Source:http://linkedlifedata.com/resource/pubmed/id/12297282
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1-3
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pubmed:dateCreated |
2002-9-25
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pubmed:abstractText |
Interleukin-21 (IL-21) has recently been identified as a novel 4-helix-bundle type I cytokine possessing a cytokine receptor gamma chain essential for the immune response. We report the preparation and functional characterization of Escherichia coli-expressed recombinant human IL-21 (rIL-21). The rIL-21, expressed as insoluble inclusion bodies in E. coli, was solubilized and then refolded by using a modified dialysis method. The introduction of redox reagents during refolding led to a dramatic increase in the refolding efficiency. Circular dichroism spectrum analysis showed that the refolded rIL-21 had an alpha-helix as a secondary structure, which is a characteristic of type I cytokines. Flow cytometry confirmed previous reports that rIL-21 binds to CD3-activated T cells (T-LAK) and to cell lines Raji, HL60, and Jurkat. rIL-21 stimulated the proliferation of T-LAK but not peripheral blood mononuclear cells, and this effect seems to be identical to that of co-stimulation with anti-CD3 antibody. Growth inhibition assay indicated that enhancement of the cytotoxicity of T-LAK to the human bile duct carcinoma TFK-1 depended on the concentration of rIL-21. Thus, refolded rIL-21 had activity identical to that of authentic IL-21 and enhanced the anti-tumor activity of T-LAK. These conclusions suggest the potential use of the refolded cytokine in adoptive immunotherapy using T-LAK cells and in the discovery of other functions of the cytokine.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antineoplastic Agents,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Recombinant,
http://linkedlifedata.com/resource/pubmed/chemical/Interleukins,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/interleukin-21
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
0014-5793
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
25
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pubmed:volume |
528
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
70-6
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:12297282-Antineoplastic Agents,
pubmed-meshheading:12297282-Base Sequence,
pubmed-meshheading:12297282-Cytotoxicity, Immunologic,
pubmed-meshheading:12297282-DNA, Recombinant,
pubmed-meshheading:12297282-Escherichia coli,
pubmed-meshheading:12297282-Humans,
pubmed-meshheading:12297282-Immunotherapy, Adoptive,
pubmed-meshheading:12297282-Inclusion Bodies,
pubmed-meshheading:12297282-Interleukins,
pubmed-meshheading:12297282-Killer Cells, Lymphokine-Activated,
pubmed-meshheading:12297282-Molecular Sequence Data,
pubmed-meshheading:12297282-Neoplasms,
pubmed-meshheading:12297282-Protein Engineering,
pubmed-meshheading:12297282-Protein Folding,
pubmed-meshheading:12297282-Recombinant Proteins,
pubmed-meshheading:12297282-T-Lymphocyte Subsets,
pubmed-meshheading:12297282-Tumor Cells, Cultured
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pubmed:year |
2002
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pubmed:articleTitle |
Antitumor activity of interleukin-21 prepared by novel refolding procedure from inclusion bodies expressed in Escherichia coli.
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pubmed:affiliation |
Cell Resource Center for Biomedical Research, Institute of Development, Aging, and Cancer, Tohoku University, 4-1 Seiryomachi, Aoba-ku, Sendai 980-8575, Japan.
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pubmed:publicationType |
Journal Article,
In Vitro,
Research Support, Non-U.S. Gov't
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