Photoaffinity labeling and characterization of isolated inositol 1,3,4,5-tetrakisphosphate- and inositol hexakisphosphate-binding proteins
We have isolated high affinity inositol (1,3,4,5)-tetrakisphosphate (IP4)- and inositol hexakisphosphate (IP6)-binding proteins from detergent-solubilized rat brain membranes using a P1-tethered IP4 derivative linked to an Affi-Gel support. To determine the identity, binding characteristics, and dis...
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| Veröffentlicht in: | The Journal of biological chemistry 1992-05, Vol.267 (13), p.9071-9079 |
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| container_title | The Journal of biological chemistry |
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| creator | THEIBERT, A. B ESTEVEZ, V. A MOUREY, R.J MARECEK, J. F BARROW, R. K PRESTWICH, G. D SNYDER, S. H |
| description | We have isolated high affinity inositol (1,3,4,5)-tetrakisphosphate (IP4)- and inositol hexakisphosphate (IP6)-binding proteins
from detergent-solubilized rat brain membranes using a P1-tethered IP4 derivative linked to an Affi-Gel support. To determine
the identity, binding characteristics, and distribution of the individual IP4 recognition sites, we have synthesized an IP4
photoaffinity label probe, 125I-(D,L)-1-O-[N-(4-azidosalicyloxy)-3-aminopropyl-1-phospho]- IP4 (125I-ASA-IP4). Two apparently
distinct IP4-binding proteins (IP4BP), isolated with the IP4 affinity column, display high affinity and selectivity for IP4
over inositol trisphosphate (IP3), inositol pentakisphosphate (IP5), and IP6. The first IP4-binding protein (IP4BP1) which
has a KD for IP4 of 4 nM, is comprised of a protein at 182 kDa which is specifically photolabeled with high affinity by 125I-ASA-IP4.
The second, IP4BP2, has an affinity for IP4 of 1.5 nM and contains proteins at 84 and 174 kDa, both of which are specifically
photoaffinity labeled. A putative IP6-binding protein (IP6BP), also isolated with the IP4 affinity column, binds IP6 with
a KD of 14 nM and comprises three proteins of 115, 105, and 50 kDa. The 115- and 105-kDa subunits, but not the 50-kDa subunit,
specifically incorporate the photolabel. The IP4BP (182, 174, and 84 kDa) and IP6BP (115 and 105 kDa) proteins are specifically
photolabeled in the crude membrane, partially purified, and purified fractions. These receptor-binding proteins vary in inositol
phosphate specificity and in the effects of pH, Ca2+, and heparin on IP4 photoaffinity labeling. In addition, IP4BP and IP6BP
are enriched in the brain but differ in their regional localizations within the brain. |
| doi_str_mv | 10.1016/S0021-9258(19)50390-8 |
| format | Article |
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from detergent-solubilized rat brain membranes using a P1-tethered IP4 derivative linked to an Affi-Gel support. To determine
the identity, binding characteristics, and distribution of the individual IP4 recognition sites, we have synthesized an IP4
photoaffinity label probe, 125I-(D,L)-1-O-[N-(4-azidosalicyloxy)-3-aminopropyl-1-phospho]- IP4 (125I-ASA-IP4). Two apparently
distinct IP4-binding proteins (IP4BP), isolated with the IP4 affinity column, display high affinity and selectivity for IP4
over inositol trisphosphate (IP3), inositol pentakisphosphate (IP5), and IP6. The first IP4-binding protein (IP4BP1) which
has a KD for IP4 of 4 nM, is comprised of a protein at 182 kDa which is specifically photolabeled with high affinity by 125I-ASA-IP4.
