scholarly journals Phosphatidylserine externalization, “necroptotic bodies” release, and phagocytosis during necroptosis

PLoS Biology ◽  
2017 ◽  
Vol 15 (6) ◽  
pp. e2002711 ◽  
Author(s):  
Sefi Zargarian ◽  
Inbar Shlomovitz ◽  
Ziv Erlich ◽  
Aria Hourizadeh ◽  
Yifat Ofir-Birin ◽  
...  
Keyword(s):  
Phosphatidylserine Externalization

C. elegans mitochondrial factor WAH-1 promotes phosphatidylserine externalization in apoptotic cells through phospholipid scramblase SCRM-1

2007 ◽  
Vol 9 (5) ◽  
pp. 541-549 ◽  
Author(s):  
Xiaochen Wang ◽  
Jin Wang ◽  
Keiko Gengyo-Ando ◽  
Lichuan Gu ◽  
Chun-Ling Sun ◽  
...  
Keyword(s):  
Apoptotic Cells ◽  
C Elegans ◽  
Phospholipid Scramblase ◽  
Phosphatidylserine Externalization

scholarly journals Stabilin Receptors: Role as Phosphatidylserine Receptors

Biomolecules ◽  
2019 ◽  
Vol 9 (8) ◽  
pp. 387 ◽  
Author(s):  
Seung-Yoon Park ◽  
In-San Kim
Keyword(s):  
Plasma Membrane ◽  
Cell Fusion ◽  
Apoptotic Cell ◽  
Lymphocyte Activation ◽  
Membrane Receptors ◽  
Phosphatidylserine Externalization ◽  
Outer Leaflet ◽  
Physiological Processes ◽  
Apoptotic Cell Clearance ◽  
Cell Clearance

Phosphatidylserine is a membrane phospholipid that is localized to the inner leaflet of the plasma membrane. Phosphatidylserine externalization to the outer leaflet of the plasma membrane is an important signal for various physiological processes, including apoptosis, platelet activation, cell fusion, lymphocyte activation, and regenerative axonal fusion. Stabilin-1 and stabilin-2 are membrane receptors that recognize phosphatidylserine on the cell surface. Here, we discuss the functions of Stabilin-1 and stabilin-2 as phosphatidylserine receptors in apoptotic cell clearance (efferocytosis) and cell fusion, and their ligand-recognition and signaling pathways.

Nanopore Formation and Phosphatidylserine Externalization in a Phospholipid Bilayer at High Transmembrane Potential

2006 ◽  
Vol 128 (19) ◽  
pp. 6288-6289 ◽  
Author(s):  
P. Thomas Vernier ◽  
Matthew J. Ziegler ◽  
Yinghua Sun ◽  
Wenji V. Chang ◽  
Martin A. Gundersen ◽  
...  
Keyword(s):  
Transmembrane Potential ◽  
Phospholipid Bilayer ◽  
Phosphatidylserine Externalization

scholarly journals Acid Sphingomyelinase Inhibition Prevents Hemolysis During Erythrocyte Storage

2016 ◽  
Vol 39 (1) ◽  
pp. 331-340 ◽  
Author(s):  
Richard S. Hoehn ◽  
Peter L. Jernigan ◽  
Alex L. Chang ◽  
Michael J. Edwards ◽  
Charles C. Caldwell ◽  
...  
Keyword(s):  
Flow Cytometry ◽  
Band 3 ◽  
Acid Sphingomyelinase ◽  
Erythrocyte Membranes ◽  
Dependent Manner ◽  
Band 3 Protein ◽  
Free Hemoglobin ◽  
Phosphatidylserine Externalization ◽  
Human Red Blood Cells ◽  
Dose Dependent

Background/Aims: During storage, units of human red blood cells (pRBCs) experience membrane destabilization and hemolysis which may cause harm to transfusion recipients. This study investigates whether inhibition of acid sphingomyelinase could stabilize erythrocyte membranes and prevent hemolysis during storage. Methods: Human and murine pRBCs were stored under standard blood banking conditions with and without the addition of amitriptyline, a known acid sphingomyelinase inhibitor. Hemoglobin was measured with an electronic hematology analyzer and flow cytometry was used to measure erythrocyte size, complexity, phosphatidylserine externalization, and band 3 protein expression. Results: Cell-free hemoglobin, a marker of hemolysis, increased during pRBC storage. Amitriptyline treatment decreased hemolysis in a dose-dependent manner. Standard pRBC storage led to loss of erythrocyte size and membrane complexity, increased phosphatidylserine externalization, and decreased band 3 protein integrity as determined by flow cytometry. Each of these changes was reduced by treatment with amitriptyline. Transfusion of amitriptyline-treated pRBCs resulted in decreased circulating free hemoglobin. Conclusion: Erythrocyte storage is associated with changes in cell size, complexity, membrane molecular composition, and increased hemolysis. Acid sphingomyelinase inhibition reduced these changes in a dose-dependent manner. Our data suggest a novel mechanism to attenuate the harmful effects after transfusion of aged blood products.

scholarly journals Caspase 3 regulates phosphatidylserine externalization and phagocytosis of oxidatively stressed erythrocytes

FEBS Letters ◽  
2002 ◽  
Vol 513 (2-3) ◽  
pp. 184-188 ◽  
Author(s):  
Debabrata Mandal ◽  
Prasun K Moitra ◽  
Samiran Saha ◽  
Joyoti Basu
Keyword(s):  
Caspase 3 ◽  
Phosphatidylserine Externalization

Another Link between Phospholipid Transmembrane Migration and ABC Transporter Gene Family, Inferred from a Rare Inherited Disorder of Phosphatidylserine Externalization

1997 ◽  
Vol 241 (2) ◽  
pp. 548-552 ◽  
Author(s):  
Florence Toti ◽  
Véronique Schindler ◽  
Jean-François Riou ◽  
Gaël Lombard-Platet ◽  
Edith Fressinaud ◽  
...  
Keyword(s):  
Gene Family ◽  
Abc Transporter ◽  
Transporter Gene ◽  
Phosphatidylserine Externalization

scholarly journals Thresholds for Phosphatidylserine Externalization in Chinese Hamster Ovarian Cells following Exposure to Nanosecond Pulsed Electrical Fields (nsPEF)

PLoS ONE ◽  
2013 ◽  
Vol 8 (4) ◽  
pp. e63122 ◽  
Author(s):  
Rebecca L. Vincelette ◽  
Caleb C. Roth ◽  
Maureen P. McConnell ◽  
Jason A. Payne ◽  
Hope T. Beier ◽  
...  
Keyword(s):  
Chinese Hamster ◽  
Electrical Fields ◽  
Phosphatidylserine Externalization ◽  
Ovarian Cells
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