scholarly journals A Comparison of CO2 Excretion IA Spontaneously Ventilating Blood Perfused Trout Preparation and Salineperfused Gill Preparations: Contribution of the Branchial Epithelium and Red Blood Cell

1982 ◽  
Vol 101 (1) ◽  
pp. 47-60 ◽  
Author(s):  
STEVE F. PERRY ◽  
PETER S. DAVIE ◽  
DAVID J. RANDALL
Keyword(s):  
Blood Cell ◽  
Red Blood Cell ◽  
Coho Salmon ◽  
Disulfonic Acid ◽  
Gill Epithelium ◽  
Rate Limiting Step ◽  
Branchial Epithelium ◽  
Epithelium Cells ◽  
Co2 Excretion

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

scholarly journals Chemical Modification of Membranes

1971 ◽  
Vol 58 (2) ◽  
pp. 190-210 ◽  
Author(s):  
Philip A. Knauf ◽  
Aser Rothstein
Keyword(s):  
Blood Cell ◽  
Red Blood Cell ◽  
Sulfonic Acid ◽  
Disulfonic Acid ◽  
Trinitrobenzene Sulfonic Acid ◽  
Ion Permeability ◽  
Amino Groups ◽  
Cation Permeability ◽  
X Irradiation

Four different amino-reactive reagents, 4-acetamido-4'-isothiocyano-stilbene-2,2'-disulfonic acid (SITS),1 1-fluoro-2,4-dinitrobenzene (FDNB), 2,4,6-trinitrobenzene sulfonic acid (TNBS), and 2-methoxy-5-nitrotropone (MNT) decrease the anion permeability of the human red blood cell, as measured by sulfate fluxes, whereas the sulfhydryl agent, parachloromercuriphenyl sulfonic acid (PCMBS), does not. In contrast, PCMBS increases the cation permeability as measured by K+ leakage, whereas SITS does not. Of the other agents, FDNB increases the cation permeability to the same extent as PCMBS but MNT and TNBS produce smaller increases. PCMBS does not protect against FDNB as it does against other sulfhydryl agents (X-irradiation) and the FDNB effect on cations is attributed to amino groups. Studies of the binding of SITS indicate that it does not penetrate into the membrane and its failure to influence cation permeability is attributed to its inability to reach an internal population of amino groups. It is concluded that two ion permeability barriers, both involving proteins, are present in the red blood cell. The more superficial barrier contains amino groups and controls anion flow; the more internal barrier contains sulfhydryl and amino groups and controls cation flow. The amino groups contribute to the control of permeability by virtue of their positive charges, but the role of sulfhydryl groups is not clear. Only a small fraction of the membrane protein amino and sulfhydryl is involved in the barriers.

The role of policy in red blood cell storage and transfusion in children

2017 ◽  
Vol 82 (6) ◽  
pp. 894-896
Author(s):  
Jean L Raphael ◽  
Keyword(s):  
Blood Cell ◽  
Red Blood Cell ◽  
Cell Storage

scholarly journals Recent insights into nitrite signaling processes in blood

2017 ◽  
Vol 398 (3) ◽  
pp. 319-329 ◽  
Author(s):  
Christine C. Helms ◽  
Xiaohua Liu ◽  
Daniel B. Kim-Shapiro
Keyword(s):  
Nitric Oxide ◽  
Human Physiology ◽  
Blood Cell ◽  
Red Blood Cell ◽  
Nitrite Reduction ◽  
No Production ◽  
The Past ◽  
Acidic Conditions ◽  
Hypoxic Vasodilation

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.

Blood viscosity during the neonatal period: The role of plasma and red blood cell type

1982 ◽  
Vol 100 (3) ◽  
pp. 449-453 ◽  
Author(s):  
Lise Riopel ◽  
Jean-Claude Fouron ◽  
Harry Bard
Keyword(s):  
Blood Cell ◽  
Red Blood Cell ◽  
Blood Viscosity ◽  
Neonatal Period ◽  
Cell Type ◽  
Blood Cell Type

scholarly journals Hemoglobin-spectrin complexes: interference with spectrin tetramer assembly as a mechanism for compartmentalization of band 1 and band 2 complexes

Blood ◽  
1995 ◽  
Vol 86 (1) ◽  
pp. 366-371 ◽  
Author(s):  
CR Kiefer ◽  
JF Trainor ◽  
JB McKenney ◽  
CR Valeri ◽  
LM Snyder
Keyword(s):  
Blood Cell ◽  
Western Blot ◽  
Red Blood Cell ◽  
Blot Analysis ◽  
Natural Phenomenon ◽  
Cell Aging ◽  
Cell Deformability ◽  
Self Association

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).

The role of malaria merozoite proteases in red blood cell invasion

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