The second, IP4BP2, has an affinity for IP4 of 1.5 nM and contains proteins at 84 and 174 kDa, both of which are specifically
photoaffinity labeled. A putative IP6-binding protein (IP6BP), also isolated with the IP4 affinity column, binds IP6 with
a KD of 14 nM and comprises three proteins of 115, 105, and 50 kDa. The 115- and 105-kDa subunits, but not the 50-kDa subunit,
specifically incorporate the photolabel. The IP4BP (182, 174, and 84 kDa) and IP6BP (115 and 105 kDa) proteins are specifically
photolabeled in the crude membrane, partially purified, and purified fractions. These receptor-binding proteins vary in inositol
phosphate specificity and in the effects of pH, Ca2+, and heparin on IP4 photoaffinity labeling. In addition, IP4BP and IP6BP
are enriched in the brain but differ in their regional localizations within the brain.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1016/S0021-9258(19)50390-8</identifier><identifier>PMID: 1315747</identifier><identifier>CODEN: JBCHA3</identifier><language>eng</language><publisher>Bethesda, MD: American Society for Biochemistry and Molecular Biology</publisher><subject>Affinity Labels ; Analytical, structural and metabolic biochemistry ; Animals ; Binding and carrier proteins ; Biological and medical sciences ; brain ; Brain - metabolism ; Calcium - metabolism ; Cations, Divalent ; Chromatography, Affinity ; Fundamental and applied biological sciences. Psychology ; inositol 1,3,4,5,-tetrakisphosphate ; inositol 1,3,4,5-tetrakisphosphate-binding protein ; inositol hexakisphosphate ; inositol hexakisphosphate-binding protein ; inositol phosphates ; Inositol Phosphates - metabolism ; isolation ; Kinetics ; localization ; Male ; photoaffinity labelling ; Photochemistry ; Proteins ; Rats ; Rats, Inbred Strains ; receptors ; Receptors, Cell Surface - metabolism ; Receptors, Cytoplasmic and Nuclear ; specificity ; Substrate Specificity</subject><ispartof>The Journal of biological chemistry, 1992-05, Vol.267 (13), p.9071-9079</ispartof><rights>1992 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c3548-d97f02a378bda0c915aa6bce60b258531e4f03cf8c190e989107fb5b8a9f3aaf3</citedby><cites>FETCH-LOGICAL-c3548-d97f02a378bda0c915aa6bce60b258531e4f03cf8c190e989107fb5b8a9f3aaf3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,778,782,27911,27912</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=5309630$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/1315747$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>THEIBERT, A. B</creatorcontrib><creatorcontrib>ESTEVEZ, V. A</creatorcontrib><creatorcontrib>MOUREY, R.J</creatorcontrib><creatorcontrib>MARECEK, J. F</creatorcontrib><creatorcontrib>BARROW, R. K</creatorcontrib><creatorcontrib>PRESTWICH, G. D</creatorcontrib><creatorcontrib>SNYDER, S. H</creatorcontrib><title>Photoaffinity labeling and characterization of isolated inositol 1,3,4,5-tetrakisphosphate- and inositol hexakisphosphate-binding proteins</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>We have isolated high affinity inositol (1,3,4,5)-tetrakisphosphate (IP4)- and inositol hexakisphosphate (IP6)-binding proteins
from detergent-solubilized rat brain membranes using a P1-tethered IP4 derivative linked to an Affi-Gel support. To determine
the identity, binding characteristics, and distribution of the individual IP4 recognition sites, we have synthesized an IP4
photoaffinity label probe, 125I-(D,L)-1-O-[N-(4-azidosalicyloxy)-3-aminopropyl-1-phospho]- IP4 (125I-ASA-IP4). Two apparently
distinct IP4-binding proteins (IP4BP), isolated with the IP4 affinity column, display high affinity and selectivity for IP4
over inositol trisphosphate (IP3), inositol pentakisphosphate (IP5), and IP6. The first IP4-binding protein (IP4BP1) which
has a KD for IP4 of 4 nM, is comprised of a protein at 182 kDa which is specifically photolabeled with high affinity by 125I-ASA-IP4.
