Can uranium follow the iron-acquisition pathway? Interaction of uranyl-loaded transferrin with receptor 1
Transferrin receptor 1 (R D ) binds iron-loaded transferrin and allows its internalization in the cytoplasm. Human serum transferrin also forms complexes with metals other than iron, including uranium in the uranyl form (UO 2 2+ ). Can the uranyl-saturated transferrin (TUr 2 ) follow the receptor-me...
Gespeichert in:
| Veröffentlicht in: | Journal of biological inorganic chemistry 2010-05, Vol.15 (4), p.497-504 |
|---|---|
| Hauptverfasser: | , , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 504 |
|---|---|
| container_issue | 4 |
| container_start_page | 497 |
| container_title | Journal of biological inorganic chemistry |
| container_volume | 15 |
| creator | Hémadi, Miryana Ha-Duong, Ngûyet-Thanh Plantevin, Sophie Vidaud, Claude El Hage Chahine, Jean-Michel |
| description | Transferrin receptor 1 (R
D
) binds iron-loaded transferrin and allows its internalization in the cytoplasm. Human serum transferrin also forms complexes with metals other than iron, including uranium in the uranyl form (UO
2
2+
). Can the uranyl-saturated transferrin (TUr
2
) follow the receptor-mediated iron-acquisition pathway? In cell-free assays, TUr
2
interacts with R
D
in two different steps. The first is fast, direct rate constant,
k
1
= (5.2 ± 0.8) × 10
6
M
−1
s
−1
; reverse rate constant,
k
−1
= 95 ± 5 s
−1
; and dissociation constant
K
1
= 18 ± 6 μM. The second occurs in the 100-s range and leads to an increase in the stability of the protein–protein adduct, with an average overall dissociation constant
K
d
= 6 ± 2 μM. This kinetic analysis implies in the proposed in vitro model possible but weak competition between TUr
2
and the C-lobe of iron-loaded transferrin toward the interaction with
R
D
. |
| doi_str_mv | 10.1007/s00775-009-0618-1 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_733564796</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>733564796</sourcerecordid><originalsourceid>FETCH-LOGICAL-c343t-1dbd968ac24603409d83e3f9af04a83d5e9a45caf999cbf80d50ee5bfa59ac9e3</originalsourceid><addsrcrecordid>eNp9kE9vFDEMxSMEokvhA3BBuXEKOJNkZnJCaMWfSpW4wDnyZhw21WyyTTJa7bdn2i0cudiy_d6T_GPsrYQPEmD4WNcyGAFgBfRyFPIZ20itOiFVNzxnG7DairEzwxV7VesdACgjzUt21QFo2Q3dhsUtJr4UTHE58JDnOZ942xOPJSeB_n6JNbaYEz9i25_w_InfpEYF_eMyh0fveRZzxokm3tapBiolJn6Kbc8LeTq2XLh8zV4EnCu9eerX7NfXLz-338Xtj28328-3wiutmpDTbrL9iL7TPSgNdhoVqWAxgMZRTYYsauMxWGv9LowwGSAyu4DGorekrtn7S-6x5PuFanOHWD3NMybKS3WDUqbXg-1Xpbwofcm1FgruWOIBy9lJcA-A3QWwWwG7B8BOrp53T-nL7kDTP8dfoquguwjqekq_qbi7vJS0fvyf1D_C1ohw</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>733564796</pqid></control><display><type>article</type><title>Can uranium follow the iron-acquisition pathway? Interaction of uranyl-loaded transferrin with receptor 1</title><source>MEDLINE</source><source>SpringerLink Journals - AutoHoldings</source><creator>Hémadi, Miryana ; Ha-Duong, Ngûyet-Thanh ; Plantevin, Sophie ; Vidaud, Claude ; El Hage Chahine, Jean-Michel</creator><creatorcontrib>Hémadi, Miryana ; Ha-Duong, Ngûyet-Thanh ; Plantevin, Sophie ; Vidaud, Claude ; El Hage Chahine, Jean-Michel</creatorcontrib><description>Transferrin receptor 1 (R
D
) binds iron-loaded transferrin and allows its internalization in the cytoplasm. Human serum transferrin also forms complexes with metals other than iron, including uranium in the uranyl form (UO
2
2+
). Can the uranyl-saturated transferrin (TUr
2
) follow the receptor-mediated iron-acquisition pathway? In cell-free assays, TUr
2
interacts with R
D
in two different steps. The first is fast, direct rate constant,
k
1
= (5.2 ± 0.8) × 10
6
M
−1
s
−1
; reverse rate constant,
k
−1
= 95 ± 5 s
−1
; and dissociation constant
K
1
= 18 ± 6 μM. The second occurs in the 100-s range and leads to an increase in the stability of the protein–protein adduct, with an average overall dissociation constant
K
d
= 6 ± 2 μM. This kinetic analysis implies in the proposed in vitro model possible but weak competition between TUr
2
and the C-lobe of iron-loaded transferrin toward the interaction with
R
D
