Comparative physiology and molecular analysis of carbonic anhydrase from the red blood cells of teleost fish

2004 ◽  
Vol 174 (5) ◽  
Author(s):  
A.J. Esbaugh ◽  
S.G. Lund ◽  
B.L. Tufts
Keyword(s):  
Carbonic Anhydrase ◽  
Red Blood Cells ◽  
Molecular Analysis ◽  
Teleost Fish ◽  
Blood Cells ◽  
Comparative Physiology

Adenosine causes cAMP-dependent activation of chick embryo red cell carbonic anhydrase and 2,3-DPG synthesis

1996 ◽  
Vol 271 (4) ◽  
pp. R973-R981 ◽  
Author(s):  
S. Glombitza ◽  
S. Dragon ◽  
M. Berghammer ◽  
M. Pannermayr ◽  
R. Baumann
Keyword(s):  
Carbonic Anhydrase ◽  
Red Blood Cells ◽  
Adenylyl Cyclase ◽  
Adenosine Receptor ◽  
Blood Cells ◽  
Cell Protein ◽  
Red Cell ◽  
Receptor Stimulation ◽  
2,3 Dpg ◽  
Stimulation Of

In late chick embryos, coordinate activation of red cell carbonic anhydrase II (CAII) and 2,3-diphosphoglycerate (2,3-DPG) synthesis is initiated by hypoxia. The effects are mediated by unidentified hormonal effectors resident in chick plasma. In the present investigation, we have analyzed the effect of adenosine receptor stimulation on embryonic red cell CAII and 2,3-DPG synthesis. We find that primitive and definitive embryonic red blood cells from chick have an A2a adenosine receptor. Stimulation of the receptor with metabolically stable adenosine analogues causes a large increase of red cell adenosine 3',5'-cyclic monophosphate (cAMP) and subsequent activation of red cell CAII and 2,3-DPG production in definitive red blood cells and of CAII synthesis in primitive red blood cells. Direct stimulation of adenylyl cyclase with forskolin has the same effect. Analysis of red cell protein pattern after labeling with [35S]methionine shows that stimulation of red cell cAMP levels activates synthesis of several other proteins aside from CAII. Presence of actinomycin D inhibits cAMP-dependent changes of protein synthesis, indicating that cAMP-dependent transcriptional activation is required. In contrast to the stable adenosine receptor analogues, adenosine itself was a very weak agonist, unless its metabolism was significantly inhibited. Thus, besides adenosine, other effectors of the adenylyl cyclase system are likely to be involved in the O2 pressure-dependent regulation of red cell metabolism in late development of avian embryos.

IgM Natural Autoantibodies Against Bromelain-Treated Mouse Red Blood Cells Recognise Carbonic Anhydrase

Autoimmunity ◽  
1991 ◽  
Vol 9 (3) ◽  
pp. 207-216 ◽  
Author(s):  
A. M. Jonusysj ◽  
K. O. Cox ◽  
E. J. Steele
Keyword(s):  
Carbonic Anhydrase ◽  
Red Blood Cells ◽  
Blood Cells ◽  
Treated Mouse ◽  
Natural Autoantibodies

scholarly journals Parvovirus B19 infection transmitted by transfusion of red blood cells confirmed by molecular analysis of linked donor and recipient samples

Transfusion ◽  
2010 ◽  
Vol 50 (8) ◽  
pp. 1712-1721 ◽  
Author(s):  
Mei-ying W. Yu ◽  
Harvey J. Alter ◽  
Maria Luisa A. Virata-Theimer ◽  
Yansheng Geng ◽  
Li Ma ◽  
...  
Keyword(s):  
Red Blood Cells ◽  
Molecular Analysis ◽  
Blood Cells ◽  
Parvovirus B19 ◽  
Parvovirus B19 Infection

Properties of a carbonic anhydrase inhibitor protein in flounder serum

2000 ◽  
Vol 203 (19) ◽  
pp. 3003-3009 ◽  
Author(s):  
T. Peters ◽  
F. Papadopoulos ◽  
H.P. Kubis ◽  
G. Gros
Keyword(s):  
Carbonic Anhydrase ◽  
Red Blood Cells ◽  
Exchange Reaction ◽  
Blood Cells ◽  
Gel Filtration ◽  
Extracellular Fluid ◽  
Circulatory System ◽  
Inhibitory Effect ◽  
Carbonic Anhydrase Inhibitor ◽  
European Flounder

The blood serum of the European flounder Platichthys flesus strongly inhibits soluble erythrocytic carbonic anhydrase from the same species. The inhibition is of the uncompetitive type. Hence, the mechanism of the carbonic anhydrase inhibition is different from that of all other known carbonic anhydrase inhibitors. The serum showed no inhibitory effect on carbonic anhydrase from human and bovine red blood cells. By applying the (18)O exchange reaction, it could be demonstrated that the presence of the carbonic anhydrase inhibitor in the extracellular fluid has no effect on carbonic anhydrase in intact red blood cells. Thus, this carbonic anhydrase inhibitor seems to act only within the plasma space of the circulatory system. However, the carbonic anhydrase inhibitor does appear to reduce the bicarbonate permeability of flounder red cells to approximately one-quarter of normal levels as measured by the (18)O exchange reaction. The 28 kDa carbonic anhydrase inhibitor was isolated from the serum by gel filtration. The isolated inhibitor was detected in acrylamide gels as a single band representing a 7 kDa protein. The denaturing conditions used in electrophoresis presumably led to a dissociation of the native protein into subunits.

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