Tissue-specific self-peptides bound by major histocompatibility complex class I molecules of a human pancreatic beta-cell line. NLM AIDSLINE Important note: Information in this article was accurate in 1997. The state of the art may have changed since the publication date.

Click here to return to AIDSLINE main menu
DonateNow
Print this Article


Tissue-specific self-peptides bound by major histocompatibility complex class I molecules of a human pancreatic beta-cell line.

Diabetes. 1996 Dec;45(12):1761-5. Unique Identifier : AIDSLINE MED/97081081
Papadopoulos KP; Colovai AI; Maffei A; Jaraquemada D; Suciu-Foca N; Harris PE; Department of Medicine, College of Physicians and Surgeons,; Columbia University, New York, New York 10032, USA.

Abstract: The process of beta-cell destruction in IDDM is mediated, in part, by CD8+ T-cells. Structural characterization of HLA-I-bound self-peptides presented by the human beta-cell line HP-62 was performed to identify possible tissue-specific autoantigens in the context of CD8+ T-cell/HLA-I interactions. The sequences of the beta-cell line HLA-I-bound peptides were compared with sequence databases. Six of the obtained sequences showed homology to known precursor proteins, three of which--GLUT2 receptor, phosphatidylinositol-glycan-specific phospholipase D, and 5-hydroxytryptamine-1F receptor--have a limited, tissue-specific expression. These HLA-bound self-peptides may be part of a pool of autoantigens recognized by beta-cell reactive cytotoxic T-cells.
Keywords: Amino Acid Sequence Autoantigens/*IMMUNOLOGY Cell Line CD8-Positive T-Lymphocytes/IMMUNOLOGY Histocompatibility Antigens Class I/*METABOLISM Human Islets of Langerhans/*IMMUNOLOGY Monosaccharide Transport Proteins/CHEMISTRY/IMMUNOLOGY Peptide Fragments/CHEMISTRY/IMMUNOLOGY Peptides/CHEMISTRY/*IMMUNOLOGY Phospholipase D/CHEMISTRY/IMMUNOLOGY Protein Precursors/IMMUNOLOGY Receptors, Serotonin/CHEMISTRY/IMMUNOLOGY Support, Non-U.S. Gov't JOURNAL ARTICLEKWDaminoacidsequenceautoantigens/KWDimmunologycelllinecd8-positivet-lymphocytes/immunologyhistocompatibilityantigensclassi/KWDmetabolismhumanisletsoflangerhans/KWDimmunologymonosaccharidetransportproteins/chemistry/immunologypeptidefragments/chemistry/immunologypeptides/chemistry/KWDimmunologyphospholipased/chemistry/immunologyproteinprecursors/immunologyreceptors,serotonin/chemistry/immunologysupport,non-uKWDsKWDgov'tjournalarticle
970228
M9721889

Copyright © 1997 - National Library of Medicine. Reproduced under license with the National Library of Medicine, Bethesda, MD.

AEGiS is a 501(c)3, not-for-profit, tax-exempt, educational corporation. AEGiS is made possible through unrestricted funding from Boehringer Ingelheim, Bridgestone/Firestone Charitable Trust, Bristol-Myers Squibb Company, Elton John AIDS Foundation, Gill Foundation, the National Library of Medicine, Quest Diagnostics, Roche and Trimeris, and donations from users like you. Always watch for outdated information. This article first appeared in 1997. This material is designed to support, not replace, the relationship that exists between you and your doctor.

AEGiS presents published material, reprinted with permission and neither endorses nor opposes any material. All information contained on this website, including information relating to health conditions, products, and treatments, is for informational purposes only. It is often presented in summary or aggregate form. It is not meant to be a substitute for the advice provided by your own physician or other medical professionals. Always discuss treatment options with a doctor who specializes in treating HIV.

Copyright ©1980, 1997. AEGiS. All materials appearing on AEGiS are protected by copyright as a collective work or compilation under U.S. copyright and other laws and are the property of AEGiS, or the party credited as the provider of the content. .