Protein Kinase C Activation Induces Phosphatidylserine Exposure on Red Blood Cells†

Biochemistry ◽  
2002 ◽  
Vol 41 (41) ◽  
pp. 12562-12567 ◽  
Author(s):  
Kitty de Jong ◽  
Michael P. Rettig ◽  
Philip S. Low ◽  
Frans A. Kuypers
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Red Blood Cells ◽  
Blood Cells ◽  
Kinase C ◽  
Phosphatidylserine Exposure ◽  
Protein Kinase C Activation

scholarly journals Supernatants and lipids from stored red blood cells activate pulmonary microvascular endothelium through the BLT2 receptor and protein kinase C activation

Transfusion ◽  
2017 ◽  
Vol 57 (11) ◽  
pp. 2690-2700 ◽  
Author(s):  
Christopher C. Silliman ◽  
Marguerite R. Kelher ◽  
Samina Y. Khan ◽  
F. Bernadette West ◽  
Nathan J.D. McLaughlin ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Red Blood Cells ◽  
Blood Cells ◽  
Microvascular Endothelium ◽  
Kinase C ◽  
Protein Kinase C Activation

Phorbol ester stimulates a protein kinase C–mediated agatoxin-TK–sensitive calcium permeability pathway in human red blood cells

Blood ◽  
2002 ◽  
Vol 100 (9) ◽  
pp. 3392-3399 ◽  
Author(s):  
Dina A. Andrews ◽  
Lu Yang ◽  
Philip S. Low
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Calcium Channel ◽  
Red Blood Cells ◽  
Blood Cells ◽  
Mature Erythrocyte ◽  
Phospholipid Scramblase ◽  
Rbc Membrane ◽  
Kinase C ◽  
Calcium Permeability

AbstractCalcium entry into mature erythrocytes (red blood cells; RBCs) is associated with multiple changes in cell properties. At low intracellular Ca2+, efflux of potassium and water predominates, leading to changes in erythrocyte rheology. At higher Ca2+ content, activation of kinases and phosphatases, rupture of membrane-to-skeleton bridges, stimulation of a phospholipid scramblase and phospholipase C, and induction of transglutaminase-mediated protein cross-linking are also observed. Because the physiologic relevance of these latter responses depends partially on whether Ca2+ entry involves a regulated channel or nonspecific leak, we explored mechanisms that initiate controlled Ca2+ influx. Protein kinase C (PKC) was considered a prime candidate for the pathway regulator, and phorbol-12 myristate-13 acetate (PMA), a stimulator of PKC, was examined for its influence on erythrocyte Ca2+. PMA was found to stimulate a rapid, dose-dependent influx of calcium, as demonstrated by the increased fluorescence of an entrapped Ca2+-sensitive dye, Fluo-3/am. The PMA-induced entry was inhibited by staurosporine and the PKC-selective inhibitor chelerythrine chloride, but was activated by the phosphatase inhibitors okadaic acid and calyculin A. The PMA-promoted calcium influx was also inhibited by ω-agatoxin-TK, a calcium channel blocker specific for Cav2.1 channels. To confirm that a Cav2.1-like calcium channel exists in the mature erythrocyte membrane, RBC membrane preparations were immunoblotted with antiserum against the α1A subunit of the channel. A polypeptide of the expected molecular weight (190 kDa) was visualized. These studies indicate that an ω-agatoxin-TK–sensitive, Cav2.1-like calcium permeability pathway is present in the RBC membrane and that it may function under the control of kinases and phosphatases.

