Protein phosphokinase activities of resting and proliferating human lymphocytes. Changes upon phytohemagglutinin stimulation and in acute lymphoblastic leukemic cells
Transformation of normal human peripheral lymphocytes by phytohemagglutinin (PHA) to blast-like cells is accompanied by an enhancement of the protein phosphokinase activity. This activity becomes maximal approx. 70 h after exposure to the mitogen and amounts to a 3- to 4-fold stimulation in the 10 0...
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todo:paper_00144827_v101_n2_p260_Horenstein2023-10-03T14:12:35Z Protein phosphokinase activities of resting and proliferating human lymphocytes. Changes upon phytohemagglutinin stimulation and in acute lymphoblastic leukemic cells Horenstein, A. Piras, M.M. Mordoh, J. Piras, R. enzyme phosphotransferase phytohemagglutinin radioisotope acute lymphocytic leukemia adenosine triphosphate p 32 human in vitro study lymphocyte lymphocyte proliferation normal human protein phosphokinase theoretical study thymidine h 3 Caseins Cyclic AMP Human Lectins Leukemia, Lymphocytic Lymphocyte Activation Lymphocytes Phosphates Protamine Kinase Protein Kinases Transformation of normal human peripheral lymphocytes by phytohemagglutinin (PHA) to blast-like cells is accompanied by an enhancement of the protein phosphokinase activity. This activity becomes maximal approx. 70 h after exposure to the mitogen and amounts to a 3- to 4-fold stimulation in the 10 000 g supernatant and 8- to 10-fold in the nuclear fraction. This augmented activity is due to the increased level of some of the multiple forms of lymphocyte protein kinase, specially the one which is active on exogenous casein and elutes from DEAE-cellulose at 125 mM phosphate (casein-kinase S-C3 and N-C2). Acute lymphoblastic leukemic cells have a protein kinase pattern upon chromatography on DEAE-cellulose which is similar, but not identical, to that of PHA-stimulated lymphocytes. The most remarkable difference is the presence in the 10 000 g supernatant of leukemic cells of a protein kinase form which was either absent or barely detectable in resting or PHA-treated normal lymphocytes. This protein kinase is active on casein and is not stimulated by cAMP. The results obtained are discussed in connection both with the known enhanced protein phosphorylation in PHA-stimulated cells and with the protein kinase changes observed in other cellular systems. © 1976. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_00144827_v101_n2_p260_Horenstein |
| institution |
Universidad de Buenos Aires |
| institution_str |
I-28 |
| repository_str |
R-134 |
| collection |
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
| topic |
enzyme phosphotransferase phytohemagglutinin radioisotope acute lymphocytic leukemia adenosine triphosphate p 32 human in vitro study lymphocyte lymphocyte proliferation normal human protein phosphokinase theoretical study thymidine h 3 Caseins Cyclic AMP Human Lectins Leukemia, Lymphocytic Lymphocyte Activation Lymphocytes Phosphates Protamine Kinase Protein Kinases |
| spellingShingle |
enzyme phosphotransferase phytohemagglutinin radioisotope acute lymphocytic leukemia adenosine triphosphate p 32 human in vitro study lymphocyte lymphocyte proliferation normal human protein phosphokinase theoretical study thymidine h 3 Caseins Cyclic AMP Human Lectins Leukemia, Lymphocytic Lymphocyte Activation Lymphocytes Phosphates Protamine Kinase Protein Kinases Horenstein, A. Piras, M.M. Mordoh, J. Piras, R. Protein phosphokinase activities of resting and proliferating human lymphocytes. Changes upon phytohemagglutinin stimulation and in acute lymphoblastic leukemic cells |
| topic_facet |
enzyme phosphotransferase phytohemagglutinin radioisotope acute lymphocytic leukemia adenosine triphosphate p 32 human in vitro study lymphocyte lymphocyte proliferation normal human protein phosphokinase theoretical study thymidine h 3 Caseins Cyclic AMP Human Lectins Leukemia, Lymphocytic Lymphocyte Activation Lymphocytes Phosphates Protamine Kinase Protein Kinases |
| description |
Transformation of normal human peripheral lymphocytes by phytohemagglutinin (PHA) to blast-like cells is accompanied by an enhancement of the protein phosphokinase activity. This activity becomes maximal approx. 70 h after exposure to the mitogen and amounts to a 3- to 4-fold stimulation in the 10 000 g supernatant and 8- to 10-fold in the nuclear fraction. This augmented activity is due to the increased level of some of the multiple forms of lymphocyte protein kinase, specially the one which is active on exogenous casein and elutes from DEAE-cellulose at 125 mM phosphate (casein-kinase S-C3 and N-C2). Acute lymphoblastic leukemic cells have a protein kinase pattern upon chromatography on DEAE-cellulose which is similar, but not identical, to that of PHA-stimulated lymphocytes. The most remarkable difference is the presence in the 10 000 g supernatant of leukemic cells of a protein kinase form which was either absent or barely detectable in resting or PHA-treated normal lymphocytes. This protein kinase is active on casein and is not stimulated by cAMP. The results obtained are discussed in connection both with the known enhanced protein phosphorylation in PHA-stimulated cells and with the protein kinase changes observed in other cellular systems. © 1976. |
| format |
JOUR |
| author |
Horenstein, A. Piras, M.M. Mordoh, J. Piras, R. |
| author_facet |
Horenstein, A. Piras, M.M. Mordoh, J. Piras, R. |
| author_sort |
Horenstein, A. |
| title |
Protein phosphokinase activities of resting and proliferating human lymphocytes. Changes upon phytohemagglutinin stimulation and in acute lymphoblastic leukemic cells |
| title_short |
Protein phosphokinase activities of resting and proliferating human lymphocytes. Changes upon phytohemagglutinin stimulation and in acute lymphoblastic leukemic cells |
| title_full |
Protein phosphokinase activities of resting and proliferating human lymphocytes. Changes upon phytohemagglutinin stimulation and in acute lymphoblastic leukemic cells |
| title_fullStr |
Protein phosphokinase activities of resting and proliferating human lymphocytes. Changes upon phytohemagglutinin stimulation and in acute lymphoblastic leukemic cells |
| title_full_unstemmed |
Protein phosphokinase activities of resting and proliferating human lymphocytes. Changes upon phytohemagglutinin stimulation and in acute lymphoblastic leukemic cells |
| title_sort |
protein phosphokinase activities of resting and proliferating human lymphocytes. changes upon phytohemagglutinin stimulation and in acute lymphoblastic leukemic cells |
| url |
http://hdl.handle.net/20.500.12110/paper_00144827_v101_n2_p260_Horenstein |
| work_keys_str_mv |
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