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polycythemia vera/phosphatase

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Using the cytochemical method after Barka and Anderson, activity and localization of lysosomal acid phosphatase (AP) was determined in peripheral-blood lymphocytes from 20 healthy subjects, 10 patients with Hodgkin's disease (HD), 10 patients with plasma cell myeloma (PCM), and 10 patients with

Defective expression of the SHP-1 phosphatase in polycythemia vera.

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The SHP-1 phosphatase associates with the receptors for erythropoietin, stem cell factor, and interleukin-3, and negatively regulates the mitogenic signals generated during engagement by their respective ligands. The erythroid progenitors of patients with polycythemia vera are hypersensitive to the
To determine whether decreased alkaline phosphatase activity in the granules from neutrophils of patients with chronic myelogenous leukemia (CML) was due to an absence of enzyme or the production of defective enzyme, we compared the immunologic properties of granule alkaline phosphatase derived from

Granulocyte alkaline phosphatase. Studies of purified enzymes from normal subjects and patients with polycythemia vera.

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To characterize the biological changes which result in increased granulocyte alkaline p-nitrophenyl phosphatase activity in patients with polycythemia vera, the enzyme was purified from granule fractions of sucrose homogenates made from dextran-sedimented leukocytes of normal subjects and patients
Erythropoietin (EP) and stem cell factor (SCF) are essential growth factors for erythroid progenitor cell proliferation and differentiation in serum-free culture. It has been previously shown that burst-forming units-erythroid and colony-forming units-erythroid from patients with polycythemia vera

Identification of increased protein tyrosine phosphatase activity in polycythemia vera erythroid progenitor cells.

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Polycythemia vera (PV) is a clonal hematologic disease characterized by hyperplasia of the three major bone marrow lineages. PV erythroid progenitor cells display hypersensitivity to several growth factors, which might be caused by an abnormality of tyrosine phosphorylation. In the present study, we

Role of tyrosine kinases and phosphatases in polycythemia vera.

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Protein tyrosine kinases (PTKs) and phosphatases (PTPs) play a crucial role in normal cell development, and dysfunction of these enzymes has been implicated in human cancers. Polycythemia vera (PV) is a clonal hematologic disease characterized by hypersensitivity of hematopoietic progenitor cells to

The gene encoding hematopoietic cell phosphatase (SHP-1) is structurally and transcriptionally intact in polycythemia vera.

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Polycythemia vera (PV) is an acquired clonal disorder characterized by increased production of mature red cells and growth of erythroid colonies in the absence of erythropoietin. Mutation of the erythropoietin receptor has been demonstrated to cause familial polycythemia, but no mutations have been

Polycythemia vera terminating with myeloblastic leukemia; correlation of morphologic findings with leukocytic phosphatase studies.

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[Alkaline phosphatase activity in neutrophils in polycythemia vera and in secondary erythrocytosis].

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[Alkaline phosphatase activity of the granulocytes in polycythemia vera and myelofibrosis].

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Electrophoretic heterogeneity of leucocyte alkaline phosphatase in normal man and in patients with polycythemia vera.

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Leucocyte alkaline-phosphatase activity in polycythaemia rubra vera.

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Electrophoretic patterns of human leukocyte alkaline phosphatase in polycythemia vera.

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[GRANULOCYTE ALKALINE PHOSPHATASE IN POLYCYTHEMIA VERA].

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