GSBS Student Publications

Title

Hyperexpressed hairy leukemic cell Ii might bind to the antigen-presenting site of class II MHC molecules

UMMS Affiliation

Graduate School of Biomedical Sciences; Department of Pharmacology; Department of Pediatrics; Department of Cell Biology

Date

April 1987

Document Type

Article

Medical Subject Headings

*Antigens, Differentiation, B-Lymphocyte; Cell Line, Transformed; Cell Transformation, Viral; Herpesvirus 4, Human; *Histocompatibility Antigens Class II; Humans; Leukemia, Hairy Cell; Membrane Proteins; Molecular Weight; Sialoglycoproteins; Tumor Cells, Cultured

Disciplines

Life Sciences | Medicine and Health Sciences

Abstract

The p35 protein which is hyperexpressed on hairy leukemic cells was determined to be Ii, the electrophoretically invariant glycoprotein that is associated with class II major histocompatibility complex (Ia) antigens from the time of their synthesis. The principal function of class II MHC antigens is to present to T cell receptors those digested foreign antigenic peptides that probably fold as amphipathic alpha-helices and adsorb to a hydrophobic surface (desetope) on Ia. By a novel strip-of-helix hydrophobicity algorithm we found that the sequence Leu-142 to His-170 in Ii formed a five-cycle, amphipathic, alpha-helix, the highest scoring one among a series of proteins commonly used as experimental antigens. This finding led to the hypothesis that this sequence in Ii bound to the antigen-binding site (desetope) of Ia until release and self-aggregation in the endosome in order that digested foreign peptides could then bind to Ia. Abundant expression of Ii in leukemic cells might be associated with an altered capacity of those cells to present foreign or leukemic antigens to the host's immune system.

Rights and Permissions

Citation: Leukemia. 1987 Apr;1(4):395-6.

Related Resources

Link to article in PubMed

Journal Title

Leukemia : official journal of the Leukemia Society of America, Leukemia Research Fund, U.K

PubMed ID

2823017

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