Literature DB >> 3878711

Association of specific tyrosine phosphorylation with stages of B-cell differentiation in human lymphoid leukemias.

H Kuratsune, K Owada, T Machii, Y Nishimori, E Ueda, Y Tokumine, S Tagawa, N Taniguchi, H Fujio, T Kitani.   

Abstract

In vitro protein phosphorylation in various types of human fresh lymphoid leukemic cells (C-ALL, B-CLL, HCL and PCL: B-cell lineage and T-ALL, ATL and T-CLL: T-cell lineage) were studied. In cases of B-CLL and HCL, tyrosine protein kinase (TPK) activity was at least 5-fold higher than that in other cases of B- and T-cell lineages. B-cell leukemic cells at various differentiation stages had different endogenous substrates in tyrosine phosphorylation as well as distinct TPK activity. The P-tyr-containing proteins of 68K, 59K and 56K were detected commonly in all the cases of B-cell lineage. The phosphorylated protein of 32K was present only in cases of PCL. On the other hand, in T-ALL and ATL, the major substrate in tyrosine phosphorylation was 58K. These results suggest that the characterization of in vitro tyrosine phosphorylation provides a new means not only to distinguish T- and B-lymphoid leukemia, but also to differentiate stages of lymphoid development.

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Year:  1985        PMID: 3878711     DOI: 10.1016/0006-291x(85)90947-7

Source DB:  PubMed          Journal:  Biochem Biophys Res Commun        ISSN: 0006-291X            Impact factor:   3.575


  1 in total

1.  Cell lines and peripheral blood leukocytes derived from individuals with chronic myelogenous leukemia display virtually identical proteins phosphorylated on tyrosine residues.

Authors:  R D Huhn; M R Posner; S I Rayter; J G Foulkes; A R Frackelton
Journal:  Proc Natl Acad Sci U S A       Date:  1987-07       Impact factor: 11.205

  1 in total

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