative to the natural hormone. In lipogenesis assays, the synthetic analogue exhibited a potency that was 435 ± 144% relative to insulin, which is statistically not different from its binding affinity. Reversed-phase HPLC indicated that the synthetic analogue is more apolar than natural insulin. We suggest that the observed properties reflect changes in the conformation of the analogue relative to natural insulin, which result in a stronger interaction with the insulin receptor. Thus, a single substitution of an amino acid residue of human insulin has resulted in a superactive hormone. |
| doi_str_mv | 10.1073/pnas.84.18.6408 |
| format | Article |
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Thompson ; Katsoyannis, Panayotis G.</creator><creatorcontrib>Schwartz, Gerald P. ; Burke, G. Thompson ; Katsoyannis, Panayotis G. ; City Univ. of New York, NY (USA)</creatorcontrib><description>The genetic basis for a case of familial hyperproinsulinemia has been elucidated recently. It involves a single point mutation in the proinsulin gene resulting in the substitution of aspartic acid for histidine-10 of the B chain of insulin. We have synthesized a human insulin analogue, [AspB10]insulin, corresponding to the mutant proinsulin and evaluated its biological activity. [AspB10]Insulin displayed a binding affinity to insulin receptors in rat liver plasma membranes that was 534 ± 146% relative to the natural hormone. In lipogenesis assays, the synthetic analogue exhibited a potency that was 435 ± 144% relative to insulin, which is statistically not different from its binding affinity. Reversed-phase HPLC indicated that the synthetic analogue is more apolar than natural insulin. We suggest that the observed properties reflect changes in the conformation of the analogue relative to natural insulin, which result in a stronger interaction with the insulin receptor. Thus, a single substitution of an amino acid residue of human insulin has resulted in a superactive hormone.</description><identifier>ISSN: 0027-8424</identifier><identifier>EISSN: 1091-6490</identifier><identifier>DOI: 10.1073/pnas.84.18.6408</identifier><identifier>PMID: 3306677</identifier><identifier>CODEN: PNASA6</identifier><language>eng</language><publisher>Washington, DC: National Academy of Sciences of the United States of America</publisher><subject>550201 - Biochemistry- Tracer Techniques ; Acetates ; ALDEHYDES ; AMINO ACID SEQUENCE ; AMINO ACIDS ; ANIMALS ; ASPARTIC ACID ; AZOLES ; BASIC BIOLOGICAL SCIENCES ; BETA DECAY RADIOISOTOPES ; Binding, Competitive ; Biochemistry ; Biological and medical sciences ; BIOSYNTHESIS ; BODY ; CARBOHYDRATES ; CARBOXYLIC ACIDS ; CELL CONSTITUENTS ; CELL MEMBRANES ; Cell physiology ; CHROMATOGRAPHY ; Chromatography, High Pressure Liquid ; CONFIGURATION INTERACTION ; DAYS LIVING RADIOISOTOPES ; DIGESTIVE SYSTEM ; DISEASES ; ELECTRON CAPTURE RADIOISOTOPES ; Ethers ; Fundamental and applied biological sciences. Psychology ; GENE MUTATIONS ; GLANDS ; GLUCOSE ; HEREDITARY DISEASES ; HETEROCYCLIC ACIDS ; HETEROCYCLIC COMPOUNDS ; HEXOSES ; HISTIDINE ; Hormonal regulation ; HORMONES ; Humans ; IMIDAZOLES ; INSULIN ; Insulin - analogs & derivatives ; Insulin - chemical synthesis ; Insulin - metabolism ; INTERMEDIATE MASS NUCLEI ; IODINE 125 ; IODINE ISOTOPES ; ISOTOPES ; LABELLED COMPOUNDS ; Lipid Mobilization - drug effects ; Lipogenesis ; LIQUID COLUMN CHROMATOGRAPHY ; LIVER ; Male ; MAMMALS ; MEMBRANE PROTEINS ; MEMBRANES ; Molecular and cellular biology ; MOLECULAR STRUCTURE ; Molecules ; MONOSACCHARIDES ; MUTATIONS ; NUCLEI ; ODD-EVEN NUCLEI ; ORGANIC ACIDS ; ORGANIC COMPOUNDS ; ORGANIC NITROGEN COMPOUNDS ; ORGANS ; PEPTIDE HORMONES ; Protein Conformation ; PROTEINS ; RADIOISOTOPES ; RATS ; Receptor, Insulin - metabolism ; RECEPTORS ; RODENTS ; Room temperature ; SACCHARIDES ; SEPARATION PROCESSES ; Solubility ; Structure-Activity Relationship ; SYNTHESIS ; THIN-LAYER CHROMATOGRAPHY ; TRITIUM COMPOUNDS ; Ungulates ; VERTEBRATES</subject><ispartof>Proc. 