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Research Article Free access | 10.1172/JCI114413

Identification of two related markers for common acute lymphoblastic leukemia as heat shock proteins.

J R Strahler, R Kuick, C Eckerskorn, F Lottspeich, B C Richardson, D A Fox, L M Stoolman, C A Hanson, D Nichols, and H J Tueche

Department of Pediatrics, University of Michigan Medical School, Ann Arbor 48109.

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Department of Pediatrics, University of Michigan Medical School, Ann Arbor 48109.

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Department of Pediatrics, University of Michigan Medical School, Ann Arbor 48109.

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Department of Pediatrics, University of Michigan Medical School, Ann Arbor 48109.

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Department of Pediatrics, University of Michigan Medical School, Ann Arbor 48109.

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Department of Pediatrics, University of Michigan Medical School, Ann Arbor 48109.

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Department of Pediatrics, University of Michigan Medical School, Ann Arbor 48109.

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Department of Pediatrics, University of Michigan Medical School, Ann Arbor 48109.

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Published January 1, 1990 - More info

Published in Volume 85, Issue 1 on January 1, 1990
J Clin Invest. 1990;85(1):200–207. https://doi.org/10.1172/JCI114413.
© 1990 The American Society for Clinical Investigation
Published January 1, 1990 - Version history
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Abstract

By direct analysis of the polypeptide constituents of leukemic cells, we have previously detected several polypeptides that are restricted in their expression to acute lymphoblastic leukemia (ALL). In this study, we provide evidence that two polypeptides designated L2 and L4 are structurally related and represent novel markers for common ALL. Partial amino acid sequence analysis did not uncover differences between L2 and L4. The sequences obtained correspond to a previously cloned human gene designated hsp 27 that is expressed, following heat shock treatment, in a variety of cells. 32Pi incorporation studies indicate that L4 is an unphosphorylated form and L2 is a phosphorylated form of hsp27. The two forms were inducible by heat shock in leukemic and nonleukemic lymphoid cells. Thus, in acute leukemia, the common ALL subtype is uniquely characterized by the constitutive expression of a polypeptide that represents a major cellular phosphoprotein.

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