Naturally processed heterodimeric disulfide-linked insulin peptides bind to major histocompatibility class II molecules on thymic epithelial cells
(1994) In Proceedings of the National Academy of Sciences of the United States of America 91(9). p.3936-3940- Abstract
We determined whether disulfide-linked insulin peptides that are immunogenic in vitro for CD4+ T cells bind to major histocompatibility complex class II in vivo. Radiolabeled recombinant human insulin (rHI) was injected into BALB/c mice, and processed rHI peptides bound to I-A(d) molecules on different thymic antigen-presenting cells were characterized. The A6-A11/B7-B19 and A19-A21/B14-B21 disulfide-linked I-A(d)-bound rHI peptides were isolated from thymic epithelial cells but not dendritic cells. While both thymic epithelial cells and dendritic cells present rHI to HI/I- A(d)-specific T cells, these antigen-presenting cells do not present the reduced or nonreduced forms of the disulfide-linked rHI peptides. Thus, a... (More)
We determined whether disulfide-linked insulin peptides that are immunogenic in vitro for CD4+ T cells bind to major histocompatibility complex class II in vivo. Radiolabeled recombinant human insulin (rHI) was injected into BALB/c mice, and processed rHI peptides bound to I-A(d) molecules on different thymic antigen-presenting cells were characterized. The A6-A11/B7-B19 and A19-A21/B14-B21 disulfide-linked I-A(d)-bound rHI peptides were isolated from thymic epithelial cells but not dendritic cells. While both thymic epithelial cells and dendritic cells present rHI to HI/I- A(d)-specific T cells, these antigen-presenting cells do not present the reduced or nonreduced forms of the disulfide-linked rHI peptides. Thus, a naturally processed disulfide-linked peptide can bind to major histocompatibility complex class II in vivo. The potential role of these peptides in immunological tolerance is discussed.
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- author
- Forquet, Frederique ; Hadzija, Mirko ; Semple, John W. LU ; Speck, Edwin and Delovitch, Terry L.
- publishing date
- 1994-04-26
- type
- Contribution to journal
- publication status
- published
- keywords
- thymic antigen-presenting cells
- in
- Proceedings of the National Academy of Sciences of the United States of America
- volume
- 91
- issue
- 9
- pages
- 5 pages
- publisher
- National Academy of Sciences
- external identifiers
-
- scopus:0028227017
- pmid:8171015
- ISSN
- 0027-8424
- DOI
- 10.1073/pnas.91.9.3936
- language
- English
- LU publication?
- no
- id
- 7b6d95cd-7aad-483b-a5d1-6e7796f48b4f
- date added to LUP
- 2019-12-03 10:33:30
- date last changed
- 2025-01-10 03:49:18
@article{7b6d95cd-7aad-483b-a5d1-6e7796f48b4f,
abstract = {{<p>We determined whether disulfide-linked insulin peptides that are immunogenic in vitro for CD4<sup>+</sup> T cells bind to major histocompatibility complex class II in vivo. Radiolabeled recombinant human insulin (rHI) was injected into BALB/c mice, and processed rHI peptides bound to I-A(d) molecules on different thymic antigen-presenting cells were characterized. The A6-A11/B7-B19 and A19-A21/B14-B21 disulfide-linked I-A(d)-bound rHI peptides were isolated from thymic epithelial cells but not dendritic cells. While both thymic epithelial cells and dendritic cells present rHI to HI/I- A(d)-specific T cells, these antigen-presenting cells do not present the reduced or nonreduced forms of the disulfide-linked rHI peptides. Thus, a naturally processed disulfide-linked peptide can bind to major histocompatibility complex class II in vivo. The potential role of these peptides in immunological tolerance is discussed.</p>}},
author = {{Forquet, Frederique and Hadzija, Mirko and Semple, John W. and Speck, Edwin and Delovitch, Terry L.}},
issn = {{0027-8424}},
keywords = {{thymic antigen-presenting cells}},
language = {{eng}},
month = {{04}},
number = {{9}},
pages = {{3936--3940}},
publisher = {{National Academy of Sciences}},
series = {{Proceedings of the National Academy of Sciences of the United States of America}},
title = {{Naturally processed heterodimeric disulfide-linked insulin peptides bind to major histocompatibility class II molecules on thymic epithelial cells}},
url = {{http://dx.doi.org/10.1073/pnas.91.9.3936}},
doi = {{10.1073/pnas.91.9.3936}},
volume = {{91}},
year = {{1994}},
}