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U.S.A.; (United States), 1987-09, Vol.84 (18), p.6408-6411</ispartof><rights>1987 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c643t-37625574677258fc57424048deb3dc3fd74f43dd5a44987938ff9328c66062763</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Uhttp://www.pnas.org/content/84/18.cover.gif</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/29846$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/29846$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>230,314,723,776,780,799,881,27901,27902,53766,53768,57992,58225</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=8359148$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/3306677$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://www.osti.gov/biblio/7143351$$D View this record in Osti.gov$$Hfree_for_read</backlink></links><search><creatorcontrib>Schwartz, Gerald P.</creatorcontrib><creatorcontrib>Burke, G. Thompson</creatorcontrib><creatorcontrib>Katsoyannis, Panayotis G.</creatorcontrib><creatorcontrib>City Univ. of New York, NY (USA)</creatorcontrib><title>A Superactive Insulin: [B 10-aspartic Acid]Insulin(Human)</title><title>Proc. Natl. Acad. Sci. U.S.A.; (United States)</title><addtitle>Proc Natl Acad Sci U S A</addtitle><description>The genetic basis for a case of familial hyperproinsulinemia has been elucidated recently. It involves a single point mutation in the proinsulin gene resulting in the substitution of aspartic acid for histidine-10 of the B chain of insulin. We have synthesized a human insulin analogue, [AspB10]insulin, corresponding to the mutant proinsulin and evaluated its biological activity. [AspB10]Insulin displayed a binding affinity to insulin receptors in rat liver plasma membranes that was 534 ± 146% relative to the natural hormone. In lipogenesis assays, the synthetic analogue exhibited a potency that was 435 ± 144% relative to insulin, which is statistically not different from its binding affinity. Reversed-phase HPLC indicated that the synthetic analogue is more apolar than natural insulin. We suggest that the observed properties reflect changes in the conformation of the analogue relative to natural insulin, which result in a stronger interaction with the insulin receptor. Thus, a single substitution of an amino acid residue of human insulin has resulted in a superactive hormone.</description><subject>550201 - Biochemistry- Tracer Techniques</subject><subject>Acetates</subject><subject>ALDEHYDES</subject><subject>AMINO ACID SEQUENCE</subject><subject>AMINO ACIDS</subject><subject>ANIMALS</subject><subject>ASPARTIC ACID</subject><subject>AZOLES</subject><subject>BASIC BIOLOGICAL SCIENCES</subject><subject>BETA DECAY RADIOISOTOPES</subject><subject>Binding, Competitive</subject><subject>Biochemistry</subject><subject>Biological and medical sciences</subject><subject>BIOSYNTHESIS</subject><subject>BODY</subject><subject>CARBOHYDRATES</subject><subject>CARBOXYLIC ACIDS</subject><subject>CELL CONSTITUENTS</subject><subject>CELL MEMBRANES</subject><subject>Cell physiology</subject><subject>CHROMATOGRAPHY</subject><subject>Chromatography, High Pressure Liquid</subject><subject>CONFIGURATION