High affinity human IgE receptor (Fc epsilon RI). Analysis of functional domains of the alpha-subunit with monoclonal antibodies
The binding of IgE to the high affinity Fc epsilon receptor (Fc epsilon RI) on mast cells and basophils is mediated by the alpha-subunit of the tetrameric receptor complex. Based on sequence homologies, the 50-kDa alpha-subunit is a member of the immunoglobulin superfamily of proteins and has two pr...
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| Veröffentlicht in: | The Journal of biological chemistry 1991-06, Vol.266 (17), p.11245-11251 |
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| container_title | The Journal of biological chemistry |
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| creator | RISKE, F HAKIMI, J MALLAMACI, M GRIFFIN, M PILSON, B TOBKES, N LIN, P DANHO, W KOCHAN, J CHIZZONITE, R |
| description | The binding of IgE to the high affinity Fc epsilon receptor (Fc epsilon RI) on mast cells and basophils is mediated by the
alpha-subunit of the tetrameric receptor complex. Based on sequence homologies, the 50-kDa alpha-subunit is a member of the
immunoglobulin superfamily of proteins and has two predicted disulfide-bonded loops. Monoclonal antibodies specific for the
human alpha-subunit have been identified and separated into two major classes: inhibitory and noninhibitory antibodies. Inhibitory
antibodies (i.e. 15A5) block 125I-IgE binding to a recombinant chimeric alpha-subunit (ch-alpha-protein) expressed on Chinese
hamster ovary cells and immunoprecipitate 125I-labeled purified ch-alpha-protein. Noninhibitory antibodies (i.e. 22E7) immunoprecipitate
both 125I-labeled ch-alpha-protein and the soluble complex of 125I-IgE cross-linked to ch-alpha-protein but do not block 125I-IgE
binding to the ch-alpha-protein expressed on Chinese hamster ovary cells. Both classes of antibodies bind to natural Fc epsilon
RI present on human basophils and induce histamine release from these cells. Inhibitory antibody 15A5 specifically binds to
a peptide corresponding to amino acids 125-140 of the putative second domain of the alpha-subunit sequence. All the inhibitory
antibodies compete with 125I-15A5 for binding to the ch-alpha-protein, indicating that these antibodies recognize inhibitory
epitopes that are either identical or sterically overlapping. Noninhibitory antibodies (i.e. 22E7) do not block 125I-15A5
binding to the ch-alpha-protein. These data suggest that antibodies binding to the predicted second domain of the alpha-subunit
can inhibit IgE binding to the alpha-subunit, while antibodies binding at a distance from this site do not inhibit IgE binding.
These inhibitory antibodies may block IgE binding to the ch-alpha-protein by direct overlap, steric inhibition, or induced
conformational changes of the receptor contact points for IgE. |
| doi_str_mv | 10.1016/S0021-9258(18)99155-6 |
| format | Article |
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alpha-subunit of the tetrameric receptor complex. Based on sequence homologies, the 50-kDa alpha-subunit is a member of the
immunoglobulin superfamily of proteins and has two predicted disulfide-bonded loops. Monoclonal antibodies specific for the
human alpha-subunit have been identified and separated into two major classes: inhibitory and noninhibitory antibodies. Inhibitory
antibodies (i.e. 15A5) block 125I-IgE binding to a recombinant chimeric alpha-subunit (ch-alpha-protein) expressed on Chinese
hamster ovary cells and immunoprecipitate 125I-labeled purified ch-alpha-protein. Noninhibitory antibodies (i.e. 22E7) immunoprecipitate
both 125I-labeled ch-alpha-protein and the soluble complex of 125I-IgE cross-linked to ch-alpha-protein but do not block 125I-IgE
binding to the ch-alpha-protein expressed on Chinese hamster ovary cells. Both classes of antibodies bind to natural Fc epsilon
RI present on human basophils and induce histamine release from these cells. Inhibitory antibody 15A5 specifically binds to
a peptide corresponding to amino acids 125-140 of the putative second domain of the alpha-subunit sequence. All the inhibitory
antibodies compete with 125I-15A5 for binding to the ch-alpha-protein, indicating that these antibodies recognize inhibitory
epitopes that are either identical or sterically overlapping. Noninhibitory antibodies (i.e. 22E7) do not block 125I-15A5
binding to the ch-alpha-protein. These data suggest that antibodies binding to the predicted second domain of the alpha-subunit
can inhibit IgE binding to the alpha-subunit, while antibodies binding at a distance from this site do not inhibit IgE binding.
