scholarly journals Differential role of Kruppel like factor 1 (KLF1) gene in red blood cell disorders

Genomics ◽  
2019 ◽  
Vol 111 (6) ◽  
pp. 1771-1776 ◽  
Author(s):  
Priya Hariharan ◽  
Roshan Colah ◽  
Kanjaksha Ghosh ◽  
Anita Nadkarni
Keyword(s):  
2017 ◽  
Vol 82 (6) ◽  
pp. 894-896
Author(s):  
Jean L Raphael ◽  

2017 ◽  
Vol 398 (3) ◽  
pp. 319-329 ◽  
Author(s):  
Christine C. Helms ◽  
Xiaohua Liu ◽  
Daniel B. Kim-Shapiro

Abstract Nitrite was once thought to be inert in human physiology. However, research over the past few decades has established a link between nitrite and the production of nitric oxide (NO) that is potentiated under hypoxic and acidic conditions. Under this new role nitrite acts as a storage pool for bioavailable NO. The NO so produced is likely to play important roles in decreasing platelet activation, contributing to hypoxic vasodilation and minimizing blood-cell adhesion to endothelial cells. Researchers have proposed multiple mechanisms for nitrite reduction in the blood. However, NO production in blood must somehow overcome rapid scavenging by hemoglobin in order to be effective. Here we review the role of red blood cell hemoglobin in the reduction of nitrite and present recent research into mechanisms that may allow nitric oxide and other reactive nitrogen signaling species to escape the red blood cell.


1982 ◽  
Vol 100 (3) ◽  
pp. 449-453 ◽  
Author(s):  
Lise Riopel ◽  
Jean-Claude Fouron ◽  
Harry Bard

1982 ◽  
Vol 101 (1) ◽  
pp. 47-60 ◽  
Author(s):  
STEVE F. PERRY ◽  
PETER S. DAVIE ◽  
DAVID J. RANDALL

A spontaneously ventilating blood-perfused trout preparation and saline perfused gill preparations were utilized to investigate the role of the erythrocyte and branchial epithelium in CO2 excretion and acid-base regulation. CO, excretion (MCOCO2) in blood-perfused preparations was positively correlated with haematocrit (Hct), and was abolished completely during plasma-perfusion. Elevating HCO3- concentration of input blood from 10 to 25 mM significantly increased MCOCO2. fourfold in blood-perfused preparations as a result of increased entry of HCO into the red blood cell and not into the gill epithelium. Increased HCO3- concentration was without effect in totally saline-perfused coho salmon (Onchorynchus kisutch). The addition of 4-acetamido-4′-wo-thiocyanatostilbene-2, 2 disulfonic acid (SITS; 10−4 M) to input blood significantly reduced MCO, and oxygen uptake (Mg,OO2) in blood-perfused fish due to inhibition of erythrocytic HCO3-exchange. Unlike blood-perfused preparations, no saline-perfused preparation (isolated holobranchs or totally perfused rainbow trout or coho salmon) displayed measureable CO, excretion at physiological Pco and pH. Increased input PCOt in both blood-perfused and saline-perfused preparations significantly increased MCOt due to enhanced branchial diffusion of molecular CO2. It is concluded that the entry of HCO3- into the erythrocyte is the rate-limiting step in CO, excretion and that movement of HCO3- from plasma to gill epithelium cells in no way contributes to overall CO3 elimination. Note: Department of Physiology and Anatomy, Massey University Palmerston North, New Zealand. Pacific Gamefish Foundation, P.O. Box 25115, Honolulu, Hawaii, U.S.A. 96825


Blood ◽  
1995 ◽  
Vol 86 (1) ◽  
pp. 366-371 ◽  
Author(s):  
CR Kiefer ◽  
JF Trainor ◽  
JB McKenney ◽  
CR Valeri ◽  
LM Snyder

The irreducible complexation of hemoglobin with spectrin is a natural phenomenon of red blood cell aging, positively correlating with increasing cell density and decreasing cell deformability. The current study begins to address the role of these complexes in the disruption of membrane skeletal physiology and structure. The effect of bound hemoglobin on spectrin dimer self-association was investigated in vitro. The extent of conversion of isolated spectrin dimers to tetramers was evaluated as a function of peroxide-induced globin complexation before the conversion incubations. The incremental accumulation of tetramer was observed to decrease with increasing peroxide concentration used in the globin complexation step. The role of oxidized heme in this process was made apparent by the inability of carboxyhemoglobin to inhibit tetramer accumulation. A Western blot analysis of naturally formed globin-spectrin conjugates demonstrated irreducible complexes of globin with both bands 1 and 2. The complexes are tentatively designated “h1” and “h2”. This analysis also demonstrated that h1 is completely extractable from cell ghosts, whereas h2 is only 50% extractable. These findings are incorporated into a hypothesis linking globin-spectrin complexation and the consequent inhibition of spectrin dimer self-association to the clustered band 3 senescence antigen (Low et al, Science 227:531, 1985).


2005 ◽  
Vol 8 (4) ◽  
pp. 422-427 ◽  
Author(s):  
Rebecca A O’Donnell ◽  
Michael J Blackman

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