Functional and immunological distinction between insulin-like growth factor I receptor subtypes in KB cells
Subtypes of insulin-growth factor I (IGF-I) receptors, including hybrid receptors containing insulin receptor alpha beta dimers associated with IGF-I receptor alpha beta dimers, have been described in a number of systems. The molecular basis of the multiple subtypes and their functional significance...
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| Veröffentlicht in: | The Journal of biological chemistry 1992-06, Vol.267 (16), p.11470-11475 |
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| creator | GAROFALO, R. S BARENTON, B |
| description | Subtypes of insulin-growth factor I (IGF-I) receptors, including hybrid receptors containing insulin receptor alpha beta dimers
associated with IGF-I receptor alpha beta dimers, have been described in a number of systems. The molecular basis of the multiple
subtypes and their functional significance is not understood. Ligand-dependent phosphorylation of insulin and IGF-I receptors
and immunoprecipitation with antipeptide and monoclonal antibodies have been used to characterize the subpopulations of these
receptors in the human KB cell line. IGF-I receptors exhibit beta subunits of 95 and 102 kDa in these cells. IGF-I receptors
containing 102-kDa beta subunits are immunoprecipitated by the IGF-I receptor-specific antibody alpha-IR3. Antibody alpha-IR3
does not appear to recognize a hybrid receptor in these cells. However, an antipeptide antibody against the carboxyl-terminal
domain of the insulin receptor (AbP5) immunoprecipitates a population of receptors phosphorylated in response to IGF-I (1
nM) which contains both 95- and 102-kDa beta subunits. These receptors must be hybrid complexes because AbP5 does not recognize
the 102-kDa beta subunit directly. The inability of antibody alpha-IR3 to recognize these complexes suggests that their IGF-I
receptor alpha subunits must differ from typical IGF-I receptor alpha subunits either in primary sequence or conformation.
Therefore, KB cells may contain more than one type of IGF-I receptor alpha subunit. Hybrid IGF-I receptors can also be distinguished
from homotypic IGF-I receptors by their responsiveness to IGF-II. Stimulation of autophosphorylation in hybrid IGF-I receptors
by IGF-I is 3-4-fold greater than that seen in response to IGF-II. In contrast, IGF-I and IGF-II are nearly equipotent in
stimulating autophosphorylation in the alpha-IR3-reactive receptor population. This suggests the existence of functionally
distinct receptor subtypes which may differ in their ability to mediate the biological effects of IGF-II. |
| doi_str_mv | 10.1016/S0021-9258(19)49933-X |
| format | Article |
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associated with IGF-I receptor alpha beta dimers, have been described in a number of systems. The molecular basis of the multiple
subtypes and their functional significance is not understood. Ligand-dependent phosphorylation of insulin and IGF-I receptors
and immunoprecipitation with antipeptide and monoclonal antibodies have been used to characterize the subpopulations of these
receptors in the human KB cell line. IGF-I receptors exhibit beta subunits of 95 and 102 kDa in these cells. IGF-I receptors
containing 102-kDa beta subunits are immunoprecipitated by the IGF-I receptor-specific antibody alpha-IR3. Antibody alpha-IR3
does not appear to recognize a hybrid receptor in these cells. However, an antipeptide antibody against the carboxyl-terminal
domain of the insulin receptor (AbP5) immunoprecipitates a population of receptors phosphorylated in response to IGF-I (1
nM) which contains both 95- and 102-kDa beta subunits. These receptors must be hybrid complexes because AbP5 does not recognize
the 102-kDa beta subunit directly. The inability of antibody alpha-IR3 to recognize these complexes suggests that their IGF-I
receptor alpha subunits must differ from typical IGF-I receptor alpha subunits either in primary sequence or conformation.
