A Mitogenic Peptide Amide Encoded within the E Peptide Domain of the Insulin-Like Growth Factor IB Prohormone
We have identified an amino acid sequence within the E peptide of the insulin-like growth factor IB (IGF-IB) precursor that is biologically active and designated this peptide insulin-like growth factor IB-(103-124) E1amide (IBE1). Its existence was predicted by a flanking Gly-Lys-Lys-Lys, a signal s...
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Veröffentlicht in: | Proceedings of the National Academy of Sciences - PNAS 1992-09, Vol.89 (17), p.8107-8111 |
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description | We have identified an amino acid sequence within the E peptide of the insulin-like growth factor IB (IGF-IB) precursor that is biologically active and designated this peptide insulin-like growth factor IB-(103-124) E1amide (IBE1). Its existence was predicted by a flanking Gly-Lys-Lys-Lys, a signal sequence for sequential proteolytic cleavage and peptidyl C-terminal amidation. A synthetic analog of the predicted IBE1peptide, designated Y-23-R-NH2, was generated with tyrosine added at position 0. This peptide at 2-20 nM had growth-promoting effects on both normal and malignant human bronchial epithelial cells. Y-23-R-NH2bound to specific high-affinity receptors (Kd= 2.8 ± 1.4 x 10-11M) present at 1-2 * 104binding sites per cell. Ligand binding was not inhibited byrecombinant insulin or recombinant IGF-I. Furthermore, a monoclonal antibody antagonist to the IGF-I receptor (αIR3) did not suppress the proliferative response induced by Y-23-R-NH2. In addition, C-terminal amidation was shown to be important in receptor recognition since the free-acid analog of IBE1(Y-23-R-OH) did not effectively compete for binding and was not a potent agonist of proliferation. Immunoblot analysis of human lung tumor cell line extracts using an antibody raised against Y-23-R-NH2detected a low molecular mass band of ≈5 kDa, implying that a protein product is produced that has immunological similarity to IBE1. Extracts of human, mammalian, and avian livers analyzed on an immunoblot with the anti-Y-23-R-NH2antibody contained proteins of ≈21 kDa that were specifically recognized by the antiserum and presumably represent an IGF-I precursor molecule. This implies that in species where an IGF-I mRNA with homology to the human IGF-IB E domain has not yet been described, an alternate mRNA must be produced that contains a sequence similar to that of the midportion of the human IGF-IB E domain. Our findings demonstrate that IBE1is a growth factor that mediates its effect through a specific high-affinity receptor and is most likely conserved in many species. |
doi_str_mv | 10.1073/pnas.89.17.8107 |
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Its existence was predicted by a flanking Gly-Lys-Lys-Lys, a signal sequence for sequential proteolytic cleavage and peptidyl C-terminal amidation. A synthetic analog of the predicted IBE1peptide, designated Y-23-R-NH2, was generated with tyrosine added at position 0. This peptide at 2-20 nM had growth-promoting effects on both normal and malignant human bronchial epithelial cells. Y-23-R-NH2bound to specific high-affinity receptors (Kd= 2.8 ± 1.4 x 10-11M) present at 1-2 * 104binding sites per cell. Ligand binding was not inhibited byrecombinant insulin or recombinant IGF-I. Furthermore, a monoclonal antibody antagonist to the IGF-I receptor (αIR3) did not suppress the proliferative response induced by Y-23-R-NH2. In addition, C-terminal amidation was shown to be important in receptor recognition since the free-acid analog of IBE1(Y-23-R-OH) did not effectively compete for binding and was not a potent agonist of proliferation. Immunoblot analysis of human lung tumor cell line extracts using an antibody raised against Y-23-R-NH2detected a low molecular mass band of ≈5 kDa, implying that a protein product is produced that has immunological similarity to IBE1. Extracts of human, mammalian, and avian livers analyzed on an immunoblot with the anti-Y-23-R-NH2antibody contained proteins of ≈21 kDa that were specifically recognized by the antiserum and presumably represent an IGF-I precursor molecule. This implies that in species where an IGF-I mRNA with homology to the human IGF-IB E domain has not yet been described, an alternate mRNA must be produced that contains a sequence similar to that of the midportion of the human IGF-IB E domain. Our findings demonstrate that IBE1is a growth factor that mediates its effect through a specific high-affinity receptor and is most likely conserved in many species.