Role of FK506 Binding Protein on Tacrolimus Distribution in Red Blood Cells

2020 ◽  
Vol 37 (7) ◽  
Author(s):  
Naoki Yoshikawa ◽  
Tsubasa Yokota ◽  
Ayako Matsuo ◽  
Nobuhiro Matsumoto ◽  
Tomomi Iwakiri ◽  
...  
Keyword(s):  
Red Blood Cells ◽  
Blood Cells ◽  
Binding Protein ◽  
Fk506 Binding Protein

scholarly journals Detection of acyl-CoA-binding protein in human red blood cells and investigation of its role in membrane phospholipid renewal

1995 ◽  
Vol 306 (3) ◽  
pp. 793-799 ◽  
Author(s):  
H Fyrst ◽  
J Knudsen ◽  
M A Schott ◽  
B H Lubin ◽  
F A Kuypers
Keyword(s):  
Red Blood Cells ◽  
Blood Cells ◽  
Human Liver ◽  
Plasma Membranes ◽  
Binding Protein ◽  
Human Red Blood Cells ◽  
Low Concentrations ◽  
Membrane Bound ◽  
High Concentrations

Acyl-CoA-binding protein (ACBP) has been identified in a number of tissues and shown to affect the intracellular distribution and utilization of acyl-CoA. We have detected ACBP in the cytosol but not the membrane of human red blood cells and, using an e.l.i.s.a. with antibodies prepared against human liver ACBP, found that its concentration was 0.5 microM. To investigate the role of ACBP in human red blood cells, we added purified human liver ACBP and radiolabelled acyl-CoA to isolated membranes from these cells. ACBP prevented high concentrations of acyl-CoA from binding to the membrane but could not keep the acyl-CoA in the aqueous phase at low concentrations. This suggested the presence of a pool in the membrane with a binding affinity for acyl-CoA that was greater than that of ACBP for acyl-CoA. In the presence of lysophospholipid, this membrane-bound pool of acyl-CoA was rapidly used as a substrate by acyl-CoA:lysophospholipid acyltransferase (LAT) to generate phospholipid from lysophospholipid. We also found that ACBP-bound acyl-CoA was preferred over free acyl-CoA as a substrate by LAT. These results are the first documentation that human red blood cells contain ACBP and that this protein can affect the utilization of acyl-CoA in plasma membranes of these cells. The interactions between acyl-CoA, ACBP and the membrane suggest that there are several pools of acyl-CoA in the human red blood cell and that ACBP may have a role in regulating their distribution and fate.

scholarly journals FK506-binding protein contributes to tacrolimus distribution in red blood cells

2021 ◽  
Vol 94 (0) ◽  
pp. 1-P2-34
Author(s):  
Naoki Yoshikawa ◽  
Ayako Matsuo ◽  
Tsubasa Yokota ◽  
Tomomi Iwakiri ◽  
Ryuji Ikeda
Keyword(s):  
Red Blood Cells ◽  
Blood Cells ◽  
Binding Protein ◽  
Fk506 Binding Protein

Role of Adhesion Molecules and Vascular Endothelium in the Pathogenesis of Sickle Cell Disease

Hematology ◽  
2007 ◽  
Vol 2007 (1) ◽  
pp. 84-90 ◽  
Author(s):  
Marilyn J. Telen
Keyword(s):  
Sickle Cell Disease ◽  
Red Blood Cells ◽  
Adhesion Molecules ◽  
Sickle Cell ◽  
Vascular Endothelium ◽  
Blood Cells ◽  
Cell Disease ◽  
Adhesive Interactions ◽  
Lines Of Evidence

AbstractA number of lines of evidence now support the hypothesis that vaso-occlusion and several of the sequelae of sickle cell disease (SCD) arise, at least in part, from adhesive interactions of sickle red blood cells, leukocytes, and the endothelium. Both experimental and genetic evidence provide support for the importance of these interactions. It is likely that future therapies for SCD might target one or more of these interactions.

scholarly journals Role of Calcium in Phosphatidylserine Externalisation in Red Blood Cells from Sickle Cell Patients