Therefore, KB cells may contain more than one type of IGF-I receptor alpha subunit. Hybrid IGF-I receptors can also be distinguished
from homotypic IGF-I receptors by their responsiveness to IGF-II. Stimulation of autophosphorylation in hybrid IGF-I receptors
by IGF-I is 3-4-fold greater than that seen in response to IGF-II. In contrast, IGF-I and IGF-II are nearly equipotent in
stimulating autophosphorylation in the alpha-IR3-reactive receptor population. This suggests the existence of functionally
distinct receptor subtypes which may differ in their ability to mediate the biological effects of IGF-II.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1016/S0021-9258(19)49933-X</identifier><identifier>PMID: 1317868</identifier><identifier>CODEN: JBCHA3</identifier><language>eng</language><publisher>Bethesda, MD: American Society for Biochemistry and Molecular Biology</publisher><subject>Biological and medical sciences ; Blotting, Western ; Cell Membrane - metabolism ; Cell receptors ; Cell structures and functions ; Computer Science ; Cross-Linking Reagents ; Fundamental and applied biological sciences. Psychology ; Hormone receptors. Growth factor receptors. Cytokine receptors. Prostaglandin receptors ; Humans ; immunological aspects ; Insulin-Like Growth Factor I - metabolism ; Insulin-Like Growth Factor II - metabolism ; insulin-like growth factor-I ; isoforms ; KB cells ; Life Sciences ; membrane proteins ; Molecular and cellular biology ; Phosphorylation ; Precipitin Tests ; protein-tyrosine kinase ; receptors ; Receptors, Cell Surface - immunology ; Receptors, Cell Surface - metabolism ; Receptors, Somatomedin ; Tumor Cells, Cultured</subject><ispartof>The Journal of biological chemistry, 1992-06, Vol.267 (16), p.11470-11475</ispartof><rights>1993 INIST-CNRS</rights><rights>Distributed under a Creative Commons Attribution 4.0 International License</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c474t-a665f0588ab06a9b6094d66965ea8a81c0d22763bacd180093e3230a58b710863</citedby><cites>FETCH-LOGICAL-c474t-a665f0588ab06a9b6094d66965ea8a81c0d22763bacd180093e3230a58b710863</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>230,314,776,780,881,27901,27902</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=4539017$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/1317868$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://hal.inrae.fr/hal-02704978$$DView record in HAL$$Hfree_for_read</backlink></links><search><creatorcontrib>GAROFALO, R. S</creatorcontrib><creatorcontrib>BARENTON, B</creatorcontrib><title>Functional and immunological distinction between insulin-like growth factor I receptor subtypes in KB cells</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>Subtypes of insulin-growth factor I (IGF-I) receptors, including hybrid receptors containing insulin receptor alpha beta dimers
associated with IGF-I receptor alpha beta dimers, have been described in a number of systems. The molecular basis of the multiple
subtypes and their functional significance is not understood. Ligand-dependent phosphorylation of insulin and IGF-I receptors
and immunoprecipitation with antipeptide and monoclonal antibodies have been used to characterize the subpopulations of these
receptors in the human KB cell line. IGF-I receptors exhibit beta subunits of 95 and 102 kDa in these cells. IGF-I receptors
containing 102-kDa beta subunits are immunoprecipitated by the IGF-I receptor-specific antibody alpha-IR3. Antibody alpha-IR3
does not appear to recognize a hybrid receptor in these cells. However, an antipeptide antibody against the carboxyl-terminal
domain of the insulin receptor (AbP5) immunoprecipitates a population of receptors phosphorylated in response to IGF-I (1
nM) which contains both 95- and 102-kDa beta subunits. These receptors must be hybrid complexes because AbP5 does not recognize
the 102-kDa beta subunit directly. The inability of antibody alpha-IR3 to recognize these complexes suggests that their IGF-I
receptor alpha subunits must differ from typical IGF-I receptor alpha subunits either in primary sequence or conformation.
