Amyloid beta peptide (1-42)-mediated antioxidant imbalance is associated with activation of protein kinase C in red blood cells

2015 ◽  
Vol 33 (4) ◽  
pp. 196-201 ◽  
Author(s):  
Cristiana Carelli-Alinovi ◽  
Bruno Giardina ◽  
Francesco Misiti
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Red Blood Cells ◽  
Amyloid Beta ◽  
Blood Cells ◽  
Amyloid Beta Peptide ◽  
Kinase C ◽  
Beta Peptide

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 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

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
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