Thyroid hormone stimulates release of calmodulin-enhancing activity from human erythrocyte membranes in vitro

1993 ◽  
Vol 84 (2) ◽  
pp. 217-223 ◽  
Author(s):  
William D. Lawrence ◽  
Mark R. Deziel ◽  
Paul J. Davis ◽  
Marion Schoenl ◽  
Faith B. Davis ◽  
...  
Keyword(s):  
Thyroid Hormone ◽  
Human Erythrocyte ◽  
Erythrocyte Membranes ◽  
Soluble Factor ◽  
Heat Stable ◽  
Enhancing Factor ◽  
Human Erythrocyte Membranes ◽  
Subsequent Addition ◽  
Stable Control

1. Thyroid hormone (L-thyroxine, 10−10mol/l) incubated in vitro with human erythrocyte membranes induced the release of a soluble calmodulin-like material, the 3′:5′-cyclic nucleotide phosphodiesterase-stimulating activity of which was at least six-fold greater than its concentration measured by a specific calmodulin radioimmunoassay. 2. The material had the characteristics of calmodulin in that it stimulated both phosphodiesterase and erythrocyte Ca2+-ATPase activities, cross-reacted with and was neutralized by anti-calmodulin antibody, was adsorbed by phenothiazine-Sepharose and was heat-stable. Control supernatant from the incubation of membranes in the absence of thyroxine contained calmodulin, the bioactivity of which was not enhanced beyond that predicted from radioimmunoassay. Subsequent addition of thyroxine did not increase calmodulin bioactivity. Calmodulin-agarose removed calmodulin-enhancing activity from the supernatant. 3. Thus, the enhancing factor(s) appears to interact directly with calmodulin. These observations indicate that thyroid hormone promotes the release from human erythrocyte membranes of a soluble factor (or factors) which binds to calmodulin and significantly increases its bioactivity. This enhancing activity is similar to that of a calmodulin activator described in a rat model of hypertension (S.-L. Huang et al., J Clin Invest 1988; 82: 276-81).

scholarly journals Degradation of Band-3 Glycoprotein in vitro by a Protease Isolated from Human Erythrocyte Membranes

1982 ◽  
Vol 121 (2) ◽  
pp. 463-467 ◽  
Author(s):  
Anne Marianne GOLOVTCHENKO-MATSUMOTO ◽  
Isamu MATSUMOTO ◽  
Toshiaki OSAWA
Keyword(s):  
Human Erythrocyte ◽  
Band 3 ◽  
Erythrocyte Membranes ◽  
Human Erythrocyte Membranes

scholarly journals Stereochemical requirements for the modulation by retinoic acid of thyroid hormone activation of Ca2+-ATPase and binding at the human erythrocyte membrane

1992 ◽  
Vol 284 (2) ◽  
pp. 583-587 ◽  
Author(s):  
T J Smith ◽  
F B Davis ◽  
P J Davis
Keyword(s):  
Retinoic Acid ◽  
Fatty Acid ◽  
Thyroid Hormone ◽  
Erythrocyte Membrane ◽  
Human Erythrocyte ◽  
Binding Sites ◽  
Erythrocyte Membranes ◽  
Side Chain ◽  
Acid Molecule

Physiological concentrations of retinoic acid can block the activation of human erythrocyte Ca(2+)-ATPase in vitro by thyroid hormone [Smith, Davis & Davis (1989) J. Biol. Chem. 264, 687-689]. The present studies were undertaken to ascertain the nature of this blockade. Two binding sites for L-thyroxine (T4) were demonstrated on washed erythrocyte membranes; the high-affinity site had a Kd value of 2.7 x 10(-10)M and a Bmax. of 76 fmol/mg of protein. The lower-affinity site possessed a Kd of 1 x 10(-8) M. Retinoic acid was as potent a displacer of radiolabelled T4 as was the unlabelled hormone. Certain retinoic acid analogues with either ring or fatty acid side chain modifications retained some ability to displace [125I]T4 binding and to block iodothyronine activation of Ca(2+)-ATPase. The side chain terminal carboxyl group was essential for full activity of the retinoic acid molecule. Its absence or replacement with an ethylsulphone group rendered the molecule considerably less active in the ATPase model. Retinol, 13-cis-retinoic acid, benzene-substituted all-trans-retinoic acid and polyprenoic acid all failed to influence iodothyronine binding or to block activation of Ca(2+)-ATPase by T4. There was good agreement between the ability of an analogue to displace [125I]iodothyronine binding and its ability to inhibit the T4-dependent activation of the Ca(2+)-ATPase. It would appear from these observations that retinoic acid can modulate the activation of erythrocyte membrane Ca(2+)-ATPase by thyroid hormone through a mechanism which involves displacement of iodothyronine from binding sites. These activities apparently derive from both the ring structure and the fatty acid side chain of the retinoic acid molecule.

