Electroconvulsive Treatment Induces a Rapid and Transient Increase in Tyrosine Phosphorylatin of a 40-Kilodalton Protein Associated with Microtubule-Associated Protein 2 Kinase Activity

1991 ◽  
Vol 56 (1) ◽  
pp. 147-152 ◽  
Author(s):  
Kathleen R. Stratton ◽  
Paul F. Worley ◽  
Julie S. Litz ◽  
Sarah J. Parsons ◽  
Richard L. Huganir ◽  
...  
Keyword(s):  
Kinase Activity ◽  
Transient Increase ◽  
Electroconvulsive Treatment

Transient Increase of a Protein Kinase Activity Identified to CK2 during Sea Urchin Development

1999 ◽  
Vol 266 (2) ◽  
pp. 425-431 ◽  
Author(s):  
Christelle Delalande ◽  
Robert Bellé ◽  
Patrick Cormier ◽  
Odile Mulner-Lorillon
Keyword(s):  
Protein Kinase ◽  
Sea Urchin ◽  
Kinase Activity ◽  
Transient Increase ◽  
Protein Kinase Activity

Ineffective Thrombopoiesis

1990 ◽  
Vol 48 (3) ◽  
pp. 266-267
Author(s):  
JM Radley ◽  
SL Ellis
Keyword(s):  
Microscopic Examination ◽  
Phosphate Buffer ◽  
Primary Myelofibrosis ◽  
Transient Increase ◽  
Major Difficulty ◽  
Adult Mice ◽  
Dense Cytoplasm

In effective thrombopoies is has been inferred to occur in several disease sates from considerations of megakaryocyte mass and platelet kinetics. Microscopic examination has demonstrated increased numbers of megakaryocytes, with a typical forms particularly pronounced, in primary myelofibrosis. It has not been documented if megakaryocyte ever fail to reach maturity in non-pathological situations. A major difficulty of establishing this is that the number of megakaryocytes normally present in the marrow is extremely low. A large transient increase in megakaryocytopoiesis can how ever be induced in mice by an injection of 5-fluorouracil. We have utilised this treatment and report here evidence for in effective thrombopoies is in healthy mice.Adult mice were perfused (2% glutaraldehyde in 0.08M phosphate buffer, pH 7.4) 8 days following an injection of 5-fluorouracil (150mg/kg). Femurs were subsequently decalcified in 10% neutral E.D.T.A. and embedded in Spurrs resin. Transverse sections of marrow revealed many megakaryocytes at various stages of maturity. Occasional megakaryocytes (less than 1%) were found to be under going degeneration prior to achieving full maturation and releasing cytoplasm as platelets. These cells were characterized by a peripheral rim of dense cytoplasm which enveloped a mass of organelles and vacuoles (Fig. 1). Numerous microtubules were foundaround and with in the organelle-rich zone (Fig 2).

Successful Electroconvulsive Treatment of a Schizophrenic Patient Suffering from Severe Haemophilia A

1996 ◽  
Vol 75 (06) ◽  
pp. 978-978 ◽  
Author(s):  
Theodora Glaub ◽  
Bela Telek ◽  
Zoltan Boda ◽  
Sandor Szabo ◽  
Geza Krall ◽  
...  
Keyword(s):  
Schizophrenic Patient ◽  
Haemophilia A ◽  
Severe Haemophilia ◽  
Electroconvulsive Treatment

Effect of Thrombin on Phosphorylation of Platelet Membrane Proteins

1976 ◽  
Vol 35 (03) ◽  
pp. 635-642 ◽  
Author(s):  
M Steiner
Keyword(s):  
Protein Kinase ◽  
Kinase Activity ◽  
Qualitative Change ◽  
Protein Kinase Activity ◽  
Protein Substrates ◽  
Phosphoprotein Phosphatase ◽  
Progressive Loss ◽  
Platelet Membranes ◽  
Endogenous Protein ◽  
Considerable Loss

SummaryThe effect of thrombin on the phosphorylating activity of platelet membranes was compared to that of trypsin. Preincubation of non-32P phosphorylated platelet membranes with or without either of these two enzymes resulted in a considerable loss of membrane protein kinase activity which was most severe when trypsin was used. Protein kinase activity and endogenous protein acceptors decreased in parallel. 32P-phosphorylated membranes showed a slow but progressive loss of label which was accelerated by trypsin. Thrombin under these conditions prevented the loss of 32P-phosphate. These results are interpreted to indicate a thrombin-induced destruction of a phosphoprotein phosphatase. The protein kinase activity of phosphorylated platelet membranes using endogenous or exogenous protein substrates showed a significant reduction compared to non-phosphorylated membranes suggesting a deactivation of protein kinase by phosphorylation of platelet membranes. Neither thrombin nor trypsin caused a qualitative change in the membrane polypeptides accepting 32P-phosphate but resulted in quantitative alterations of their ability to become phosphorylated.

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