These inhibitory antibodies may block IgE binding to the ch-alpha-protein by direct overlap, steric inhibition, or induced
conformational changes of the receptor contact points for IgE.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1016/S0021-9258(18)99155-6</identifier><identifier>PMID: 1710221</identifier><identifier>CODEN: JBCHA3</identifier><language>eng</language><publisher>Bethesda, MD: American Society for Biochemistry and Molecular Biology</publisher><subject>Animals ; Antibodies, Monoclonal ; Antigen-Antibody Complex ; Antigens, Differentiation, B-Lymphocyte - genetics ; Antigens, Differentiation, B-Lymphocyte - metabolism ; Basophils - immunology ; Biological and medical sciences ; Cell receptors ; Cell structures and functions ; Chimera ; Fluorescent Antibody Technique ; Fundamental and applied biological sciences. Psychology ; Histamine Release ; Humans ; Hybridomas - immunology ; Immunoglobulin E - isolation & purification ; Immunoglobulin E - metabolism ; Kinetics ; leukocytes (basophilic) ; Macromolecular Substances ; mast cells ; Mice ; Mice, Inbred BALB C - immunology ; Miscellaneous ; Molecular and cellular biology ; Molecular Weight ; Rats ; Receptors, Fc - genetics ; Receptors, Fc - metabolism ; Receptors, IgE</subject><ispartof>The Journal of biological chemistry, 1991-06, Vol.266 (17), p.11245-11251</ispartof><rights>1992 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c492t-2d0ab8b28204b0ce709a53c6ef75a357b1e94f2f3540c2f9f85d51b2f16a98183</citedby><cites>FETCH-LOGICAL-c492t-2d0ab8b28204b0ce709a53c6ef75a357b1e94f2f3540c2f9f85d51b2f16a98183</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27901,27902</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=4960917$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/1710221$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>RISKE, F</creatorcontrib><creatorcontrib>HAKIMI, J</creatorcontrib><creatorcontrib>MALLAMACI, M</creatorcontrib><creatorcontrib>GRIFFIN, M</creatorcontrib><creatorcontrib>PILSON, B</creatorcontrib><creatorcontrib>TOBKES, N</creatorcontrib><creatorcontrib>LIN, P</creatorcontrib><creatorcontrib>DANHO, W</creatorcontrib><creatorcontrib>KOCHAN, J</creatorcontrib><creatorcontrib>CHIZZONITE, R</creatorcontrib><title>High affinity human IgE receptor (Fc epsilon RI). Analysis of functional domains of the alpha-subunit with monoclonal antibodies</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>The binding of IgE to the high affinity Fc epsilon receptor (Fc epsilon RI) on mast cells and basophils is mediated by the
alpha-subunit of the tetrameric receptor complex. Based on sequence homologies, the 50-kDa alpha-subunit is a member of the
immunoglobulin superfamily of proteins and has two predicted disulfide-bonded loops. Monoclonal antibodies specific for the
human alpha-subunit have been identified and separated into two major classes: inhibitory and noninhibitory antibodies. Inhibitory
antibodies (i.e. 15A5) block 125I-IgE binding to a recombinant chimeric alpha-subunit (ch-alpha-protein) expressed on Chinese
hamster ovary cells and immunoprecipitate 125I-labeled purified ch-alpha-protein. Noninhibitory antibodies (i.e. 22E7) immunoprecipitate
both 125I-labeled ch-alpha-protein and the soluble complex of 125I-IgE cross-linked to ch-alpha-protein but do not block 125I-IgE
binding to the ch-alpha-protein expressed on Chinese hamster ovary cells. Both classes of antibodies bind to natural Fc epsilon
RI present on human basophils and induce histamine release from these cells. Inhibitory antibody 15A5 specifically binds to
a peptide corresponding to amino acids 125-140 of the putative second domain of the alpha-subunit sequence. All the inhibitory
antibodies compete with 125I-15A5 for binding to the ch-alpha-protein, indicating that these antibodies recognize inhibitory
epitopes that are either identical or sterically overlapping. Noninhibitory antibodies (i.e. 22E7) do not block 125I-15A5
binding to the ch-alpha-protein. These data suggest that antibodies binding to the predicted second domain of the alpha-subunit
can inhibit IgE binding to the alpha-subunit, while antibodies binding at a distance from this site do not inhibit IgE binding.