INTERACTION</subject><subject>DAYS LIVING RADIOISOTOPES</subject><subject>DIGESTIVE SYSTEM</subject><subject>DISEASES</subject><subject>ELECTRON CAPTURE RADIOISOTOPES</subject><subject>Ethers</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>GENE MUTATIONS</subject><subject>GLANDS</subject><subject>GLUCOSE</subject><subject>HEREDITARY DISEASES</subject><subject>HETEROCYCLIC ACIDS</subject><subject>HETEROCYCLIC COMPOUNDS</subject><subject>HEXOSES</subject><subject>HISTIDINE</subject><subject>Hormonal regulation</subject><subject>HORMONES</subject><subject>Humans</subject><subject>IMIDAZOLES</subject><subject>INSULIN</subject><subject>Insulin - analogs & derivatives</subject><subject>Insulin - chemical synthesis</subject><subject>Insulin - metabolism</subject><subject>INTERMEDIATE MASS NUCLEI</subject><subject>IODINE 125</subject><subject>IODINE ISOTOPES</subject><subject>ISOTOPES</subject><subject>LABELLED COMPOUNDS</subject><subject>Lipid Mobilization - drug effects</subject><subject>Lipogenesis</subject><subject>LIQUID COLUMN CHROMATOGRAPHY</subject><subject>LIVER</subject><subject>Male</subject><subject>MAMMALS</subject><subject>MEMBRANE PROTEINS</subject><subject>MEMBRANES</subject><subject>Molecular and cellular biology</subject><subject>MOLECULAR STRUCTURE</subject><subject>Molecules</subject><subject>MONOSACCHARIDES</subject><subject>MUTATIONS</subject><subject>NUCLEI</subject><subject>ODD-EVEN NUCLEI</subject><subject>ORGANIC ACIDS</subject><subject>ORGANIC COMPOUNDS</subject><subject>ORGANIC NITROGEN COMPOUNDS</subject><subject>ORGANS</subject><subject>PEPTIDE HORMONES</subject><subject>Protein Conformation</subject><subject>PROTEINS</subject><subject>RADIOISOTOPES</subject><subject>RATS</subject><subject>Receptor, Insulin - metabolism</subject><subject>RECEPTORS</subject><subject>RODENTS</subject><subject>Room temperature</subject><subject>SACCHARIDES</subject><subject>SEPARATION PROCESSES</subject><subject>Solubility</subject><subject>Structure-Activity Relationship</subject><subject>SYNTHESIS</subject><subject>THIN-LAYER CHROMATOGRAPHY</subject><subject>TRITIUM COMPOUNDS</subject><subject>Ungulates</subject><subject>VERTEBRATES</subject><issn>0027-8424</issn><issn>1091-6490</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1987</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkctrFTEYxYMo9VpdC4IySPGxmNs8vrwEF9eitlBwoa5EQprJ2JS5mWmSKfrfd4Y7XOpGVwmc3zkn4SD0lOA1wZIdD9HmtYI1UWsBWN1DK4I1qQVofB-tMKayVkDhIXqU8xXGWHOFD9ABY1gIKVdIb6qv4-CTdSXc-Oos5rEL8V3140NFcG3zYFMJrtq40PxcxDen49bGt4_Rg9Z22T9ZzkP0_dPHbyen9fmXz2cnm_PaCWClZlJQziVMbZSr1k1XChhU4y9Y41jbSGiBNQ23AFpJzVTbakaVEwILKgU7RO93ucN4sfWN87Ek25khha1Nf0xvg_lbieHS_OpvDNUaKz75X-78fS7BZBeKd5euj9G7YiQBxjiZoFdLSeqvR5-L2YbsfNfZ6PsxGymFohz4f0ECmmgNegKPd6BLfc7Jt_sXE2zm6cw8nVFgiDLzdJPj-d2P7vllq0k_WnSbne3aZKMLeY8pxjWBOebFgs35e_Vuz-t_AqYdu67432Uin-3Iq1z6tEepViDYLbbYv8M</recordid><startdate>19870901</startdate><enddate>19870901</enddate><creator>Schwartz, Gerald P.</creator><creator>Burke, G. Thompson</creator><creator>Katsoyannis, Panayotis G.</creator><general>National Academy of Sciences of the United States of America</general><general>National Acad Sciences</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>7QL</scope><scope>C1K</scope><scope>7X8</scope><scope>OTOTI</scope><scope>5PM</scope></search><sort><creationdate>19870901</creationdate><title>A Superactive Insulin: [B 10-aspartic Acid]Insulin(Human)</title><author>Schwartz, Gerald P. ; Burke, G. Thompson ; Katsoyannis, Panayotis G.