Effect of Aldosterone on the Human Erythrocyte Sodium-Potassium Pump in vitro

1983 ◽  
Vol 64 (2) ◽  
pp. 183-186 ◽  
Author(s):  
N. Stern ◽  
F. Beck ◽  
J. Sowers
Keyword(s):  
Atpase Activity ◽  
Human Erythrocyte ◽  
Erythrocyte Membranes ◽  
Ouabain Binding ◽  
Physiological Concentration ◽  
Sodium Potassium ◽  
Human Erythrocyte Membranes ◽  
Erythrocyte Sodium ◽  
Sodium Potassium Pump

1. The effects of aldosterone in vitro on the Na+,K+-dependent ATPase activity of isolated human erythrocyte membranes and on rubidium (86Rb) uptake and [3H]ouabain binding of intact erythrocytes were studied. 2. ATPase activity was nearly doubled (0.061 ± 0.006 to 0.110 ± 0.01 μmol of Pl h−1 mg−1 of protein) by the addition of a physiological concentration of aldosterone (2.7 × 10-10 mol/l). Higher concentrations had no greater effect. 3. Aldosterone had no significant effect on 86Rb uptake or [3H]ouabain binding. 4. Erythrocytes contain aldosterone at concentrations similar to that in plasma. The effect of aldosterone on ATPase is probably maximal.

scholarly journals Identification of a sialoglycopeptide released by self-digestion from human erythrocyte membranes

1976 ◽  
Vol 158 (2) ◽  
pp. 497-500 ◽  
Author(s):  
A Brovelli ◽  
G Pallavicini ◽  
F Sinigaglia ◽  
C L Balduini ◽  
C Balduini
Keyword(s):  
Amino Acids ◽  
Chemical Composition ◽  
Human Erythrocyte ◽  
Molecular Size ◽  
Erythrocyte Membranes ◽  
Erythrocyte Ghosts ◽  
Human Erythrocyte Membranes

Membranes from human O Rhesus-positive erythrocyte ‘ghosts’ were tested in vitro for their ability to digest their own glycoproteins. ‘Ghost’ membranes incubated in Tris/HCl buffer, pH 7.4, release a sialoglycopeptide, which contains glucosamine, galactosamine, galactose and mainly polar amino acids. Chemical composition, molecular size and aggregation properties suggest that this glycopeptide may be a fragment of glycophorin.

Effects of phenylpropanolamine (PPA) on in vitro human erythrocyte membranes and molecular models

2011 ◽  
Vol 406 (3) ◽  
pp. 320-325 ◽  
Author(s):  
Mario Suwalsky ◽  
Pablo Zambrano ◽  
Sigrid Mennickent ◽  
Fernando Villena ◽  
Carlos P. Sotomayor ◽  
...  
Keyword(s):  
Human Erythrocyte ◽  
Erythrocyte Membranes ◽  
Molecular Models ◽  
Human Erythrocyte Membranes

scholarly journals Interaction of platelet plasma membranes with thrombin-activated platelets

Blood ◽  
1981 ◽  
Vol 57 (2) ◽  
pp. 305-312 ◽  
Author(s):  
HR Prasanna ◽  
HH Edwards ◽  
DR Phillips
Keyword(s):  
Human Erythrocyte ◽  
Plasma Membranes ◽  
Membrane Binding ◽  
Human Platelets ◽  
Platelet Membrane ◽  
Erythrocyte Membranes ◽  
Functional Sites ◽  
Activated Platelets ◽  
Platelet Membranes ◽  
Human Erythrocyte Membranes

Abstract This study described the binding of platelet plasma membranes to either control or thrombin-activated platelets. Glycoproteins in plasma membranes isolated from human platelets were labeled by oxidation with periodate followed by reduction with [3H]NaBH4. Labeled membranes were incubated with either control or thrombin-activated platelets. The amount of membranes bound was measured by separating platelets with bound membranes from solution by rapid centrifugation through 27% sucrose and determining the amount of radioactivity associated with platelets. Five- to sevenfold more membranes bound to thrombin- activated platelets than to control platelets. This enhanced binding of labeled membranes was completely inhibited by an excess of unlabeled platelet membranes. Human erythrocyte membranes had little affinity for either washed or thrombin-activated platelets and therefore did not compete for platelet-membrane binding. Binding of platelet membranes to thrombin-treated platelets was inhibited by prior incubation of the platelets with PGI2 suggesting that the enhanced binding of membranes was to activated platelets. This study demonstrates that the purified platelet membranes have functional sites that can mediate membrane binding to platelets and that quantitation of membrane binding appears to reflect the increased aggregation capability of activated platelets.

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