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Molecular cloning of two isoforms of the murine homolog of the myeloid CD33
antigen
EZ Tchilian, PC Beverley, BD Young and SM Watt
Imperial Cancer Research Fund, University College London Medical School,
UK.
CD33 monoclonal antibodies recognize a 67-kD glycoprotein of unknown
function that is expressed by early myeloid progenitors and their leukemic
counterparts. We report here the cloning of the murine homolog of the human
CD33 antigen. Two cDNA clones, differing by an 83- nucleotide insertion in
the cytoplasmic region, were isolated. The insertion generated a shift in
the reading frame within the cytoplasmic tail, resulting in two mouse CD33
isoforms, m33-A and m33-B, with distinct cytoplasmic domains and with
predicted protein core molecular weights of 37 kD and 45 kD, respectively.
The cDNAs and deduced amino acid sequences show extensive similarity with
the human CD33 sequence with the highest homology occurring in the first
and second lg-like domains (61% amino acid identity). The most significant
divergence between the human and murine proteins occurs in their
cytoplasmic portions. The murine CD33 mRNAs were detected in bone marrow,
spleen, thymus, brain, liver, the multipotential progenitor cell line, A4,
the myelomonocytic cell line, WEHI3B, the myeloid cell line, M1, and the
macrophage cell line, P388, by Northern blot analysis. The expression
pattern of the murine CD33 homolog suggests that the function of CD33
antigen in hematopoiesis may be conserved between humans and mice.
Volume 83,
Issue 11,
pp. 3188-3198,
06/01/1994
Copyright © 1994 by The American Society of Hematology
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