| Cationization of protein antigens. IV. Increased antigen uptake by antigen-presenting cells. | |
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MedLine Citation:
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PMID: 3258879 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Cationization of BSA generates a molecule that mounts antibody responses of increased magnitude and duration and induces T cell proliferation at concentrations 500 times less than native BSA (nBSA). To explain the alteration in immunogenic properties of this Ag, the uptake of nBSA and cationized BSA (cBSA) by splenic APC has been investigated. T cell proliferation assays were conducted with nBSA and cBSA preparations with varying degrees of substitution. An inverse correlation between the degree of cationization and the amounts of Ag needed for optimal T cell reactivity was observed. To determine whether affinity for APC resulted in an increased uptake of cBSA, splenic APC were incubated with nBSA or cBSA for varying amounts of time. Comparisons were made at each time point between untreated Ag-pulsed APC (Ag uptake) and paraformaldehyde-fixed Ag-pulsed APC (processed Ag). Proliferation of T cells primed with nBSA or cBSA increased in proportion to the amount of time of APC exposure to high concentrations of nBSA, first appearing after a 2-h pulse and peaking at 8 h. Conversely, untreated APC needed only a 30-min cBSA exposure to induce either nBSA- or cBSA-primed T cell proliferation, indicating a rapid uptake of cBSA. Comparisons with proliferation induced by paraformaldehyde-fixed cBSA APC indicate that nBSA T cells recognize a lag phase-processed form of cBSA, whereas a majority of cBSA T cells recognize either a rapidly processed form of cBSA, or a membrane-processed cBSA molecule without a classical lag phase processing event. When monensin was used as an inhibitor of fluid phase pinocytosis in splenic APC, the presentation of nBSA was inhibited by 85%, but the presentation of cBSA was inhibited by only 20%. These results imply that nBSA enters the cell by fluid phase pinocytosis, whereas cBSA enters by a nonspecific adsorptive mechanism. The different modes of cellular entry for the two molecules, nBSA and cBSA, resulting in a rapid uptake of cBSA, may have important ramifications on T cell activation and immunoregulation. |
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Authors:
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R J Apple; P L Domen; A Muckerheide; J G Michael |
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Publication Detail:
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Type: Journal Article; Research Support, U.S. Gov't, P.H.S. |
Journal Detail:
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Title: Journal of immunology (Baltimore, Md. : 1950) Volume: 140 ISSN: 0022-1767 ISO Abbreviation: J. Immunol. Publication Date: 1988 May |
Date Detail:
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Created Date: 1988-06-09 Completed Date: 1988-06-09 Revised Date: 2007-11-14 |
Medline Journal Info:
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Nlm Unique ID: 2985117R Medline TA: J Immunol Country: UNITED STATES |
Other Details:
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Languages: eng Pagination: 3290-5 Citation Subset: AIM; IM |
Affiliation:
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Department of Microbiology and Molecular Genetics, University of Cincinnati College of Medicine, OH 45267. |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Animals Antigen-Presenting Cells / metabolism* Antigens / metabolism* Cations Dose-Response Relationship, Immunologic Kinetics Lymphocyte Activation Mice Monensin / pharmacology Pinocytosis / drug effects Protein Conformation Serum Albumin, Bovine / immunology*, metabolism Spleen / cytology T-Lymphocytes / immunology |
| Grant Support | |
ID/Acronym/Agency:
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A115520//PHS HHS |
| Chemical | |
Reg. No./Substance:
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0/Antigens; 0/Cations; 0/Serum Albumin, Bovine; 17090-79-8/Monensin |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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