The second, IP4BP2, has an affinity for IP4 of 1.5 nM and contains proteins at 84 and 174 kDa, both of which are specifically
photoaffinity labeled. A putative IP6-binding protein (IP6BP), also isolated with the IP4 affinity column, binds IP6 with
a KD of 14 nM and comprises three proteins of 115, 105, and 50 kDa. The 115- and 105-kDa subunits, but not the 50-kDa subunit,
specifically incorporate the photolabel. The IP4BP (182, 174, and 84 kDa) and IP6BP (115 and 105 kDa) proteins are specifically
photolabeled in the crude membrane, partially purified, and purified fractions. These receptor-binding proteins vary in inositol
phosphate specificity and in the effects of pH, Ca2+, and heparin on IP4 photoaffinity labeling. In addition, IP4BP and IP6BP
are enriched in the brain but differ in their regional localizations within the brain.</description><subject>Affinity Labels</subject><subject>Analytical, structural and metabolic biochemistry</subject><subject>Animals</subject><subject>Binding and carrier proteins</subject><subject>Biological and medical sciences</subject><subject>brain</subject><subject>Brain - metabolism</subject><subject>Calcium - metabolism</subject><subject>Cations, Divalent</subject><subject>Chromatography, Affinity</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>inositol 1,3,4,5,-tetrakisphosphate</subject><subject>inositol 1,3,4,5-tetrakisphosphate-binding protein</subject><subject>inositol hexakisphosphate</subject><subject>inositol hexakisphosphate-binding protein</subject><subject>inositol phosphates</subject><subject>Inositol Phosphates - metabolism</subject><subject>isolation</subject><subject>Kinetics</subject><subject>localization</subject><subject>Male</subject><subject>photoaffinity labelling</subject><subject>Photochemistry</subject><subject>Proteins</subject><subject>Rats</subject><subject>Rats, Inbred Strains</subject><subject>receptors</subject><subject>Receptors, Cell Surface - metabolism</subject><subject>Receptors, Cytoplasmic and Nuclear</subject><subject>specificity</subject><subject>Substrate Specificity</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>eNqFkV9rFDEUxYNY6lr9CIUBRRR2NHcymUkepfgPCgoq-BZuMkknOjvZJlm0_Qj91Gb_sMUnAyEP53fP4eYQcg70NVDo3nyltIFaNly8BPmKUyZpLR6QBVDBasbhx0OyOCKPyOOUftJyWgmn5BQY8L7tF-TuyxhyQOf87PNNNaG2k5-vKpyHyowY0WQb_S1mH-YquMqnMGG2Q-XnkHwOUwVLtmyXvM42R_zl03oM5Ram3pkcudH--VfWfh62UesYsvVzekJOHE7JPj28Z-T7-3ffLj7Wl58_fLp4e1kbxltRD7J3tEHWCz0gNRI4YqeN7agui3IGtnWUGScMSGqlkEB7p7kWKB1DdOyMvNj7luDrjU1ZrXwydppwtmGTVN9IBh3w_4LQNeU7JSsg34MmhpSidWod_QrjjQKqtmWpXVlq24QCqXZlKVHmzg8BG72yw_3Uvp2iPz_omAxOLuJsfDpinFHZMVqwZ3ts9Ffjbx-t0j6Y0a5U0_XFTEnaA_sLoxGrCA</recordid><startdate>19920505</startdate><enddate>19920505</enddate><creator>THEIBERT, A. B</creator><creator>ESTEVEZ, V. A</creator><creator>MOUREY, R.J</creator><creator>MARECEK, J. F</creator><creator>BARROW, R. K</creator><creator>PRESTWICH, G. D</creator><creator>SNYDER, S. H</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>7TK</scope><scope>8FD</scope><scope>FR3</scope><scope>M7Z</scope><scope>P64</scope><scope>7X8</scope></search><sort><creationdate>19920505</creationdate><title>Photoaffinity labeling and characterization of isolated inositol 1,3,4,5-tetrakisphosphate- and inositol hexakisphosphate-binding proteins</title><author>THEIBERT, A. B ; ESTEVEZ, V. A ; MOUREY, R.J ; MARECEK, J. F ; BARROW, R. K ; PRESTWICH, G. D ; SNYDER, S. H</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c3548-d97f02a378bda0c915aa6bce60b258531e4f03cf8c190e989107fb5b8a9f3aaf3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1992</creationdate><topic>Affinity Labels</topic><topic>Analytical, structural and metabolic biochemistry</topic><topic>Animals</topic><topic>Binding and carrier proteins</topic><topic>Biological and medical sciences</topic><topic>brain</topic><topic>Brain - metabolism</topic><topic>Calcium - metabolism</topic><topic>Cations, Divalent</topic><topic>Chromatography, Affinity</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>inositol 1,3,4,5,-tetrakisphosphate</topic><topic>inositol 1,3,4,5-tetrakisphosphate-binding protein</topic><topic>inositol hexakisphosphate</topic><topic>inositol hexakisphosphate-binding protein</topic><topic>inositol phosphates</topic><topic>Inositol Phosphates - metabolism</topic><topic>isolation</topic><topic>Kinetics</topic><topic>localization</topic><topic>Male</topic><topic>photoaffinity labelling</topic><topic>Photochemistry</topic><topic>Proteins</topic><topic>Rats</topic><topic>Rats, Inbred