</description><identifier>ISSN: 0027-8424</identifier><identifier>EISSN: 1091-6490</identifier><identifier>DOI: 10.1073/pnas.89.17.8107</identifier><identifier>PMID: 1325646</identifier><identifier>CODEN: PNASA6</identifier><language>eng</language><publisher>Washington, DC: National Academy of Sciences of the United States of America</publisher><subject>Amides ; Amino Acid Sequence ; Amino acids ; Analytical, structural and metabolic biochemistry ; Base Sequence ; Biological and medical sciences ; Blotting, Western ; cDNA ; Cell growth ; Cell lines ; Cellular biology ; E peptide ; Fundamental and applied biological sciences. Psychology ; genes ; Hormones ; Humans ; In Vitro Techniques ; Insulin-Like Growth Factor I - chemistry ; Insulin-Like Growth Factor I - immunology ; Insulin-Like Growth Factor I - metabolism ; insulin-like growth factor IB ; Lungs ; man ; Messenger RNA ; Mitogens - chemistry ; Mitogens - immunology ; Mitogens - metabolism ; Molecular Sequence Data ; Molecules ; nucleotide sequence ; Peptide Fragments - metabolism ; predictions ; Protein hormones. Growth factors. Cytokines ; Protein Precursors - metabolism ; Protein Processing, Post-Translational ; Proteins ; Receptors ; Receptors, Cell Surface - metabolism ; Tumor Cells, Cultured</subject><ispartof>Proceedings of the National Academy of Sciences - PNAS, 1992-09, Vol.89 (17), p.8107-8111</ispartof><rights>Copyright 1992 The National Academy of Sciences of the United States of America</rights><rights>1992 INIST-CNRS</rights><rights>Copyright National Academy of Sciences Sep 1, 1992</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c549t-2df564ed8e9748e8ee1987a5b59534ece88e69fb1bb5dbada0a1a27f047c27663</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Uhttp://www.pnas.org/content/89/17.cover.gif</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/2361304$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/2361304$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>230,314,727,780,784,803,885,27924,27925,53791,53793,58017,58250</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=5552687$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/1325646$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Siegfried, Jill M.</creatorcontrib><creatorcontrib>Kasprzyk, Philip G.</creatorcontrib><creatorcontrib>Treston, Anthony M.</creatorcontrib><creatorcontrib>Mulshine, James L.</creatorcontrib><creatorcontrib>Quinn, Kathryn A.</creatorcontrib><creatorcontrib>Cuttitta, Frank</creatorcontrib><title>A Mitogenic Peptide Amide Encoded within the E Peptide Domain of the Insulin-Like Growth Factor IB Prohormone</title><title>Proceedings of the National Academy of Sciences - PNAS</title><addtitle>Proc Natl Acad Sci U S A</addtitle><description>We have identified an amino acid sequence within the E peptide of the insulin-like growth factor IB (IGF-IB) precursor that is biologically active and designated this peptide insulin-like growth factor IB-(103-124) E1amide (IBE1). Its existence was predicted by a flanking Gly-Lys-Lys-Lys, a signal sequence for sequential proteolytic cleavage and peptidyl C-terminal amidation. A synthetic analog of the predicted IBE1peptide, designated Y-23-R-NH2, was generated with tyrosine added at position 0. This peptide at 2-20 nM had growth-promoting effects on both normal and malignant human bronchial epithelial cells. Y-23-R-NH2bound to specific high-affinity receptors (Kd= 2.8 ± 1.4 x 10-11M) present at 1-2 * 104binding sites per cell. Ligand binding was not inhibited byrecombinant insulin or recombinant IGF-I. Furthermore, a monoclonal antibody antagonist to the IGF-I receptor (αIR3) did not suppress the proliferative response induced by Y-23-R-NH2. In addition, C-terminal amidation was shown to be important in receptor recognition since the free-acid analog of IBE1(Y-23-R-OH) did not effectively compete for binding and was not a potent agonist of proliferation. Immunoblot analysis of human lung tumor cell line extracts using an antibody raised against Y-23-R-NH2detected a low molecular mass band of ≈5 kDa, implying that a protein product is produced that has immunological similarity to IBE1. Extracts of human, mammalian, and avian livers analyzed on an immunoblot with the anti-Y-23-R-NH2antibody contained proteins of ≈21 kDa that were specifically recognized by the antiserum and presumably represent an IGF-I precursor molecule. This implies that in species where an IGF-I mRNA with homology to the human IGF-IB E domain has not yet been described, an alternate mRNA must be produced that contains a sequence similar to that of the midportion of the human IGF-IB E domain. Our findings demonstrate that IBE1is a growth factor that mediates its effect through a specific high-affinity receptor and is most likely conserved in many species.