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c643t-37625574677258fc57424048deb3dc3fd74f43dd5a44987938ff9328c66062763</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1987</creationdate><topic>550201 - Biochemistry- Tracer Techniques</topic><topic>Acetates</topic><topic>ALDEHYDES</topic><topic>AMINO ACID SEQUENCE</topic><topic>AMINO ACIDS</topic><topic>ANIMALS</topic><topic>ASPARTIC ACID</topic><topic>AZOLES</topic><topic>BASIC BIOLOGICAL SCIENCES</topic><topic>BETA DECAY RADIOISOTOPES</topic><topic>Binding, Competitive</topic><topic>Biochemistry</topic><topic>Biological and medical sciences</topic><topic>BIOSYNTHESIS</topic><topic>BODY</topic><topic>CARBOHYDRATES</topic><topic>CARBOXYLIC ACIDS</topic><topic>CELL CONSTITUENTS</topic><topic>CELL MEMBRANES</topic><topic>Cell physiology</topic><topic>CHROMATOGRAPHY</topic><topic>Chromatography, High Pressure Liquid</topic><topic>CONFIGURATION INTERACTION</topic><topic>DAYS LIVING RADIOISOTOPES</topic><topic>DIGESTIVE SYSTEM</topic><topic>DISEASES</topic><topic>ELECTRON CAPTURE RADIOISOTOPES</topic><topic>Ethers</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>GENE MUTATIONS</topic><topic>GLANDS</topic><topic>GLUCOSE</topic><topic>HEREDITARY DISEASES</topic><topic>HETEROCYCLIC ACIDS</topic><topic>HETEROCYCLIC COMPOUNDS</topic><topic>HEXOSES</topic><topic>HISTIDINE</topic><topic>Hormonal regulation</topic><topic>HORMONES</topic><topic>Humans</topic><topic>IMIDAZOLES</topic><topic>INSULIN</topic><topic>Insulin - analogs & derivatives</topic><topic>Insulin - chemical synthesis</topic><topic>Insulin - metabolism</topic><topic>INTERMEDIATE MASS NUCLEI</topic><topic>IODINE 125</topic><topic>IODINE ISOTOPES</topic><topic>ISOTOPES</topic><topic>LABELLED COMPOUNDS</topic><topic>Lipid Mobilization - drug effects</topic><topic>Lipogenesis</topic><topic>LIQUID COLUMN CHROMATOGRAPHY</topic><topic>LIVER</topic><topic>Male</topic><topic>MAMMALS</topic><topic>MEMBRANE PROTEINS</topic><topic>MEMBRANES</topic><topic>Molecular and cellular biology</topic><topic>MOLECULAR STRUCTURE</topic><topic>Molecules</topic><topic>MONOSACCHARIDES</topic><topic>MUTATIONS</topic><topic>NUCLEI</topic><topic>ODD-EVEN NUCLEI</topic><topic>ORGANIC ACIDS</topic><topic>ORGANIC COMPOUNDS</topic><topic>ORGANIC NITROGEN COMPOUNDS</topic><topic>ORGANS</topic><topic>PEPTIDE HORMONES</topic><topic>Protein Conformation</topic><topic>PROTEINS</topic><topic>RADIOISOTOPES</topic><topic>RATS</topic><topic>Receptor, Insulin - metabolism</topic><topic>RECEPTORS</topic><topic>RODENTS</topic><topic>Room temperature</topic><topic>SACCHARIDES</topic><topic>SEPARATION PROCESSES</topic><topic>Solubility</topic><topic>Structure-Activity Relationship</topic><topic>SYNTHESIS</topic><topic>THIN-LAYER CHROMATOGRAPHY</topic><topic>TRITIUM COMPOUNDS</topic><topic>Ungulates</topic><topic>VERTEBRATES</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Schwartz, Gerald P.</creatorcontrib><creatorcontrib>Burke, G. Thompson</creatorcontrib><creatorcontrib>Katsoyannis, Panayotis G.</creatorcontrib><creatorcontrib>City Univ. of New York, NY (USA)</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>Bacteriology Abstracts (Microbiology B)</collection><collection>Environmental Sciences and Pollution Management</collection><collection>MEDLINE - Academic</collection><collection>OSTI.GOV</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Proc. Natl. Acad. Sci. U.S.A.; (United States)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Schwartz, Gerald P.</au><au>Burke, G. Thompson</au><au>Katsoyannis, Panayotis G.