https://www.cell.com/cell/pdf/0092-8674(92)90553-O.pdf

TNF activates NF-κB by phosphatidylcholine-specific phospholipase C-induced “Acidic” sphingomyelin breakdown

Considerable evidence supports the hypothesis that renal sodium excretion is partly regulated by a humoral agent released or activated by extracellular fluid volume (ECFY) expansion1, including the demonstration of biological activities in extracts of plasma and urine which support the natriuretic hormone (NH) hypothesis2–4. NH is a low molecular weight peptide formed from a precursor in plasma5, which inhibits sodium transport (anti-natriferic activity) in isolated toad bladder, an analogue of the distal renal tubule and collecting duct. Other evidence indicates that NH can inhibit renal (Na++ K+) ATPase6, which suggests that it might be an endogenous digitalis-like substance. Although an immunoreactive ouabain-like substance has been demonstrated in amphibian plasma7, none has been reported in mammals. To identify an endogenous digitalis-like substance, we used an approach suggested by the work of Spector and his collaborators, who demonstrated that biological substances which bind to the same receptors as drugs, such as endogenous opioids8 and benzodiazepines9, may compete with antibodies specific for the drugs. Hough and Edwardson10 showed that antibodies to thaumatin, a sweet-tasting plant protein, also bind non-protein sweet substances in a linearly related fashion to the sweetness of the compound, suggesting that the antibody binding site may be similar to the sweet taste receptor. Based on these observations, we postulated that if NH were an endogenous digitalis-like substance, it might bind to antibodies specific for digitalis glycosides. We report here the preliminary isolation of a substance in plasma of dogs which competes with digoxin for two specific digoxin antibodies and is an inhibitor of (Na+ + K+) ATPase activity. Increased amounts of this factor are found in plasma of volume-expanded dogs, suggesting it is the putative NH.

Endogenous digitalis-like substance in plasma of volume-expanded dogs

Publisher Summary This chapter discusses the metabolism of molecular species of diacylglycerophospholipids. The glycerolipid composition of cell membranes and lipoproteins is metabolically adjusted to meet specific requirements, and it does not merely reflect the supply of different fatty acids in the diet or in the cell culture medium. However, adequate adjustment cannot always be possible, and under such conditions, the cellular activity can take place in a suboptimal physicochemical environment and characteristic symptoms of a disease state can appear. As the cellular lipid composition is subject to considerable dietary and pharmacological manipulation, there can be therapeutic alterations in the composition of the molecular species of the tissues and other animal species. The metabolism of the molecular species of the glycerophospholipids is intimately involved with the activity of the acyl transferases. Therapeutic alterations in the composition of the molecular species of the glycerolipids can be feasible and can yield beneficial results in the treatment of membrane diseases.

Metabolism of molecular species of diacylglycerophospholipids.

Superoxide anion permeability of phospholipid membranes and chloroplast thylakoids

Electrostatic interactions at charged lipid membranes: I. Effects of ph and univalent cations on membrane structure

https://deepblue.lib.umich.edu/bitstream/handle/2027.42/32933/0000316.pdf

Hansjörg Eibl

Papers

A new, sensitive determination of phosphate

Acyl coenzyme a: 2-acyl-sn-glycerol-3-phosphate acyltransferase activity in rat liver microsomes

A new spectrophotometric micro determination of vicinal diols