These inhibitory antibodies may block IgE binding to the ch-alpha-protein by direct overlap, steric inhibition, or induced
conformational changes of the receptor contact points for IgE.</description><subject>Animals</subject><subject>Antibodies, Monoclonal</subject><subject>Antigen-Antibody Complex</subject><subject>Antigens, Differentiation, B-Lymphocyte - genetics</subject><subject>Antigens, Differentiation, B-Lymphocyte - metabolism</subject><subject>Basophils - immunology</subject><subject>Biological and medical sciences</subject><subject>Cell receptors</subject><subject>Cell structures and functions</subject><subject>Chimera</subject><subject>Fluorescent Antibody Technique</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Histamine Release</subject><subject>Humans</subject><subject>Hybridomas - immunology</subject><subject>Immunoglobulin E - isolation & purification</subject><subject>Immunoglobulin E - metabolism</subject><subject>Kinetics</subject><subject>leukocytes (basophilic)</subject><subject>Macromolecular Substances</subject><subject>mast cells</subject><subject>Mice</subject><subject>Mice, Inbred BALB C - immunology</subject><subject>Miscellaneous</subject><subject>Molecular and cellular biology</subject><subject>Molecular Weight</subject><subject>Rats</subject><subject>Receptors, Fc - genetics</subject><subject>Receptors, Fc - metabolism</subject><subject>Receptors, IgE</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1991</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkUtr3TAQRkVpSG-S_oSAFqUkC6ca2ZKlZQh5XAgU0hayE5IsxSq25Fo24e760-v7IFlWG8HMmW-EDkLnQK6AAP_2gxAKhaRMXIC4lBIYK_gHtAIiyqJk8PwRrd6QT-gk599kOZWEY3QMNRBKYYX-PoSXFmvvQwzTBrdzryNev9zi0Vk3TGnEF3cWuyGHLkX8tL68wtdRd5scMk4e-znaKaSlgpvU6xB31al1WHdDq4s8m3kJxq9hanGfYrLdDtZxCiY1weUzdOR1l93nw32Kft3d_rx5KB6_369vrh8LW0k6FbQh2ghDBSWVIdbVRGpWWu58zXTJagNOVp76klXEUi-9YA0DQz1wLQWI8hR93ecOY_ozuzypPmTruk5Hl-asBGGylJz9FwQOdSWrLcj2oB1TzqPzahhDr8eNAqK2itROkdr-vwKhdooUX-bODwtm07vmfWrvZOl_OfR1trrzo4425DeskpxIqN-xdjH4GkanTEi2db2inC9hCoAur_wHKGmlSw</recordid><startdate>19910615</startdate><enddate>19910615</enddate><creator>RISKE, F</creator><creator>HAKIMI, J</creator><creator>MALLAMACI, M</creator><creator>GRIFFIN, M</creator><creator>PILSON, B</creator><creator>TOBKES, N</creator><creator>LIN, P</creator><creator>DANHO, W</creator><creator>KOCHAN, J</creator><creator>CHIZZONITE, R</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></search><sort><creationdate>19910615</creationdate><title>High affinity human IgE receptor (Fc epsilon RI). Analysis of functional domains of the alpha-subunit with monoclonal antibodies</title><author>RISKE, F ; HAKIMI, J ; MALLAMACI, M ; GRIFFIN, M ; PILSON, B ; TOBKES, N ; LIN, P ; DANHO, W ; KOCHAN, J ; CHIZZONITE, R</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c492t-2d0ab8b28204b0ce709a53c6ef75a357b1e94f2f3540c2f9f85d51b2f16a98183</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1991</creationdate><topic>Animals</topic><topic>Antibodies, Monoclonal</topic><topic>Antigen-Antibody Complex</topic><topic>Antigens, Differentiation, B-Lymphocyte - genetics</topic><topic>Antigens, Differentiation, B-Lymphocyte - metabolism</topic><topic>Basophils - immunology</topic><topic>Biological and medical sciences</topic><topic>Cell receptors</topic><topic>Cell structures and functions</topic><topic>Chimera</topic><topic>Fluorescent Antibody Technique</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Histamine Release</topic><topic>Humans</topic><topic>Hybridomas - immunology</topic><topic>Immunoglobulin E - isolation & purification</topic><topic>Immunoglobulin E - metabolism</topic><topic>Kinetics</topic><topic>leukocytes (basophilic)</topic><topic>Macromolecular Substances</topic><topic>mast cells</topic><topic>Mice</topic><topic>Mice, Inbred BALB C - immunology</topic><topic>Miscellaneous</topic><topic>Molecular and cellular biology</topic><topic>Molecular Weight</topic><topic>Rats</topic><topic>Receptors, Fc - genetics</topic><topic>Receptors, Fc - metabolism</topic><topic>Receptors, IgE</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>RISKE, F</creatorcontrib><creatorcontrib>HAKIMI, J</creatorcontrib><creatorcontrib>MALLAMACI, M</creatorcontrib><creatorcontrib>GRIFFIN, M</creatorcontrib><creatorcontrib>PILSON, B</creatorcontrib><creatorcontrib>TOBKES, N</creatorcontrib><creatorcontrib>LIN, P</creatorcontrib><creatorcontrib>DANHO, W</creatorcontrib><creatorcontrib>KOCHAN, J</creatorcontrib><creatorcontrib>CHIZZONITE, R</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><jtitle>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>RISKE, F</au><au>HAKIMI, J</au><au>MALLAMACI, M</au><au>GRIFFIN, M</au><au>PILSON, B</au><au>TOBKES, N</au><au>LIN, P</au><au>DANHO, W</au><au>KOCHAN, J</au><au>CHIZZONITE, R</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>High affinity human IgE receptor (Fc epsilon RI). Analysis of functional domains of the alpha-subunit with monoclonal antibodies</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>1991-06-15</date><risdate>1991</risdate><volume>266</volume><issue>17</issue><spage>11245</spage><epage>11251</epage><pages>11245-11251</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><coden>JBCHA3</coden><abstract>The binding of IgE to the high affinity Fc epsilon receptor (Fc epsilon RI) on mast cells and basophils is mediated by the
alpha-subunit of the tetrameric receptor complex. Based on sequence homologies, the 50-kDa alpha-subunit is a member of the
immunoglobulin superfamily of proteins and has two predicted disulfide-bonded loops. Monoclonal antibodies specific for the
human alpha-subunit have been identified and separated into two major classes: inhibitory and noninhibitory antibodies. Inhibitory
antibodies (i.e. 15A5) block 125I-IgE binding to a recombinant chimeric alpha-subunit (ch-alpha-protein) expressed on Chinese
hamster ovary cells and immunoprecipitate 125I-labeled purified ch-alpha-protein. Noninhibitory antibodies (i.e. 22E7) immunoprecipitate
both 125I-labeled ch-alpha-protein and the soluble complex of 125I-IgE cross-linked to ch-alpha-protein but do not block 125I-IgE
binding to the ch-alpha-protein expressed on Chinese hamster ovary cells. Both classes of antibodies bind to natural Fc epsilon
RI present on human basophils and induce histamine release from these cells. Inhibitory antibody 15A5 specifically binds to
a peptide corresponding to amino acids 125-140 of the putative second domain of the alpha-subunit sequence. All the inhibitory
antibodies compete with 125I-15A5 for binding to the ch-alpha-protein, indicating that these antibodies recognize inhibitory
epitopes that are either identical or sterically overlapping. Noninhibitory antibodies (i.e. 22E7) do not block 125I-15A5
binding to the ch-alpha-protein. These data suggest that antibodies binding to the predicted second domain of the alpha-subunit
can inhibit IgE binding to the alpha-subunit, while antibodies binding at a distance from this site do not inhibit IgE binding.
These inhibitory antibodies may block IgE binding to the ch-alpha-protein by direct overlap, steric inhibition, or induced
conformational changes of the receptor contact points for IgE.</abstract><cop>Bethesda, MD</cop><pub>American Society for Biochemistry and Molecular Biology</pub><pmid>1710221</pmid><doi>10.1016/S0021-9258(18)99155-6</doi><tpages>7</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0021-9258 |
| ispartof | The Journal of biological chemistry, 1991-06, Vol.266 (17), p.11245-11251 |
| issn | 0021-9258 1083-351X |
| language | eng |
| recordid | cdi_proquest_miscellaneous_80593965 |
| source | MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Alma/SFX Local Collection |
| subjects | Animals Antibodies, Monoclonal Antigen-Antibody Complex Antigens, Differentiation, B-Lymphocyte - genetics Antigens, Differentiation, B-Lymphocyte - metabolism Basophils - immunology Biological and medical sciences Cell receptors Cell structures and functions Chimera Fluorescent Antibody Technique Fundamental and applied biological sciences. Psychology Histamine Release Humans Hybridomas - immunology Immunoglobulin E - isolation & purification Immunoglobulin E - metabolism Kinetics leukocytes (basophilic) Macromolecular Substances mast cells Mice Mice, Inbred BALB C - immunology Miscellaneous Molecular and cellular biology Molecular Weight Rats Receptors, Fc - genetics Receptors, Fc - metabolism Receptors, IgE |
| title | High affinity human IgE receptor (Fc epsilon RI). Analysis of functional domains of the alpha-subunit with monoclonal antibodies |
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