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At least 703 records · Page 39Linked to original sources
PubMed1989

Erythrocyte membrane Ca2+ ATPase: reactivities of human A, AS, and S erythrocytes with steroid hormones.

In a preliminary study we reported a significant enhancement of Ca2+ ATPase activity in sickle cell membranes in the presence of progesterone and testosterone. In this work the reactivity of various classes of steroid hormones with the membranes of hemoglobin variants was investigated. A consistent universal stimulation of Ca2+ ATPase activity in sickle cell membranes by the different classes of steroid hormones does not appear to correlate with any major structural differences of the hormones or the presence of reactive functional groups. The universal interaction of the hormones with sickle cell membranes probably enhances Ca2+ efflux through the Ca2+ ATPase without directly affecting the characteristics of the pump.

Anemia, Sickle Cell↗
PubMed2003

Occurrence of lipid receptors inferred from brain and erythrocyte spectrins binding NaOH-extracted and protease-treated neuronal and erythrocyte membranes.

It was previously shown in model systems that brain spectrin binds membrane phospholipids. In the present study, we analysed binding of isolated brain spectrin and red blood cell spectrin to red blood or neuronal membranes which had been treated as follows: (1). extracted with low ionic-strength solution, (2). the above membranes extracted with 0.1 M NaOH, and (3). membranes treated as above, followed by protease treatment and re-extraction with 0.1 M NaOH. It was found that isolated, NaOH-extracted, protease-treated neuronal and red blood cell membranes bind brain and red blood cell spectrin with moderate affinities similar to those obtained in model phospholipid membrane-spectrin interaction experiments. Moreover, this binding was competitively inhibited by liposomes prepared from membrane lipids. The presented results indicate the occurrence of receptor sites for spectrins that are extraction- and protease-resistant, therefore most probably of lipidic nature, in native membranes.

Animals↗
PubMed1987

Electron spin resonance (ESR) studies of skeletal protein interactions in human erythrocyte membranes exposed to polyanions and in membranes prepared from inositol hexaphosphate (IHP)-incorporated low-affinity erythrocytes.

Previous biophysical investigations, including those from our laboratories, have reported that polyphosphates weaken RBC membrane skeletal protein-protein interactions and decrease hemoglobin affinity for oxygen. We have additionally demonstrated that low-affinity intact RBC's may be produced by inositol hexaphosphate (IHP) incorporation via an osmotic pulse method. In the present electron spin resonance (ESR) study, IHP was shown to cause a concentration-dependent increase in the segmental motion of ghost membrane skeletal proteins, but no alterations in spin-labeled terminal sialic acid. Pyrophosphate and inositol hexasulfate were significantly less effective in altering the physical state of skeletal proteins than was IHP. Additional ESR studies of both the interaction of IHP with membrane skeletal proteins in the presence of hemoglobin and of membranes obtained from osmotic pulse-treated intact cells were performed. The results of all these studies are discussed in terms of previous biophysical investigations of the effects of polyphosphates on membranes and of possible molecular events that occur during the osmotic pulse procedure.

2,3-Diphosphoglycerate↗