scholarly journals A Phospholipid Substrate Molecule Residing in the Membrane Surface Mediates Opening of the Lid Region in Group IVA Cytosolic Phospholipase A2

2008 ◽  
Vol 283 (45) ◽  
pp. 31227-31236 ◽  
Author(s):  
John E. Burke ◽  
Yuan-Hao Hsu ◽  
Raymond A. Deems ◽  
Sheng Li ◽  
Virgil L. Woods ◽  
...  
Keyword(s):  
Phospholipase A2 ◽  
Membrane Surface ◽  
Cytosolic Phospholipase A2 ◽  
Substrate Molecule ◽  
Cytosolic Phospholipase ◽  
Group Iva

scholarly journals Binding Conformation of 2-Oxoamide Inhibitors to Group IVA Cytosolic Phospholipase A2 Determined by Molecular Docking Combined with Molecular Dynamics

2012 ◽  
Vol 52 (1) ◽  
pp. 243-254 ◽  
Author(s):  
Varnavas D. Mouchlis ◽  
Vasiliki Michopoulou ◽  
Violetta Constantinou-Kokotou ◽  
Thomas Mavromoustakos ◽  
Edward A. Dennis ◽  
...  
Keyword(s):  
Molecular Dynamics ◽  
Molecular Docking ◽  
Phospholipase A2 ◽  
Cytosolic Phospholipase A2 ◽  
Binding Conformation ◽  
Cytosolic Phospholipase ◽  
Group Iva

scholarly journals Group IVA cytosolic phospholipase A2 (cPLA2α) and integrin αIIbβ3 reinforce each other's functions during αIIbβ3 signaling in platelets

Blood ◽  
2009 ◽  
Vol 113 (2) ◽  
pp. 447-457 ◽  
Author(s):  
Nicolas Prévost ◽  
John V. Mitsios ◽  
Hisashi Kato ◽  
John E. Burke ◽  
Edward A. Dennis ◽  
...  
Keyword(s):  
Phospholipase A2 ◽  
Human Platelets ◽  
Cytosolic Phospholipase A2 ◽  
Binding Studies ◽  
Cytosolic Phospholipase ◽  
Fibrinogen Binding ◽  
Cytoplasmic Tails ◽  
Group Iva ◽  
Functional Consequences ◽  
Platelet Spreading

Abstract Group IVA cytosolic phospholipase A2 (cPLA2α) catalyzes release of arachidonic acid from glycerophospholipids, leading to thromboxane A2 (TxA2) production. Some platelet agonists stimulate cPLA2α, but others require fibrinogen binding to αIIbβ3 to elicit TxA2. Therefore, relationships between cPLA2α and αIIbβ3 were examined. cPLA2α and a cPLA2α binding partner, vimentin, coimmunoprecipitated with αIIbβ3 from platelets, independent of fibrinogen binding. Studies with purified proteins and with recombinant proteins expressed in CHO cells determined that the interaction between cPLA2α and αIIbβ3 was indirect and was dependent on the αIIb and β3 cytoplasmic tails. Fibrinogen binding to αIIbβ3 caused an increase in integrin-associated cPLA2α activity in normal platelets, but not in cPLA2α-deficient mouse platelets or in human platelets treated with pyrrophenone, a cPLA2α inhibitor. cPLA2α activation downstream of αIIbβ3 had functional consequences for platelets in that it was required for fibrinogen-dependent recruitment of activated protein kinase Cβ to the αIIbβ3 complex and for platelet spreading. Thus, cPLA2α and αIIbβ3 interact to reinforce each other's functions during αIIbβ3 signaling. This provides a plausible explanation for the role of αIIbβ3 in TxA2 formation and in the defective hemostatic function of mouse or human platelets deficient in cPLA2α.

scholarly journals Restoration of On-Time Embryo Implantation Corrects the Timing of Parturition in Cytosolic Phospholipase A2 Group IVA Deficient Mice1

2009 ◽  
Vol 81 (6) ◽  
pp. 1131-1138 ◽  
Author(s):  
Naoko Brown ◽  
Jason D. Morrow ◽  
James C. Slaughter ◽  
Bibhash C. Paria ◽  
Jeff Reese
Keyword(s):  
Phospholipase A2 ◽  
Embryo Implantation ◽  
Cytosolic Phospholipase A2 ◽  
Cytosolic Phospholipase ◽  
Group Iva

Cytosolic phospholipase A2 group IVA is overexpressed in patients with persistent asthma and regulated by the promoter microsatellites

2010 ◽  
Vol 125 (6) ◽  
pp. 1393-1395 ◽  
Author(s):  
Milena Sokolowska ◽  
Joanna Stefanska ◽  
Karolina Wodz-Naskiewicz ◽  
Malgorzata Cieslak ◽  
Rafal Pawliczak
Keyword(s):  
Phospholipase A2 ◽  
Persistent Asthma ◽  
Cytosolic Phospholipase A2 ◽  
Cytosolic Phospholipase ◽  
Group Iva
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