Abstract
Abstract Murine T cell hybridomas were used to examine the requirements for processing and presentation of human fibrinogen. In contrast to most protein Ag, fibrinogen (Mr 340,000) did not need to be processed by an APC, inasmuch as intact fibrinogen was presented by both pre-fixed and chloroquine-treated macrophages. Through the use of a variety of protease inhibitors, no involvement of proteases either on the macrophage surface or in the culture medium in the presentation of fibrinogen was observed. The epitope recognized by two T cell hybridomas was localized to the peptide, A alpha (551-578), which was located on the carboxy portion of the A alpha-chain. This portion of the A alpha-chain has no defined secondary structure and must possess the conformational flexibility which allows it to directly associate with an I-Ek molecule. Thus conformational flexibility may be a major factor in determining the processing requirements of a protein Ag.
Dates
Type | When |
---|---|
Created | 2 years, 8 months ago (Dec. 31, 2022, 12:36 a.m.) |
Deposited | 5 months ago (March 29, 2025, 11:24 p.m.) |
Indexed | 1 month, 2 weeks ago (July 14, 2025, 11:23 p.m.) |
Issued | 37 years, 7 months ago (Feb. 1, 1988) |
Published | 37 years, 7 months ago (Feb. 1, 1988) |
Published Online | 37 years, 6 months ago (Feb. 15, 1988) |
Published Print | 37 years, 6 months ago (Feb. 15, 1988) |
@article{Lee_1988, title={T cell recognition of fibrinogen. A determinant on the A alpha-chain does not require processing.}, volume={140}, ISSN={1550-6606}, url={http://dx.doi.org/10.4049/jimmunol.140.4.1063}, DOI={10.4049/jimmunol.140.4.1063}, number={4}, journal={The Journal of Immunology}, publisher={Oxford University Press (OUP)}, author={Lee, P and Matsueda, G R and Allen, P M}, year={1988}, month=feb, pages={1063–1068} }