Higher Cardol Homologues (5-Alkenylresorcinols) from Rye Affect the Red Cell Membrane-Water Transport

1985 ◽  
Vol 40 (1-2) ◽  
pp. 80-84 ◽  
Author(s):  
Arkadiusz Kozubek
Keyword(s):  
Cell Membrane ◽  
Blood Cell ◽  
Water Permeability ◽  
Threshold Concentration ◽  
Water Soluble ◽  
Red Cell ◽  
Cell Water ◽  
Red Cell Membrane ◽  
Soluble Surfactants ◽  
Hypotonic Lysis

The influence of 5-heptadecenylresorcinol and total rye 5-alkenylresorcinols isolated from rye grains on the red blood cell water permeability was studied using osmotic shrinkage experiments performed in 300 mᴍ sucrose. The studied compounds induced significant increase of erythro­cyte water permeability. The threshold concentration needed for the increase of water per­meability was in an order of 10-6mol/l. The temperature dependence of the observed process showed the discontinuity which was related to the 5-alkenylresorcinol transition temperatures. It was shown also that alkenylresorcinols did not exert the biphasic action on hypotonic lysis of erythrocytes usually observed for water soluble surfactants. The specific lysine activity is postulated for the studied compounds.

Evidence that spectrin binds to macromolecular complexes on the inner surface of the red cell membrane

1980 ◽  
Vol 42 (1) ◽  
pp. 1-22 ◽  
Author(s):  
D. Litman ◽  
D.J. Hsu ◽  
V.T. Marchesi
Keyword(s):  
Cell Membrane ◽  
Blood Cell ◽  
Glycophorin A ◽  
Red Cell ◽  
Exposed Surface ◽  
Red Cell Membrane ◽  
Macromolecular Complexes ◽  
High Affinity ◽  
Cytoplasmic Surface ◽  
Inner Surface

Spectrin binds to a population of high-affinity sites on the exposed surface of inverted vesicles prepared from human red blood cell ghost membranes. Optimal spectrin binding requires the presence of monovalent salts but does not require calcium or magnesium. The band 2 subunit of spectrin, prepared in SDS, can also bind to vesicles, but isolated band 1 is inactive. Pre-incubation of inverted vesicles with antibodies directed against the cytoplasmic segment of band 3 or against bands 4.1-4.2 inhibits the binding of spectrin to the same vesicles. Antibodies against the cytoplasmic portion of glycophorin A have no effect. These results suggest that spectrin binds to a protein acceptor on the cytoplasmic surface of the red cell membrane which is close to the cytoplasmic segments of bands 3 and 4.1 and/or 4.2.

Water-soluble proteins of the human red cell membrane

1970 ◽  
Vol 3 (1) ◽  
pp. 156-172 ◽  
Author(s):  
J. Th. Hoogeveen ◽  
R. Juliano ◽  
J. Coleman ◽  
A. Rothstein
Keyword(s):  
Cell Membrane ◽  
Soluble Proteins ◽  
Water Soluble ◽  
Red Cell ◽  
Red Cell Membrane ◽  
Human Red Cell Membrane

scholarly journals Active Uptake of Ca++ and Ca++-Activated Mg++ ATPase in Red Cell Membrane Fragments

1971 ◽  
Vol 57 (2) ◽  
pp. 202-215 ◽  
Author(s):  
Young N. Cha ◽  
Bak C. Shin ◽  
Kwang S. Lee
Keyword(s):  
Cell Membrane ◽  
Blood Cell ◽  
Phospholipase D ◽  
Transport Mechanism ◽  
Red Cell ◽  
Experimental Conditions ◽  
Red Cell Membrane ◽  
Ca Uptake ◽  
Incubation Temperatures ◽  
Phospholipases A

Isolated human red blood cell membrane fragments (RBCMF) were found to take up Ca++ in the presence of ATP.1 This ATP-dependent Ca++ uptake by RBCMF appears to be the manifestation of an active Ca++ transport mechanism in the red cell membrane reported previously (Schatzmann, 1966; Lee and Shin, 1969). The influences of altering experimental conditions on Ca++-stimulated Mg++ ATPase (Ca++ ATPase) and Ca++ uptake of RBCMF were studied. It was found that pretreatment of RBCMF at 50°C abolished both Ca++ ATPase and Ca++ uptake. Pretreatment of RBCMF with phospholipases A and C decreased both Ca++ ATPase and Ca++ uptake, whereas pretreatment with phospholipase D did not significantly alter either Ca++ ATPase or Ca++ uptake. Both Ca++ ATPase and Ca++ uptake had ATP specificity, similar optimum pH's, and optimum incubation temperatures. From these results, it was concluded that Ca++ uptake is intimately linked to Ca++ ATPase.

scholarly journals Phosphorylation of the red blood cell membrane during the active transport of C++.

1976 ◽  
Vol 67 (2) ◽  
pp. 251-261 ◽  
Author(s):  
Y N Cha ◽  
K S Lee
Keyword(s):  
Cell Membrane ◽  
Blood Cell ◽  
Red Blood Cell ◽  
Transport Mechanism ◽  
Initial Reaction ◽  
Red Cell ◽  
Red Cell Membrane ◽  
Red Blood Cell Membrane ◽  
Ca Transport ◽  
Phosphorylation Reaction

The phosphorylation of red blood cell membrane fragments (RBCMF) during Ca++ transport was investigated. When red cell membrane fragments are incubated with [gamma-32P]ATP under the experimental condition which minimizes the phosphorylation of Na+-K+-ATPase, RBCMF are labeled in the presence of Mg++ without Ca++. When Ca++ is added, the labeling decreases due to dephosphorylation of RBCMF. The initial reaction of phosphorylation is reversed in the presence of excess ADP. The treatment of RBCMF with n-ethylmaleimide (NEM) does not interfere with the initial phosphorylation reaction, but blocks the dephosphorylation in the presence of Ca++. These data suggest that the enzymatic sequence of the Ca++ transport mechanism may be very similar to that of the Na+ transport mechanism.

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