Therefore, KB cells may contain more than one type of IGF-I receptor alpha subunit. Hybrid IGF-I receptors can also be distinguished
from homotypic IGF-I receptors by their responsiveness to IGF-II. Stimulation of autophosphorylation in hybrid IGF-I receptors
by IGF-I is 3-4-fold greater than that seen in response to IGF-II. In contrast, IGF-I and IGF-II are nearly equipotent in
stimulating autophosphorylation in the alpha-IR3-reactive receptor population. This suggests the existence of functionally
distinct receptor subtypes which may differ in their ability to mediate the biological effects of IGF-II.</description><subject>Biological and medical sciences</subject><subject>Blotting, Western</subject><subject>Cell Membrane - metabolism</subject><subject>Cell receptors</subject><subject>Cell structures and functions</subject><subject>Computer Science</subject><subject>Cross-Linking Reagents</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Hormone receptors. Growth factor receptors. Cytokine receptors. Prostaglandin receptors</subject><subject>Humans</subject><subject>immunological aspects</subject><subject>Insulin-Like Growth Factor I - metabolism</subject><subject>Insulin-Like Growth Factor II - metabolism</subject><subject>insulin-like growth factor-I</subject><subject>isoforms</subject><subject>KB cells</subject><subject>Life Sciences</subject><subject>membrane proteins</subject><subject>Molecular and cellular biology</subject><subject>Phosphorylation</subject><subject>Precipitin Tests</subject><subject>protein-tyrosine kinase</subject><subject>receptors</subject><subject>Receptors, Cell Surface - immunology</subject><subject>Receptors, Cell Surface - metabolism</subject><subject>Receptors, Somatomedin</subject><subject>Tumor Cells, Cultured</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1992</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkUtv1DAUhS0EKtOBn1DJC4ToIuAbJ34s24o-xEgsAGl2luM4E9MkHuyEUf89TjOaLvHG1j3fvT72QegCyGcgwL78ICSHTOal-ATyspCS0mz7Cq2ACJrRErav0eqEvEXnMf4maRUSztAZUOCCiRV6vJ0GMzo_6A7rocau76fBd37nTKrULo5u0XFlx4O1A3ZDnDo3ZJ17tHgX_GFscaPN6AN-wMEau5-PcarGp72NCcffrrGxXRffoTeN7qJ9f9zX6Nft158399nm-93DzdUmMwUvxkwzVjakFEJXhGlZMSKLmjHJSquFFmBIneec0UqbGgQhklqaU6JLUfH0eEbX6HKZ2-pO7YPrdXhSXjt1f7VRc43kPP0DF38hsR8Xdh_8n8nGUfUuzm71YP0UFc8lz4HQ_4LAKCuLRK5RuYAm-BiDbU4WgKg5OfWcnJpjUSDVc3Jqm_oujhdMVW_rl64lqqR_OOo6pmyaoAfj4gkrSioJ8Besdbv24IJVlfOmtb3KGU8uFUDBCf0HY9GsFQ</recordid><startdate>19920605</startdate><enddate>19920605</enddate><creator>GAROFALO, R. S</creator><creator>BARENTON, B</creator><general>American Society for Biochemistry and Molecular Biology</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>8FD</scope><scope>FR3</scope><scope>M7Z</scope><scope>P64</scope><scope>7X8</scope><scope>1XC</scope></search><sort><creationdate>19920605</creationdate><title>Functional and immunological distinction between insulin-like growth factor I receptor subtypes in KB cells</title><author>GAROFALO, R. S ; BARENTON, B</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c474t-a665f0588ab06a9b6094d66965ea8a81c0d22763bacd180093e3230a58b710863</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1992</creationdate><topic>Biological and medical sciences</topic><topic>Blotting, Western</topic><topic>Cell Membrane - metabolism</topic><topic>Cell receptors</topic><topic>Cell structures and functions</topic><topic>Computer Science</topic><topic>Cross-Linking Reagents</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Hormone receptors. Growth factor receptors. Cytokine receptors. Prostaglandin receptors</topic><topic>Humans</topic><topic>immunological aspects</topic><topic>Insulin-Like Growth Factor I - metabolism</topic><topic>Insulin-Like Growth Factor II - metabolism</topic><topic>insulin-like growth factor-I</topic><topic>isoforms</topic><topic>KB cells</topic><topic>Life Sciences</topic><topic>membrane proteins</topic><topic>Molecular and cellular biology</topic><topic>Phosphorylation</topic><topic>Precipitin Tests</topic><topic>protein-tyrosine kinase</topic><topic>receptors</topic><topic>Receptors, Cell Surface - immunology</topic><topic>Receptors, Cell Surface - metabolism</topic><topic>Receptors, Somatomedin</topic><topic>Tumor