Anemia ◽  
2011 ◽  
Vol 2011 ◽  
pp. 1-8 ◽  
Author(s):  
Erwin Weiss ◽  
David Charles Rees ◽  
John Stanley Gibson
Keyword(s):  
Red Blood Cells ◽  
Sickle Cell ◽  
Blood Cells ◽  
Phosphatidylserine Exposure ◽  
Channel Inhibition ◽  
Cation Conductance ◽  
Gardos Channel ◽  
Cation Permeability

Phosphatidylserine exposure occurs in red blood cells (RBCs) from sickle cell disease (SCD) patients and is increased by deoxygenation. The mechanisms responsible remain unclear. RBCs from SCD patients also have elevated cation permeability, and, in particular, a deoxygenation-induced cation conductance which mediates entry, providing an obvious link with phosphatidylserine exposure. The role of was investigated using FITC-labelled annexin. Results confirmed high phosphatidylserine exposure in RBCs from SCD patients increasing upon deoxygenation. When deoxygenated, phosphatidylserine exposure was further elevated as extracellular [] was increased. This effect was inhibited by dipyridamole, intracellular chelation, and Gardos channel inhibition. Phosphatidylserine exposure was reduced in high saline. levels required to elicit phosphatidylserine exposure were in the low micromolar range. Findings are consistent with entry through the deoxygenation-induced pathway (), activating the Gardos channel. [] required for phosphatidylserine scrambling are in the range achievablein vivo.

scholarly journals The Emerging Role of Large Immunophilin FK506 Binding Protein 51 in Cancer

2011 ◽  
Vol 18 (35) ◽  
pp. 5424-5429 ◽  
Author(s):  
S. Romano ◽  
A. Sorrentino ◽  
A. L. Di Pace ◽  
G. Nappo ◽  
C. Mercogliano ◽  
...  
Keyword(s):  
Binding Protein ◽  
Fk506 Binding Protein

The role of red blood cells in the progression and instability of atherosclerotic plaque

2010 ◽  
Vol 142 (1) ◽  
pp. 2-7 ◽  
Author(s):  
Dimitrios N. Tziakas ◽  
Georgios K. Chalikias ◽  
Dimitrios Stakos ◽  
Harisios Boudoulas
Keyword(s):  
Red Blood Cells ◽  
Atherosclerotic Plaque ◽  
Blood Cells

Red cell oxygen affinity in fetal sheep: role of 2,3-DPG and adult hemoglobin

1978 ◽  
Vol 45 (1) ◽  
pp. 7-10 ◽  
Author(s):  
H. Bard ◽  
J. C. Fouron ◽  
J. E. Robillard ◽  
A. Cornet ◽  
M. A. Soukini
Keyword(s):  
Red Blood Cells ◽  
Blood Cells ◽  
Oxygen Affinity ◽  
Fetal Life ◽  
Red Cell ◽  
Adult Type ◽  
Fetal Sheep ◽  
Adult Hemoglobin ◽  
Relationship Of

Studies were carried out during fetal life in sheep to determine the relationship of 2,3-diphosphoglycerate (DPG), the intracellular red cell and extracellular pH, and the switchover to adult hemoglobin synthesis in regulating the position of the fetal red cell oxygen-affinity curve in utero. Adult hemoglobin first appeared near 120 days of gestation. The mean oxygen tension at which hemoglobin is half saturated (P50) prior to 120 days of gestation remained constant at 13.9 +/- 0.3 (SD) Torr and then increased gradually as gestation continued, reaching 19 Torr at term. During the interval of fetal life studied, the level of DPG was 4.43 +/- 1.63 (SD) micromol/g Hb and the deltapH between plasma and red blood cells was 0.227 +/- 0.038 (SD); neither was affected by gestational age. The decrease in the red cell oxygen affinity after 120 days of gestation ocrrelated with the amount of adult hemoglobin present in the fetus (r = 0.78; P less than 0.001). This decrease can be attributed only to the amount of the adult-type hemoglobin present, and not to DPG, or to changes in the deltapH between plasma and red blood cells, because both remained stable during the last trimester.

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