Abstract
The 45-kD autoantigen associated with juvenile rheumatoid arthritis (JRA) has been isolated from HeLa cell nuclei and purified about 2500-fold to near homogeneity in a five-step chromatographic procedure. Purification of the antigen was monitored by immunoblot assays using a nearly monospecific anti-45-kD serum from a child with JRA. Tryptic peptide mapping and partial amino acid sequencing of the purified 45-kD antigen demonstrated its identity with the DEK protein. DEK is a 43-kD protein of unknown function expressed by the putative oncogene dek located on chromosome 6. As a result of a (6;9) translocation offociated with a rare subtype of acute myeloid leukaemia a chimeric protein containing most of DEK amino acids at the N-terminus is found in leukaemic cells (von Linden et al., Mol Cell Biol. 1992; 12: 1687-97). The 43-kD DEK was detected by immunoblotting with serum from a patient with JRA in a variety of rat tissues, and was most abundant in the spleen and in bone marrow.
MeSH Terms
Amino Acid Sequence
Animals
Arthritis, Juvenile/immunology
Autoantigens/isolation & purification
Cells, Cultured
Child, Preschool
Chromatography, High Pressure Liquid
Chromatography, Ion Exchange
Chromosomal Proteins, Non-Histone
Electrophoresis, Polyacrylamide Gel
HeLa Cells
Humans
Leukemia, Myeloid/immunology
Molecular Sequence Data
Molecular Weight
Oncogene Proteins/isolation & purification
Peptide Mapping
Poly-ADP-Ribose Binding Proteins
Rats
Chemicals
Autoantigens
Chromosomal Proteins, Non-Histone
Dek protein, human
Oncogene Proteins
Poly-ADP-Ribose Binding Proteins
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Sierakowska H
Department of Biochemistry, New York University School of Medicine 10016.
Williams K R
Szer I S
Szer W
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