.</description><identifier>ISSN: 0949-8257</identifier><identifier>EISSN: 1432-1327</identifier><identifier>DOI: 10.1007/s00775-009-0618-1</identifier><identifier>PMID: 20041272</identifier><language>eng</language><publisher>Berlin/Heidelberg: Springer-Verlag</publisher><subject>Antigens, CD - metabolism ; Biochemistry ; Biomedical and Life Sciences ; Humans ; Iron - metabolism ; Kinetics ; Life Sciences ; Microbiology ; Original Paper ; Protein Binding ; Receptors, Transferrin - metabolism ; Spectrometry, Fluorescence ; Thermodynamics ; Transferrin - metabolism ; Uranium - metabolism ; Uranium Compounds - metabolism</subject><ispartof>Journal of biological inorganic chemistry, 2010-05, Vol.15 (4), p.497-504</ispartof><rights>SBIC 2009</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c343t-1dbd968ac24603409d83e3f9af04a83d5e9a45caf999cbf80d50ee5bfa59ac9e3</citedby><cites>FETCH-LOGICAL-c343t-1dbd968ac24603409d83e3f9af04a83d5e9a45caf999cbf80d50ee5bfa59ac9e3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1007/s00775-009-0618-1$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1007/s00775-009-0618-1$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,776,780,27903,27904,41467,42536,51297</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/20041272$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Hémadi, Miryana</creatorcontrib><creatorcontrib>Ha-Duong, Ngûyet-Thanh</creatorcontrib><creatorcontrib>Plantevin, Sophie</creatorcontrib><creatorcontrib>Vidaud, Claude</creatorcontrib><creatorcontrib>El Hage Chahine, Jean-Michel</creatorcontrib><title>Can uranium follow the iron-acquisition pathway? Interaction of uranyl-loaded transferrin with receptor 1</title><title>Journal of biological inorganic chemistry</title><addtitle>J Biol Inorg Chem</addtitle><addtitle>J Biol Inorg Chem</addtitle><description>Transferrin receptor 1 (R
D
) binds iron-loaded transferrin and allows its internalization in the cytoplasm. Human serum transferrin also forms complexes with metals other than iron, including uranium in the uranyl form (UO
2
2+
). Can the uranyl-saturated transferrin (TUr
2
) follow the receptor-mediated iron-acquisition pathway? In cell-free assays, TUr
2
interacts with R
D
in two different steps. The first is fast, direct rate constant,
k
1
= (5.2 ± 0.8) × 10
6
M
−1
s
−1
; reverse rate constant,
k
−1
= 95 ± 5 s
−1
; and dissociation constant
K
1
= 18 ± 6 μM. The second occurs in the 100-s range and leads to an increase in the stability of the protein–protein adduct, with an average overall dissociation constant
K
d
= 6 ± 2 μM. This kinetic analysis implies in the proposed in vitro model possible but weak competition between TUr
2
and the C-lobe of iron-loaded transferrin toward the interaction with
R
D
.</description><subject>Antigens, CD - metabolism</subject><subject>Biochemistry</subject><subject>Biomedical and Life Sciences</subject><subject>Humans</subject><subject>Iron - metabolism</subject><subject>Kinetics</subject><subject>Life Sciences</subject><subject>Microbiology</subject><subject>Original Paper</subject><subject>Protein Binding</subject><subject>Receptors, Transferrin - metabolism</subject><subject>Spectrometry, Fluorescence</subject><subject>Thermodynamics</subject><subject>Transferrin - metabolism</subject><subject>Uranium - metabolism</subject><subject>Uranium Compounds - metabolism</subject><issn>0949-8257</issn><issn>1432-1327</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2010</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kE9vFDEMxSMEokvhA3BBuXEKOJNkZnJCaMWfSpW4wDnyZhw21WyyTTJa7bdn2i0cudiy_d6T_GPsrYQPEmD4WNcyGAFgBfRyFPIZ20itOiFVNzxnG7DairEzwxV7VesdACgjzUt21QFo2Q3dhsUtJr4UTHE58JDnOZ942xOPJSeB_n6JNbaYEz9i25_w_InfpEYF_eMyh0fveRZzxokm3tapBiolJn6Kbc8LeTq2XLh8zV4EnCu9eerX7NfXLz-338Xtj28328-3wiutmpDTbrL9iL7TPSgNdhoVqWAxgMZRTYYsauMxWGv9LowwGSAyu4DGorekrtn7S-6x5PuFanOHWD3NMybKS3WDUqbXg-1Xpbwofcm1FgruWOIBy9lJcA-A3QWwWwG7B8BOrp53T-nL7kDTP8dfoquguwjqekq_qbi7vJS0fvyf1D_C1ohw</recordid><startdate>20100501</startdate><enddate>20100501</enddate><creator>Hémadi, Miryana</creator><creator>Ha-Duong, Ngûyet-Thanh</creator><creator>Plantevin, Sophie</creator><creator>Vidaud, Claude</creator><creator>El Hage Chahine, Jean-Michel</creator><general>Springer-Verlag</general><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>7X8</scope></search><sort><creationdate>20100501</creationdate><title>Can uranium follow the iron-acquisition pathway? Interaction of uranyl-loaded transferrin with receptor 1</title><author>Hémadi, Miryana ; Ha-Duong, Ngûyet-Thanh ; Plantevin, Sophie ; Vidaud, Claude ; El Hage Chahine, Jean-Michel</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c343t-1dbd968ac24603409d83e3f9af04a83d5e9a45caf999cbf80d50ee5bfa59ac9e3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2010</creationdate><topic>Antigens, CD - metabolism</topic><topic>Biochemistry</topic><topic>Biomedical and Life Sciences</topic><topic>Humans</topic><topic>Iron - metabolism</topic><topic>Kinetics</topic><topic>Life Sciences</topic><topic>Microbiology</topic><topic>Original Paper</topic><topic>Protein Binding</topic><topic>Receptors, Transferrin - metabolism</topic><topic>Spectrometry, Fluorescence</topic><topic>Thermodynamics</topic><topic>Transferrin - metabolism</topic><topic>Uranium - metabolism</topic><topic>Uranium Compounds - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Hémadi, Miryana</creatorcontrib><creatorcontrib>Ha-Duong, Ngûyet-Thanh</creatorcontrib><creatorcontrib>Plantevin, Sophie</creatorcontrib><creatorcontrib>Vidaud, Claude</creatorcontrib><creatorcontrib>El Hage Chahine, Jean-Michel</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Journal of biological inorganic chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Hémadi, Miryana</au><au>Ha-Duong, Ngûyet-Thanh</au><au>Plantevin, Sophie</au><au>Vidaud, Claude</au><au>El Hage Chahine, Jean-Michel</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Can uranium follow the iron-acquisition pathway? Interaction of uranyl-loaded transferrin with receptor 1</atitle><jtitle>Journal of biological inorganic chemistry</jtitle><stitle>J Biol Inorg Chem</stitle><addtitle>J Biol Inorg Chem</addtitle><date>2010-05-01</date><risdate>2010</risdate><volume>15</volume><issue>4</issue><spage>497</spage><epage>504</epage><pages>497-504</pages><issn>0949-8257</issn><eissn>1432-1327</eissn><abstract>Transferrin receptor 1 (R
D
) binds iron-loaded transferrin and allows its internalization in the cytoplasm. Human serum transferrin also forms complexes with metals other than iron, including uranium in the uranyl form (UO
2
2+
). Can the uranyl-saturated transferrin (TUr
2
) follow the receptor-mediated iron-acquisition pathway? In cell-free assays, TUr
2
interacts with R
D
in two different steps. The first is fast, direct rate constant,
k
1
= (5.2 ± 0.8) × 10
6
M
−1
s
−1
; reverse rate constant,
k
−1
= 95 ± 5 s
−1
; and dissociation constant
K
1
= 18 ± 6 μM. The second occurs in the 100-s range and leads to an increase in the stability of the protein–protein adduct, with an average overall dissociation constant
K
d
= 6 ± 2 μM. This kinetic analysis implies in the proposed in vitro model possible but weak competition between TUr
2
and the C-lobe of iron-loaded transferrin toward the interaction with
R
D
.</abstract><cop>Berlin/Heidelberg</cop><pub>Springer-Verlag</pub><pmid>20041272</pmid><doi>10.1007/s00775-009-0618-1</doi><tpages>8</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0949-8257 |
| ispartof | Journal of biological inorganic chemistry, 2010-05, Vol.15 (4), p.497-504 |
| issn | 0949-8257 1432-1327 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_733564796 |
| source | MEDLINE; SpringerLink Journals - AutoHoldings |
| subjects | Antigens, CD - metabolism Biochemistry Biomedical and Life Sciences Humans Iron - metabolism Kinetics Life Sciences Microbiology Original Paper Protein Binding Receptors, Transferrin - metabolism Spectrometry, Fluorescence Thermodynamics Transferrin - metabolism Uranium - metabolism Uranium Compounds - metabolism |
| title | Can uranium follow the iron-acquisition pathway? Interaction of uranyl-loaded transferrin with receptor 1 |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-28T05%3A36%3A15IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Can%20uranium%20follow%20the%20iron-acquisition%20pathway?%20Interaction%20of%20uranyl-loaded%20transferrin%20with%20receptor%201&rft.jtitle=Journal%20of%20biological%20inorganic%20chemistry&rft.au=H%C3%A9madi,%20Miryana&rft.date=2010-05-01&rft.volume=15&rft.issue=4&rft.spage=497&rft.epage=504&rft.pages=497-504&rft.issn=0949-8257&rft.eissn=1432-1327&rft_id=info:doi/10.1007/s00775-009-0618-1&rft_dat=%3Cproquest_cross%3E733564796%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=733564796&rft_id=info:pmid/20041272&rfr_iscdi=true |