</au><aucorp>City Univ. of New York, NY (USA)</aucorp><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>A Superactive Insulin: [B 10-aspartic Acid]Insulin(Human)</atitle><jtitle>Proc. Natl. Acad. Sci. U.S.A.; (United States)</jtitle><addtitle>Proc Natl Acad Sci U S A</addtitle><date>1987-09-01</date><risdate>1987</risdate><volume>84</volume><issue>18</issue><spage>6408</spage><epage>6411</epage><pages>6408-6411</pages><issn>0027-8424</issn><eissn>1091-6490</eissn><coden>PNASA6</coden><abstract>The genetic basis for a case of familial hyperproinsulinemia has been elucidated recently. It involves a single point mutation in the proinsulin gene resulting in the substitution of aspartic acid for histidine-10 of the B chain of insulin. We have synthesized a human insulin analogue, [AspB10]insulin, corresponding to the mutant proinsulin and evaluated its biological activity. [AspB10]Insulin displayed a binding affinity to insulin receptors in rat liver plasma membranes that was 534 ± 146% relative to the natural hormone. In lipogenesis assays, the synthetic analogue exhibited a potency that was 435 ± 144% relative to insulin, which is statistically not different from its binding affinity. Reversed-phase HPLC indicated that the synthetic analogue is more apolar than natural insulin. We suggest that the observed properties reflect changes in the conformation of the analogue relative to natural insulin, which result in a stronger interaction with the insulin receptor. Thus, a single substitution of an amino acid residue of human insulin has resulted in a superactive hormone.</abstract><cop>Washington, DC</cop><pub>National Academy of Sciences of the United States of America</pub><pmid>3306677</pmid><doi>10.1073/pnas.84.18.6408</doi><tpages>4</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | Proc. Natl. Acad. Sci. U.S.A.; (United States), 1987-09, Vol.84 (18), p.6408-6411 |
| issn | 0027-8424 1091-6490 |
| language | eng |
| recordid | cdi_pnas_primary_84_18_6408 |
| source | Jstor Complete Legacy; MEDLINE; PubMed Central; Alma/SFX Local Collection; Free Full-Text Journals in Chemistry |
| subjects | 550201 - Biochemistry- Tracer Techniques Acetates ALDEHYDES AMINO ACID SEQUENCE AMINO ACIDS ANIMALS ASPARTIC ACID AZOLES BASIC BIOLOGICAL SCIENCES BETA DECAY RADIOISOTOPES Binding, Competitive Biochemistry Biological and medical sciences BIOSYNTHESIS BODY CARBOHYDRATES CARBOXYLIC ACIDS CELL CONSTITUENTS CELL MEMBRANES Cell physiology CHROMATOGRAPHY Chromatography, High Pressure Liquid CONFIGURATION INTERACTION DAYS LIVING RADIOISOTOPES DIGESTIVE SYSTEM DISEASES ELECTRON CAPTURE RADIOISOTOPES Ethers Fundamental and applied biological sciences. Psychology GENE MUTATIONS GLANDS GLUCOSE HEREDITARY DISEASES HETEROCYCLIC ACIDS HETEROCYCLIC COMPOUNDS HEXOSES HISTIDINE Hormonal regulation HORMONES Humans IMIDAZOLES INSULIN Insulin - analogs & derivatives Insulin - chemical synthesis Insulin - metabolism INTERMEDIATE MASS NUCLEI IODINE 125 IODINE ISOTOPES ISOTOPES LABELLED COMPOUNDS Lipid Mobilization - drug effects Lipogenesis LIQUID COLUMN CHROMATOGRAPHY LIVER Male MAMMALS MEMBRANE PROTEINS MEMBRANES Molecular and cellular biology MOLECULAR STRUCTURE Molecules MONOSACCHARIDES MUTATIONS NUCLEI ODD-EVEN NUCLEI ORGANIC ACIDS ORGANIC COMPOUNDS ORGANIC NITROGEN COMPOUNDS ORGANS PEPTIDE HORMONES Protein Conformation PROTEINS RADIOISOTOPES RATS Receptor, Insulin - metabolism RECEPTORS RODENTS Room temperature SACCHARIDES SEPARATION PROCESSES Solubility Structure-Activity Relationship SYNTHESIS THIN-LAYER CHROMATOGRAPHY TRITIUM COMPOUNDS Ungulates VERTEBRATES |
| title | A Superactive Insulin: [B 10-aspartic Acid]Insulin(Human) |
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