Recombinant human transferrin: Beyond iron binding and transport
Iron is indispensible for life and essential for such processes as oxygen transport, electron transfer and DNA synthesis. Transferrin (Tf) is a ubiquitous protein with a central role in iron transport and metabolism. There is evidence, however, that Tf has many other biological roles in addition to...
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| Veröffentlicht in: | Biotechnology advances 2011-03, Vol.29 (2), p.230-238 |
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| creator | Brandsma, Martin E. Jevnikar, Anthony M. Ma, Shengwu |
| description | Iron is indispensible for life and essential for such processes as oxygen transport, electron transfer and DNA synthesis. Transferrin (Tf) is a ubiquitous protein with a central role in iron transport and metabolism. There is evidence, however, that Tf has many other biological roles in addition to its primary function of facilitating iron transport and metabolism, such as its profound effect on mammalian cell growth and productivity. The multiple functions of Tf can be exploited to develop many novel applications. Indeed, over the past several years, considerable efforts have been directed towards exploring human serum Tf (hTf), especially the use of recombinant native hTf and recombinant Tf fusion proteins, for various applications within biotechnology and medicine. Here, we review some of the remarkable progress that has been made towards the application of hTf in these diverse areas and discuss some of the exciting future prospects for hTf. |
| doi_str_mv | 10.1016/j.biotechadv.2010.11.007 |
| format | Article |
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Transferrin (Tf) is a ubiquitous protein with a central role in iron transport and metabolism. There is evidence, however, that Tf has many other biological roles in addition to its primary function of facilitating iron transport and metabolism, such as its profound effect on mammalian cell growth and productivity. The multiple functions of Tf can be exploited to develop many novel applications. Indeed, over the past several years, considerable efforts have been directed towards exploring human serum Tf (hTf), especially the use of recombinant native hTf and recombinant Tf fusion proteins, for various applications within biotechnology and medicine. Here, we review some of the remarkable progress that has been made towards the application of hTf in these diverse areas and discuss some of the exciting future prospects for hTf.</description><identifier>ISSN: 0734-9750</identifier><identifier>EISSN: 1873-1899</identifier><identifier>DOI: 10.1016/j.biotechadv.2010.11.007</identifier><identifier>PMID: 21147210</identifier><identifier>CODEN: BIADDD</identifier><language>eng</language><publisher>Kidlington: Elsevier Inc</publisher><subject>application ; Biological and medical sciences ; Biological Transport ; Biotechnological and medical application ; Biotechnology ; Biotechnology - methods ; blood serum ; cell growth ; Disease management ; Drug Delivery Systems ; electron transfer ; Fundamental and applied biological sciences. Psychology ; Fusion protein technology ; Humans ; iron ; Iron - metabolism ; Iron-binding protein ; metabolism ; Multi-tasking protein ; Novel drug delivery and targeting system ; Novel therapy ; oxygen ; Protein Binding ; proteins ; Recombinant Fusion Proteins - biosynthesis ; Recombinant Fusion Proteins - pharmacology ; Recombinant Fusion Proteins - therapeutic use ; Recombinant production ; recombinant proteins ; Serum-free medium supplement ; transfer DNA ; Transferrin ; Transferrin - biosynthesis ; Transferrin - pharmacology ; Transferrin - therapeutic use ; transferrins ; transport</subject><ispartof>Biotechnology advances, 2011-03, Vol.29 (2), p.230-238</ispartof><rights>2010 Elsevier Inc.</rights><rights>2015 INIST-CNRS</rights><rights>Copyright © 2010 Elsevier Inc. All rights reserved.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c525t-9c9a8b3275ff66eba6e983c07f13fe2280de9ae252f6d0483896830213c024bb3</citedby><cites>FETCH-LOGICAL-c525t-9c9a8b3275ff66eba6e983c07f13fe2280de9ae252f6d0483896830213c024bb3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0734975010001643$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3537,27901,27902,65306</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=23901300$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/21147210$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Brandsma, Martin E.