Faculty Opinions recommendation of Diphosphothreonine-specific interaction between an SQ/TQ cluster and an FHA domain in the Rad53-Dun1 kinase cascade.

2008 ◽  
Author(s):  
Stephen Jackson
Keyword(s):  
Specific Interaction ◽  
Fha Domain ◽  
Kinase Cascade

scholarly journals Diphosphothreonine-Specific Interaction between an SQ/TQ Cluster and an FHA Domain in the Rad53-Dun1 Kinase Cascade

2008 ◽  
Vol 30 (6) ◽  
pp. 767-778 ◽  
Author(s):  
Hyun Lee ◽  
Chunhua Yuan ◽  
Andrew Hammet ◽  
Anjali Mahajan ◽  
Eric S.-W. Chen ◽  
...  
Keyword(s):  
Specific Interaction ◽  
Fha Domain ◽  
Kinase Cascade

Heparin Counteracts the Antiaggregating Effect of Prostacyclin by Potentiating Platelet Aggregation

1983 ◽  
Vol 49 (02) ◽  
pp. 081-083 ◽  
Author(s):  
Vittorio Bertelé ◽  
Maria Carla Roncaglioni ◽  
Maria Benedetta Donati ◽  
Giovanni de Gaetano
Keyword(s):  
Platelet Aggregation ◽  
Human Platelet ◽  
Specific Interaction ◽  
Inhibitory Effect ◽  
Effective Inhibitor ◽  
Inhibitory Potency ◽  
Human Platelet Aggregation

SummaryIt has recently been reported that heparin neutralizes the inhibitory effect of prostacyclin (PGI2) on human platelet aggregation. The mechanism of this interaction has not yet been unequivocally established. We present here evidence that heparin (Liquemin Roche) does not react directly with PGI2 but counteracts its inhibitory effect by potentiating platelet aggregation. In the absence of heparin, PGI2 was a less effective inhibitor of platelet aggregation induced by the combination of ADP and serotonin than by ADP alone. Moreover, the inhibitory effect of PGI2 was similarly reduced when increasing the concentrations of ADP (in the absence of heparin). The lack of a specific interaction between heparin and PGI2 is supported by the observation that, in the presence of heparin, other prostaglandins such as PGD2 and PGE1, and a non-prostanoid compound such as adenosine also appeared to lose their inhibitory potency. It is concluded that heparin opposes platelet aggregation inhibitory effect of PGI2 by enhancement of platelet aggregation.

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