Cells, Cultured</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>GAROFALO, R. S</creatorcontrib><creatorcontrib>BARENTON, B</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>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>Biochemistry Abstracts 1</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>MEDLINE - Academic</collection><collection>Hyper Article en Ligne (HAL)</collection><jtitle>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>GAROFALO, R. S</au><au>BARENTON, B</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Functional and immunological distinction between insulin-like growth factor I receptor subtypes in KB cells</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>1992-06-05</date><risdate>1992</risdate><volume>267</volume><issue>16</issue><spage>11470</spage><epage>11475</epage><pages>11470-11475</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><coden>JBCHA3</coden><abstract>Subtypes of insulin-growth factor I (IGF-I) receptors, including hybrid receptors containing insulin receptor alpha beta dimers
associated with IGF-I receptor alpha beta dimers, have been described in a number of systems. The molecular basis of the multiple
subtypes and their functional significance is not understood. Ligand-dependent phosphorylation of insulin and IGF-I receptors
and immunoprecipitation with antipeptide and monoclonal antibodies have been used to characterize the subpopulations of these
receptors in the human KB cell line. IGF-I receptors exhibit beta subunits of 95 and 102 kDa in these cells. IGF-I receptors
containing 102-kDa beta subunits are immunoprecipitated by the IGF-I receptor-specific antibody alpha-IR3. Antibody alpha-IR3
does not appear to recognize a hybrid receptor in these cells. However, an antipeptide antibody against the carboxyl-terminal
domain of the insulin receptor (AbP5) immunoprecipitates a population of receptors phosphorylated in response to IGF-I (1
nM) which contains both 95- and 102-kDa beta subunits. These receptors must be hybrid complexes because AbP5 does not recognize
the 102-kDa beta subunit directly. The inability of antibody alpha-IR3 to recognize these complexes suggests that their IGF-I
receptor alpha subunits must differ from typical IGF-I receptor alpha subunits either in primary sequence or conformation.
Therefore, KB cells may contain more than one type of IGF-I receptor alpha subunit. Hybrid IGF-I receptors can also be distinguished
from homotypic IGF-I receptors by their responsiveness to IGF-II. Stimulation of autophosphorylation in hybrid IGF-I receptors
by IGF-I is 3-4-fold greater than that seen in response to IGF-II. In contrast, IGF-I and IGF-II are nearly equipotent in
stimulating autophosphorylation in the alpha-IR3-reactive receptor population. This suggests the existence of functionally
distinct receptor subtypes which may differ in their ability to mediate the biological effects of IGF-II.</abstract><cop>Bethesda, MD</cop><pub>American Society for Biochemistry and Molecular Biology</pub><pmid>1317868</pmid><doi>10.1016/S0021-9258(19)49933-X</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | The Journal of biological chemistry, 1992-06, Vol.267 (16), p.11470-11475 |
| issn | 0021-9258 1083-351X |
| language | eng |
| recordid | cdi_hal_primary_oai_HAL_hal_02704978v1 |
| source | MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Alma/SFX Local Collection |
| subjects | Biological and medical sciences Blotting, Western Cell Membrane - metabolism Cell receptors Cell structures and functions Computer Science Cross-Linking Reagents Fundamental and applied biological sciences. Psychology Hormone receptors. Growth factor receptors. Cytokine receptors. Prostaglandin receptors Humans immunological aspects Insulin-Like Growth Factor I - metabolism Insulin-Like Growth Factor II - metabolism insulin-like growth factor-I isoforms KB cells Life Sciences membrane proteins Molecular and cellular biology Phosphorylation Precipitin Tests protein-tyrosine kinase receptors Receptors, Cell Surface - immunology Receptors, Cell Surface - metabolism Receptors, Somatomedin Tumor Cells, Cultured |
| title | Functional and immunological distinction between insulin-like growth factor I receptor subtypes in KB cells |
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