Secretion of HLA-A and -B antigens via an alternative RNA splicing pathway

Human class I major histocompatibility antigens (HLA-A, -B and -C) are integral membrane protein heterodimers, which are anchored in the membrane via a stretch of hydrophobic amino acids near the carboxyl terminus of the heavy chain. It has previously been shown that a mutagenized cell line secretes...

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Bibliographic Details
Published inThe Journal of experimental medicine Vol. 163; no. 5; pp. 1173 - 1190
Main Author KRANGEL, M. S
Format Journal Article
LanguageEnglish
Published New York, NY Rockefeller University Press 01.05.1986
The Rockefeller University Press
Subjects
Amino Acid Sequence
Animals
Antigens
Base Sequence
Biological and medical sciences
Cell Line
Fundamental and applied biological sciences. Psychology
Fundamental immunology
Gene Expression Regulation
Histocompatibility antigens (hla, h-2 and other systems)
HLA Antigens - genetics
Humans
Isoelectric Point
Liver Neoplasms, Experimental - metabolism
Lymphocytes - metabolism
Membrane Proteins - genetics
Membrane Proteins - metabolism
Molecular immunology
Molecular Weight
RNA Splicing
Solubility
Antigen
Human
HLA-System
Splicing
RNA
Nucleotide sequence
Transcription
Secretion
Major histocompatibility system
Mechanism
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Summary:Human class I major histocompatibility antigens (HLA-A, -B and -C) are integral membrane protein heterodimers, which are anchored in the membrane via a stretch of hydrophobic amino acids near the carboxyl terminus of the heavy chain. It has previously been shown that a mutagenized cell line secretes a water soluble form of the HLA-A2 antigen, due to a pattern of RNA splicing that removes exon 5 (encoding the transmembrane hydrophobic amino acids) from mature, HLA-A2--encoding transcripts. The present study was undertaken to assess whether a similar process might be operative in nonmutagenized cells. It is shown that water soluble class I molecules (primarily HLA-A24) are secreted by the T leukemic cell line HPB-ALL, and that alternative splicing removes exon 5 from a fraction of HLA-A24--encoding transcripts. It is further shown that class I molecules are secreted, possibly in an allele-specific fashion, from a variety of tumor cells and normal cells. The possible relationship between these findings and previous reports of HLA-A and -B antigens in human serum is discussed.
ISSN:0022-1007
1540-9538
DOI:10.1084/jem.163.5.1173