Strains</topic><topic>receptors</topic><topic>Receptors, Cell Surface - metabolism</topic><topic>Receptors, Cytoplasmic and Nuclear</topic><topic>specificity</topic><topic>Substrate Specificity</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>THEIBERT, A. B</creatorcontrib><creatorcontrib>ESTEVEZ, V. A</creatorcontrib><creatorcontrib>MOUREY, R.J</creatorcontrib><creatorcontrib>MARECEK, J. F</creatorcontrib><creatorcontrib>BARROW, R. K</creatorcontrib><creatorcontrib>PRESTWICH, G. D</creatorcontrib><creatorcontrib>SNYDER, S. H</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>Neurosciences Abstracts</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>THEIBERT, A. B</au><au>ESTEVEZ, V. A</au><au>MOUREY, R.J</au><au>MARECEK, J. F</au><au>BARROW, R. K</au><au>PRESTWICH, G. D</au><au>SNYDER, S. H</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Photoaffinity labeling and characterization of isolated inositol 1,3,4,5-tetrakisphosphate- and inositol hexakisphosphate-binding proteins</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>1992-05-05</date><risdate>1992</risdate><volume>267</volume><issue>13</issue><spage>9071</spage><epage>9079</epage><pages>9071-9079</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><coden>JBCHA3</coden><abstract>We have isolated high affinity inositol (1,3,4,5)-tetrakisphosphate (IP4)- and inositol hexakisphosphate (IP6)-binding proteins
from detergent-solubilized rat brain membranes using a P1-tethered IP4 derivative linked to an Affi-Gel support. To determine
the identity, binding characteristics, and distribution of the individual IP4 recognition sites, we have synthesized an IP4
photoaffinity label probe, 125I-(D,L)-1-O-[N-(4-azidosalicyloxy)-3-aminopropyl-1-phospho]- IP4 (125I-ASA-IP4). Two apparently
distinct IP4-binding proteins (IP4BP), isolated with the IP4 affinity column, display high affinity and selectivity for IP4
over inositol trisphosphate (IP3), inositol pentakisphosphate (IP5), and IP6. The first IP4-binding protein (IP4BP1) which
has a KD for IP4 of 4 nM, is comprised of a protein at 182 kDa which is specifically photolabeled with high affinity by 125I-ASA-IP4.
The second, IP4BP2, has an affinity for IP4 of 1.5 nM and contains proteins at 84 and 174 kDa, both of which are specifically
photoaffinity labeled. A putative IP6-binding protein (IP6BP), also isolated with the IP4 affinity column, binds IP6 with
a KD of 14 nM and comprises three proteins of 115, 105, and 50 kDa. The 115- and 105-kDa subunits, but not the 50-kDa subunit,
specifically incorporate the photolabel. The IP4BP (182, 174, and 84 kDa) and IP6BP (115 and 105 kDa) proteins are specifically
photolabeled in the crude membrane, partially purified, and purified fractions. These receptor-binding proteins vary in inositol
phosphate specificity and in the effects of pH, Ca2+, and heparin on IP4 photoaffinity labeling. In addition, IP4BP and IP6BP
are enriched in the brain but differ in their regional localizations within the brain.</abstract><cop>Bethesda, MD</cop><pub>American Society for Biochemistry and Molecular Biology</pub><pmid>1315747</pmid><doi>10.1016/S0021-9258(19)50390-8</doi><tpages>9</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | The Journal of biological chemistry, 1992-05, Vol.267 (13), p.9071-9079 |
| issn | 0021-9258 1083-351X |
| language | eng |
| recordid | cdi_proquest_miscellaneous_72931615 |
| source | MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Alma/SFX Local Collection |
| subjects | Affinity Labels Analytical, structural and metabolic biochemistry Animals Binding and carrier proteins Biological and medical sciences brain Brain - metabolism Calcium - metabolism Cations, Divalent Chromatography, Affinity Fundamental and applied biological sciences. Psychology inositol 1,3,4,5,-tetrakisphosphate inositol 1,3,4,5-tetrakisphosphate-binding protein inositol hexakisphosphate inositol hexakisphosphate-binding protein inositol phosphates Inositol Phosphates - metabolism isolation Kinetics localization Male photoaffinity labelling Photochemistry Proteins Rats Rats, Inbred Strains receptors Receptors, Cell Surface - metabolism Receptors, Cytoplasmic and Nuclear specificity Substrate Specificity |
| title | Photoaffinity labeling and characterization of isolated inositol 1,3,4,5-tetrakisphosphate- and inositol hexakisphosphate-binding proteins |
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