Biomimetic liposomes hybrid with platelet membranes for targeted therapy of atherosclerosis

2020 ◽  
pp. 127296
Author(s):  
Yanan Song ◽  
Ning Zhang ◽  
Qiyu Li ◽  
Jing Chen ◽  
Qiaozi Wang ◽  
...  
Keyword(s):  
Targeted Therapy ◽  
Platelet Membranes

Lungenkarzinom: Genomisch stratefiziert behandeln: Wohin geht die Entwicklung?

2012 ◽  
Vol 03 (04) ◽  
pp. 184-185
Author(s):  
Christine Vetter
Keyword(s):  
Targeted Therapy

Die „Targeted Therapy” hat in den vergangenen Jahren in vielen Bereichen der Onkologie Fuß gefasst und gewinnt auch beim Lungenkarzinom zunehmend an Boden. Wie sich diese neue Therapierichtung künftig entwickeln kann, war eines der Themen beim diesjährigen Deutschen Krebskongress in Berlin.

The Uptake of Adenine by Isolated Human Platelet Membranes

1974 ◽  
Vol 32 (02/03) ◽  
pp. 457-464
Author(s):  
Paul C. French ◽  
Jan J. Sixma ◽  
Holm Holmsen
Keyword(s):  
Human Platelet ◽  
Facilitated Diffusion ◽  
Adenine Phosphoribosyltransferase ◽  
Ph Optimum ◽  
Intact Cells ◽  
Platelet Membranes ◽  
Group Translocation ◽  
Triton X

SummaryAdenine uptake into isolated platelet membranes had about the same Km (151 ± 21 • 9 nM) as uptake into intact cells (159 ± 21 nM) and was also competitively inhibited by papaverine and hypoxanthine. No uptake occurred at 0° and accumulated adenine was converted to AMP. AMP was not firmly bound to protein as judged by chromatography of triton X-100 solubilized membranes on Sephadex G25. The pH optimum for adenine uptake was at pH 5-5. Exogenous 5-phosphoribosyl-l-pyrophos- phate strongly stimulated uptake. These data may be explained by uptake of adenine by facilitated diffusion followed by conversion to AMP by adenine phosphoribosyltransferase but group translocation cannot be entirely excluded.

“Active Sites” on Platelet Membranes

1975 ◽  
Vol 34 (03) ◽  
pp. 859-860
Author(s):  
M. G Davey
Keyword(s):  
Active Sites ◽  
Platelet Membranes

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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