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CI Rivas, D Wisniewski, A Strife, A Perez, C Lambek, S Bruno, Z Darzynkiewicz and B Clarkson
Memorial Sloan-Kettering Cancer Center, Laboratory of Hematopoietic Cell
Kinetics, New York, NY 10021.
Previous studies by others using metabolic labeling, cell lysis, and
immunoprecipitation have reported elevated levels of p53 protein in blast
cells derived from patients with acute lymphoblastic leukemia (ALL) and
acute myeloblastic leukemia (AML), whereas p53 protein was not detected in
normal light-density bone marrow cells. In this report, using the same
detection methods, we confirm the negligible expression of p53 protein in
normal light density marrow cells. However, we find clearly significant
levels of p53 protein expression in enriched normal human marrow blast
populations. Furthermore, using a panel of p53 specific monoclonal
antibodies, we find the p53 protein constitutively synthesized by normal
marrow blasts has the immunologic phenotype identified by PAb240 that
reportedly recognizes a common conformational- dependent epitope on mutant
p53. We have also found that the p53 immunologic subclass identified by
PAb240 exists in normal human circulating lymphocytes either resting, serum
starved, or PHA activated. In summary, it is clear that (1) normal marrow
blast populations provide the appropriate control for assessing the levels
of p53 protein expression in leukemic blast cells; and (2) PAb240 cannot be
used to distinguish p53 mutated at the DNA level from normal p53 in fresh
human hematopoietic cells.
This article has been cited by other articles:
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| Copyright © 1992 by American Society of Hematology Online ISSN: 1528-0020 | |||||||||