Protein Kinase C and Regulatory Volume Decrease in Mudpuppy Red Blood Cells

1998 ◽  
Vol 166 (2) ◽  
pp. 119-132 ◽  
Author(s):  
D.B. Light ◽  
M.R. Adler ◽  
J.K. Ter Beest ◽  
S.A. Botsford ◽  
R.T. Gronau
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Red Blood Cells ◽  
Blood Cells ◽  
Regulatory Volume Decrease ◽  
Kinase C ◽  
Volume Decrease

Calcium/protein kinase C signaling mechanisms in shear-induced mechanical responses of red blood cells

2021 ◽  
Vol 135 ◽  
pp. 104124
Author(s):  
Elif Ugurel ◽  
Zeynep Busra Kisakurek ◽  
Yasemin Aksu ◽  
Evrim Goksel ◽  
Neslihan Cilek ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Red Blood Cells ◽  
Blood Cells ◽  
Mechanical Responses ◽  
Kinase C ◽  
Signaling Mechanisms

scholarly journals Endothelin-1 Improves the Impaired Filterability of Red Blood Cells through the Activation of Protein Kinase C.

1999 ◽  
Vol 49 (1) ◽  
pp. 113-120 ◽  
Author(s):  
Kanako SAKASHITA ◽  
Tadahiro OONISHI ◽  
Noriaki ISHIOKA ◽  
Nobuhiro UYESAKA
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Red Blood Cells ◽  
Blood Cells ◽  
Endothelin 1 ◽  
Kinase C

scholarly journals Characterization of Microvesicles Released from Human Red Blood Cells

2016 ◽  
Vol 38 (3) ◽  
pp. 1085-1099 ◽  
Author(s):  
Duc Bach Nguyen ◽  
Thi Bich Thuy Ly ◽  
Mauro Carlos Wesseling ◽  
Marius Hittinger ◽  
Afra Torge ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Zeta Potential ◽  
Red Blood Cells ◽  
Blood Cells ◽  
Annexin V ◽  
Human Red Blood Cells ◽  
Isolation And Characterization ◽  
Kinase C

Background/Aims: Extracellular vesicles (EVs) are spherical fragments of cell membrane released from various cell types under physiological as well as pathological conditions. Based on their size and origin, EVs are classified as exosome, microvesicles (MVs) and apoptotic bodies. Recently, the release of MVs from human red blood cells (RBCs) under different conditions has been reported. MVs are released by outward budding and fission of the plasma membrane. However, the outward budding process itself, the release of MVs and the physical properties of these MVs have not been well investigated. The aim of this study is to investigate the formation process, isolation and characterization of MVs released from RBCs under conditions of stimulating Ca2+ uptake and activation of protein kinase C. Methods: Experiments were performed based on single cell fluorescence imaging, fluorescence activated cell sorter/flow cytometer (FACS), scanning electron microscopy (SEM), atomic force microscopy (AFM) and dynamic light scattering (DLS). The released MVs were collected by differential centrifugation and characterized in both their size and zeta potential. Results: Treatment of RBCs with 4-bromo-A23187 (positive control), lysophosphatidic acid (LPA), or phorbol-12 myristate-13 acetate (PMA) in the presence of 2 mM extracellular Ca2+ led to an alteration of cell volume and cell morphology. In stimulated RBCs, exposure of phosphatidylserine (PS) and formation of MVs were observed by using annexin V-FITC. The shedding of MVs was also observed in the case of PMA treatment in the absence of Ca2+, especially under the transmitted bright field illumination. By using SEM, AFM and DLS the morphology and size of stimulated RBCs, MVs were characterized. The sizes of the two populations of MVs were 205.8 ± 51.4 nm and 125.6 ± 31.4 nm, respectively. Adhesion of stimulated RBCs and MVs was observed. The zeta potential of MVs was determined in the range from - 40 mV to - 10 mV depended on the solutions and buffers used. Conclusion: An increase of intracellular Ca2+ or an activation of protein kinase C leads to the formation and release of MVs in human RBCs.

Involvement of acetylcholinesterase and protein kinase C in the protective effect of caffeine against β-amyloid-induced alterations in red blood cells

Biochimie ◽  
2016 ◽  
Vol 121 ◽  
pp. 52-59 ◽  
Author(s):  
Cristiana Carelli-Alinovi ◽  
Silvana Ficarra ◽  
Anna Maria Russo ◽  
Elena Giunta ◽  
Davide Barreca ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Protective Effect ◽  
Red Blood Cells ◽  
Blood Cells ◽  
Kinase C ◽  
Β Amyloid
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