</description><subject>Amides</subject><subject>Amino Acid Sequence</subject><subject>Amino acids</subject><subject>Analytical, structural and metabolic biochemistry</subject><subject>Base Sequence</subject><subject>Biological and medical sciences</subject><subject>Blotting, Western</subject><subject>cDNA</subject><subject>Cell growth</subject><subject>Cell lines</subject><subject>Cellular biology</subject><subject>E peptide</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>genes</subject><subject>Hormones</subject><subject>Humans</subject><subject>In Vitro Techniques</subject><subject>Insulin-Like Growth Factor I - chemistry</subject><subject>Insulin-Like Growth Factor I - immunology</subject><subject>Insulin-Like Growth Factor I - metabolism</subject><subject>insulin-like growth factor IB</subject><subject>Lungs</subject><subject>man</subject><subject>Messenger RNA</subject><subject>Mitogens - chemistry</subject><subject>Mitogens - immunology</subject><subject>Mitogens - metabolism</subject><subject>Molecular Sequence Data</subject><subject>Molecules</subject><subject>nucleotide sequence</subject><subject>Peptide Fragments - metabolism</subject><subject>predictions</subject><subject>Protein hormones. Growth factors. Cytokines</subject><subject>Protein Precursors - metabolism</subject><subject>Protein Processing, Post-Translational</subject><subject>Proteins</subject><subject>Receptors</subject><subject>Receptors, Cell Surface - metabolism</subject><subject>Tumor Cells, Cultured</subject><issn>0027-8424</issn><issn>1091-6490</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1992</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkc1v0zAYxiMEGmVw5gIoQghO6ewk_pK4dGMblYrYAc6W47xZXRK72M4G_z0OLR1wgIstPc_v_bCfLHuK0RwjVp1srQpzLuaYzXkS7mUzjAQuaC3Q_WyGUMkKXpf1w-xRCBuEkCAcHWVHuCoJreksGxb5BxPdNVij8yvYRtNCvhim89xq10Kb35q4NjaP6yQdkHduUEl03U99acPYG1uszBfIL727jev8QunofL48za-8Wzs_OAuPswed6gM82d_H2eeL809n74vVx8vl2WJVaFKLWJRtl7aDloNgNQcOgAVnijREkKoGDZwDFV2Dm4a0jWoVUliVrEM10yWjtDrO3u76bsdmgFaDjV71cuvNoPx36ZSRfzrWrOW1u5G14JSk8tf7cu--jhCiHEzQ0PfKghuDZBVmFBP-XxDTCiEmUAJf_gVu3Oht-gNZIlwyhNkEnewg7V0IHrrDwhjJKW05pS25kJjJKe1U8fz3d97xu3iT_2rvq6BV33lltQkHjBBSUj61ebPHpv6_3Ls5shv7PsK3mMgX_yQT8GwHbEJK_0CUFcUVqqsfwXTUcA</recordid><startdate>19920901</startdate><enddate>19920901</enddate><creator>Siegfried, Jill M.</creator><creator>Kasprzyk, Philip G.</creator><creator>Treston, Anthony M.</creator><creator>Mulshine, James L.</creator><creator>Quinn, Kathryn A.</creator><creator>Cuttitta, Frank</creator><general>National Academy of Sciences of the United States of America</general><general>National Acad Sciences</general><general>National Academy of 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>7QG</scope><scope>7QL</scope><scope>7QP</scope><scope>7QR</scope><scope>7SN</scope><scope>7SS</scope><scope>7T5</scope><scope>7TK</scope><scope>7TM</scope><scope>7TO</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope><scope>7T3</scope><scope>M81</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>19920901</creationdate><title>A Mitogenic Peptide Amide Encoded within the E Peptide Domain of the Insulin-Like Growth Factor IB Prohormone</title><author>Siegfried, Jill M. ; Kasprzyk, Philip G. ; Treston, Anthony M. ; Mulshine, James L. ; Quinn, Kathryn A. ; Cuttitta, Frank</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c549t-2df564ed8e9748e8ee1987a5b59534ece88e69fb1bb5dbada0a1a27f047c27663</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1992</creationdate><topic>Amides</topic><topic>Amino Acid Sequence</topic><topic>Amino acids</topic><topic>Analytical, structural and metabolic biochemistry</topic><topic>Base Sequence</topic><topic>Biological and medical sciences</topic><topic>Blotting, Western</topic><topic>cDNA</topic><topic>Cell growth</topic><topic>Cell lines</topic><topic>Cellular biology</topic><topic>E peptide</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>genes</topic><topic>Hormones</topic><topic>Humans</topic><topic>In Vitro Techniques</topic><topic>Insulin-Like Growth Factor I - chemistry</topic><topic>Insulin-Like Growth Factor I - immunology</topic><topic>Insulin-Like Growth Factor I - metabolism</topic><topic>insulin-like growth factor IB</topic><topic>Lungs</topic><topic>man</topic><topic>Messenger RNA</topic><topic>Mitogens - chemistry</topic><topic>Mitogens - immunology</topic><topic>Mitogens - metabolism</topic><topic>Molecular Sequence Data</topic><topic>Molecules</topic><topic>nucleotide sequence</topic><topic>Peptide Fragments - metabolism</topic><topic>predictions</topic><topic>Protein hormones. Growth factors. Cytokines</topic><topic>Protein Precursors - metabolism</topic><topic>Protein Processing, Post-Translational</topic><topic>Proteins</topic><topic>Receptors</topic><topic>Receptors, Cell Surface - metabolism</topic><topic>Tumor Cells, Cultured</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Siegfried, Jill M.