Antigen expression and cell surface properties of human leukemic blasts

J. P. Cotropia, J. U. Gutterman, Evan M Hersh

Research output: Contribution to journalArticle

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Abstract

Cell surface proteins of human leukemic blasts were studied by direct immunofluorescence (DIF), low pH elution and immunodiffusion (ID). Among AML blasts from 19 patients, the average proportions of blasts positive for IgG, IgM, and IgA were 62%, 5%, and 6%, respectively. In contrast, blasts from three CML patients in blast crisis and 12 ALL patients had surface IgG, IgM, and IgA values of 8%, 4% and 1% respectively, for the former group and 1.1%, 0.8% and 0.6%, respectively, for the latter group. Blasts from 15 leukemic cell preparations were eluted at pH 2.4 for 30 minutes at 4°C in glycine HCl buffer. Immunodiffusion with appropriate specific antisera demonstrated intact IgG in 3 of 11 AML eluates. Eight of 11 AML eluates, 1 of 2 CML eluates, and 1 of 2 ALL eluates contained intact IgG and Fab fragment, but no Fc fragment. The remaining CML eluate contained Fab fragment only. One ALL eluate contained no IgG or fragments by double diffusion. An eluate from a pool of normal human leukocytes from 20 normal donors contained intact IgG and Fc fragment, but no Fab fragment. All leukemic cell eluates also contained the antiproteases alpha 1 antitrypsin and alpha 1 antichymotrypsin which were demonstrated to have been proteolytically modified. Three of 15 leukemic cell eluates contained the antiprotease alpha 2 macroglubulin. The normal leukocyte eluate contained alpha 1 antitrypsin but no alpha 1 antichymotrypsin or alpha 2 macroglobulin. The presence of Fab fragment in AML, CML blast crisis, and ALL eluates suggests IgG binding by Fab as antibody, whereas Fc fragment in normal leukocyte eluate suggests binding via Fc to the Fc receptor. The expression of cell associated proteolytic enzymes, as revealed by the presence of protease modified antiproteases, may explain cell surface IgG degradation. A consequence of surface proteolytic activity would be the degradation of IgG antibody to yield Fab fragment bound to membrane antigenic determinants. The Fab reaction product is incapable of interacting with either complement or Fc receptors. Therefore, such proteolytic activity may protect the leukemic blasts from lysis by complement dependent or antibody dependent cell mediated cytotoxic mechanisms (81 references).

Original languageEnglish (US)
Pages (from-to)146-164
Number of pages19
JournalAnnals of the New York Academy of Sciences
VolumeVol. 276
StatePublished - 1976
Externally publishedYes

Fingerprint

Surface Properties
Surface properties
Immunoglobulin G
Immunoglobulin Fab Fragments
Antigens
Emitter coupled logic circuits
Immunoglobulin Fc Fragments
Protease Inhibitors
alpha 1-Antichymotrypsin
Blast Crisis
alpha 1-Antitrypsin
Leukocytes
Fc Receptors
Immunodiffusion
Immunoglobulin A
Immunoglobulin M
Antibodies
Peptide Hydrolases
alpha-Macroglobulins
Cells

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)

Cite this

Antigen expression and cell surface properties of human leukemic blasts. / Cotropia, J. P.; Gutterman, J. U.; Hersh, Evan M.

In: Annals of the New York Academy of Sciences, Vol. Vol. 276, 1976, p. 146-164.

Research output: Contribution to journalArticle

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N2 - Cell surface proteins of human leukemic blasts were studied by direct immunofluorescence (DIF), low pH elution and immunodiffusion (ID). Among AML blasts from 19 patients, the average proportions of blasts positive for IgG, IgM, and IgA were 62%, 5%, and 6%, respectively. In contrast, blasts from three CML patients in blast crisis and 12 ALL patients had surface IgG, IgM, and IgA values of 8%, 4% and 1% respectively, for the former group and 1.1%, 0.8% and 0.6%, respectively, for the latter group. Blasts from 15 leukemic cell preparations were eluted at pH 2.4 for 30 minutes at 4°C in glycine HCl buffer. Immunodiffusion with appropriate specific antisera demonstrated intact IgG in 3 of 11 AML eluates. Eight of 11 AML eluates, 1 of 2 CML eluates, and 1 of 2 ALL eluates contained intact IgG and Fab fragment, but no Fc fragment. The remaining CML eluate contained Fab fragment only. One ALL eluate contained no IgG or fragments by double diffusion. An eluate from a pool of normal human leukocytes from 20 normal donors contained intact IgG and Fc fragment, but no Fab fragment. All leukemic cell eluates also contained the antiproteases alpha 1 antitrypsin and alpha 1 antichymotrypsin which were demonstrated to have been proteolytically modified. Three of 15 leukemic cell eluates contained the antiprotease alpha 2 macroglubulin. The normal leukocyte eluate contained alpha 1 antitrypsin but no alpha 1 antichymotrypsin or alpha 2 macroglobulin. The presence of Fab fragment in AML, CML blast crisis, and ALL eluates suggests IgG binding by Fab as antibody, whereas Fc fragment in normal leukocyte eluate suggests binding via Fc to the Fc receptor. The expression of cell associated proteolytic enzymes, as revealed by the presence of protease modified antiproteases, may explain cell surface IgG degradation. A consequence of surface proteolytic activity would be the degradation of IgG antibody to yield Fab fragment bound to membrane antigenic determinants. The Fab reaction product is incapable of interacting with either complement or Fc receptors. Therefore, such proteolytic activity may protect the leukemic blasts from lysis by complement dependent or antibody dependent cell mediated cytotoxic mechanisms (81 references).

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