</creatorcontrib><creatorcontrib>Jevnikar, Anthony M.</creatorcontrib><creatorcontrib>Ma, Shengwu</creatorcontrib><title>Recombinant human transferrin: Beyond iron binding and transport</title><title>Biotechnology advances</title><addtitle>Biotechnol Adv</addtitle><description>Iron is indispensible for life and essential for such processes as oxygen transport, electron transfer and DNA synthesis. Transferrin (Tf) is a ubiquitous protein with a central role in iron transport and metabolism. There is evidence, however, that Tf has many other biological roles in addition to its primary function of facilitating iron transport and metabolism, such as its profound effect on mammalian cell growth and productivity. The multiple functions of Tf can be exploited to develop many novel applications. Indeed, over the past several years, considerable efforts have been directed towards exploring human serum Tf (hTf), especially the use of recombinant native hTf and recombinant Tf fusion proteins, for various applications within biotechnology and medicine. Here, we review some of the remarkable progress that has been made towards the application of hTf in these diverse areas and discuss some of the exciting future prospects for hTf.</description><subject>application</subject><subject>Biological and medical sciences</subject><subject>Biological Transport</subject><subject>Biotechnological and medical application</subject><subject>Biotechnology</subject><subject>Biotechnology - methods</subject><subject>blood serum</subject><subject>cell growth</subject><subject>Disease management</subject><subject>Drug Delivery Systems</subject><subject>electron transfer</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Fusion protein technology</subject><subject>Humans</subject><subject>iron</subject><subject>Iron - metabolism</subject><subject>Iron-binding protein</subject><subject>metabolism</subject><subject>Multi-tasking protein</subject><subject>Novel drug delivery and targeting system</subject><subject>Novel therapy</subject><subject>oxygen</subject><subject>Protein Binding</subject><subject>proteins</subject><subject>Recombinant Fusion Proteins - biosynthesis</subject><subject>Recombinant Fusion Proteins - pharmacology</subject><subject>Recombinant Fusion Proteins - therapeutic use</subject><subject>Recombinant production</subject><subject>recombinant proteins</subject><subject>Serum-free medium supplement</subject><subject>transfer DNA</subject><subject>Transferrin</subject><subject>Transferrin - biosynthesis</subject><subject>Transferrin - pharmacology</subject><subject>Transferrin - therapeutic use</subject><subject>transferrins</subject><subject>transport</subject><issn>0734-9750</issn><issn>1873-1899</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2011</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqF0U1vEzEQBmALgWga-AuwF8Rp0xl7P2xOtFWBSpWQgJ4tr3fcOsrawd5U6r_HIYEee7I0esYzeoexCmGFgN3ZejX4OJO9N-PDisO-jCuA_gVboOxFjVKpl2wBvWhq1bdwwk5zXgNgC614zU44YtNzhAX7_INsnAYfTJir-91kQjUnE7KjlHz4VF3QYwxj5VMMVVGjD3eVKYW_aBvT_Ia9cmaT6e3xXbLbL1e_Lr_VN9-_Xl-e39S25e1cK6uMHATvW-e6jgbTkZLCQu9QOOJcwkjKEG-560ZopJCqkwI4FsObYRBL9vHw7zbF3zvKs558trTZmEBxl7XsQEgUCp6XjWq4aoQqUh6kTTHnRE5vk59MetQIeh-0XuunoPU-aI2oS9Cl9d1xyG6YaPzf-C_ZAj4cgcnWbFzJy_r85MqmKGDv3h-cM1Gbu1TM7c8yqQMALkS515JdHASVeB88JZ2tp2Bp9InsrMfon9_3D7UiqO8</recordid><startdate>20110301</startdate><enddate>20110301</enddate><creator>Brandsma, Martin E.</creator><creator>Jevnikar, Anthony M.</creator><creator>Ma, Shengwu</creator><general>Elsevier Inc</general><general>Elsevier</general><scope>FBQ</scope><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>7X8</scope><scope>7QO</scope><scope>8FD</scope><scope>FR3</scope><scope>P64</scope></search><sort><creationdate>20110301</creationdate><title>Recombinant human transferrin: Beyond iron binding and transport</title><author>Brandsma, Martin E. ; Jevnikar, Anthony M. ; Ma, Shengwu</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c525t-9c9a8b3275ff66eba6e983c07f13fe2280de9ae252f6d0483896830213c024bb3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2011</creationdate><topic>application</topic><topic>Biological and medical sciences</topic><topic>Biological Transport</topic><topic>Biotechnological