</creatorcontrib><creatorcontrib>Kasprzyk, Philip G.</creatorcontrib><creatorcontrib>Treston, Anthony M.</creatorcontrib><creatorcontrib>Mulshine, James L.</creatorcontrib><creatorcontrib>Quinn, Kathryn A.</creatorcontrib><creatorcontrib>Cuttitta, Frank</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>Animal Behavior Abstracts</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Ecology Abstracts</collection><collection>Entomology Abstracts (Full archive)</collection><collection>Immunology Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Oncogenes and Growth Factors Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>Human Genome Abstracts</collection><collection>Biochemistry Abstracts 3</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Siegfried, Jill M.</au><au>Kasprzyk, Philip G.</au><au>Treston, Anthony M.</au><au>Mulshine, James L.</au><au>Quinn, Kathryn A.</au><au>Cuttitta, Frank</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>A Mitogenic Peptide Amide Encoded within the E Peptide Domain of the Insulin-Like Growth Factor IB Prohormone</atitle><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle><addtitle>Proc Natl Acad Sci U S A</addtitle><date>1992-09-01</date><risdate>1992</risdate><volume>89</volume><issue>17</issue><spage>8107</spage><epage>8111</epage><pages>8107-8111</pages><issn>0027-8424</issn><eissn>1091-6490</eissn><coden>PNASA6</coden><abstract>We have identified an amino acid sequence within the E peptide of the insulin-like growth factor IB (IGF-IB) precursor that is biologically active and designated this peptide insulin-like growth factor IB-(103-124) E1amide (IBE1). Its existence was predicted by a flanking Gly-Lys-Lys-Lys, a signal sequence for sequential proteolytic cleavage and peptidyl C-terminal amidation. A synthetic analog of the predicted IBE1peptide, designated Y-23-R-NH2, was generated with tyrosine added at position 0. This peptide at 2-20 nM had growth-promoting effects on both normal and malignant human bronchial epithelial cells. Y-23-R-NH2bound to specific high-affinity receptors (Kd= 2.8 ± 1.4 x 10-11M) present at 1-2 * 104binding sites per cell. Ligand binding was not inhibited byrecombinant insulin or recombinant IGF-I. Furthermore, a monoclonal antibody antagonist to the IGF-I receptor (αIR3) did not suppress the proliferative response induced by Y-23-R-NH2. In addition, C-terminal amidation was shown to be important in receptor recognition since the free-acid analog of IBE1(Y-23-R-OH) did not effectively compete for binding and was not a potent agonist of proliferation. Immunoblot analysis of human lung tumor cell line extracts using an antibody raised against Y-23-R-NH2detected a low molecular mass band of ≈5 kDa, implying that a protein product is produced that has immunological similarity to IBE1. Extracts of human, mammalian, and avian livers analyzed on an immunoblot with the anti-Y-23-R-NH2antibody contained proteins of ≈21 kDa that were specifically recognized by the antiserum and presumably represent an IGF-I precursor molecule. This implies that in species where an IGF-I mRNA with homology to the human IGF-IB E domain has not yet been described, an alternate mRNA must be produced that contains a sequence similar to that of the midportion of the human IGF-IB E domain. Our findings demonstrate that IBE1is a growth factor that mediates its effect through a specific high-affinity receptor and is most likely conserved in many species.</abstract><cop>Washington, DC</cop><pub>National Academy of Sciences of the United States of America</pub><pmid>1325646</pmid><doi>10.1073/pnas.89.17.8107</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
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subjects | Amides Amino Acid Sequence Amino acids Analytical, structural and metabolic biochemistry Base Sequence Biological and medical sciences Blotting, Western cDNA Cell growth Cell lines Cellular biology E peptide Fundamental and applied biological sciences. Psychology genes Hormones Humans In Vitro Techniques Insulin-Like Growth Factor I - chemistry Insulin-Like Growth Factor I - immunology Insulin-Like Growth Factor I - metabolism insulin-like growth factor IB Lungs man Messenger RNA Mitogens - chemistry Mitogens - immunology Mitogens - metabolism Molecular Sequence Data Molecules nucleotide sequence Peptide Fragments - metabolism predictions Protein hormones. Growth factors. Cytokines Protein Precursors - metabolism Protein Processing, Post-Translational Proteins Receptors Receptors, Cell Surface - metabolism Tumor Cells, Cultured |
title | A Mitogenic Peptide Amide Encoded within the E Peptide Domain of the Insulin-Like Growth Factor IB Prohormone |
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