and medical application</topic><topic>Biotechnology</topic><topic>Biotechnology - methods</topic><topic>blood serum</topic><topic>cell growth</topic><topic>Disease management</topic><topic>Drug Delivery Systems</topic><topic>electron transfer</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Fusion protein technology</topic><topic>Humans</topic><topic>iron</topic><topic>Iron - metabolism</topic><topic>Iron-binding protein</topic><topic>metabolism</topic><topic>Multi-tasking protein</topic><topic>Novel drug delivery and targeting system</topic><topic>Novel therapy</topic><topic>oxygen</topic><topic>Protein Binding</topic><topic>proteins</topic><topic>Recombinant Fusion Proteins - biosynthesis</topic><topic>Recombinant Fusion Proteins - pharmacology</topic><topic>Recombinant Fusion Proteins - therapeutic use</topic><topic>Recombinant production</topic><topic>recombinant proteins</topic><topic>Serum-free medium supplement</topic><topic>transfer DNA</topic><topic>Transferrin</topic><topic>Transferrin - biosynthesis</topic><topic>Transferrin - pharmacology</topic><topic>Transferrin - therapeutic use</topic><topic>transferrins</topic><topic>transport</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Brandsma, Martin E.</creatorcontrib><creatorcontrib>Jevnikar, Anthony M.</creatorcontrib><creatorcontrib>Ma, Shengwu</creatorcontrib><collection>AGRIS</collection><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>MEDLINE - Academic</collection><collection>Biotechnology Research Abstracts</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><jtitle>Biotechnology advances</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Brandsma, Martin E.</au><au>Jevnikar, Anthony M.</au><au>Ma, Shengwu</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Recombinant human transferrin: Beyond iron binding and transport</atitle><jtitle>Biotechnology advances</jtitle><addtitle>Biotechnol Adv</addtitle><date>2011-03-01</date><risdate>2011</risdate><volume>29</volume><issue>2</issue><spage>230</spage><epage>238</epage><pages>230-238</pages><issn>0734-9750</issn><eissn>1873-1899</eissn><coden>BIADDD</coden><abstract>Iron is indispensible for life and essential for such processes as oxygen transport, electron transfer and DNA synthesis. Transferrin (Tf) is a ubiquitous protein with a central role in iron transport and metabolism. There is evidence, however, that Tf has many other biological roles in addition to its primary function of facilitating iron transport and metabolism, such as its profound effect on mammalian cell growth and productivity. The multiple functions of Tf can be exploited to develop many novel applications. Indeed, over the past several years, considerable efforts have been directed towards exploring human serum Tf (hTf), especially the use of recombinant native hTf and recombinant Tf fusion proteins, for various applications within biotechnology and medicine. Here, we review some of the remarkable progress that has been made towards the application of hTf in these diverse areas and discuss some of the exciting future prospects for hTf.</abstract><cop>Kidlington</cop><pub>Elsevier Inc</pub><pmid>21147210</pmid><doi>10.1016/j.biotechadv.2010.11.007</doi><tpages>9</tpages></addata></record> |
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| ispartof | Biotechnology advances, 2011-03, Vol.29 (2), p.230-238 |
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| subjects | application Biological and medical sciences Biological Transport Biotechnological and medical application Biotechnology Biotechnology - methods blood serum cell growth Disease management Drug Delivery Systems electron transfer Fundamental and applied biological sciences. Psychology Fusion protein technology Humans iron Iron - metabolism Iron-binding protein metabolism Multi-tasking protein Novel drug delivery and targeting system Novel therapy oxygen Protein Binding proteins Recombinant Fusion Proteins - biosynthesis Recombinant Fusion Proteins - pharmacology Recombinant Fusion Proteins - therapeutic use Recombinant production recombinant proteins Serum-free medium supplement transfer DNA Transferrin Transferrin - biosynthesis Transferrin - pharmacology Transferrin - therapeutic use transferrins transport |
| title | Recombinant human transferrin: Beyond iron binding and transport |
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