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PubMed1982

Glycerolipid biosynthesis in rat adipose tissue. IX. Activation of diglyceride acyltransferase by spermine.

The effect of Z protein, bovine serum albumin and spermine on 1,2-diacylglycerol acyltransferase (DGAT) was investigated. DGAT was measured in the presence of [14C]-palmitoyl-CoA and 1,2-diacylglycerol dispersed in Tween 20. As noted earlier, the activation of DGAT was observed in the presence of either spermine or Mg2+, with spermine being more effective. Addition of bovine serum albumin or Z protein to the incubation mixture resulted in further increase in the activity of this enzyme. However, in the absence of spermine or Mg2+, these proteins were ineffective in the activation of this reaction. The activation of DGAT, either by spermine or Mg2+ was reversed in the presence of ATP. Hydrogen peroxide was inhibitory, while catalase had no effect on the activation of DGAT by spermine. These results suggest that the activation of DGAT by spermine may reside in its ability to preserve the membrane integrity of microsomal membranes, to maintain the optimal and noninhibitory levels of palmitoyl-CoA and to provide a cationic environment required for the optimal activity of this enzyme.

Acyltransferases↗
PubMed1975

[Comparative study of neurophysiological effects of unsubstituted phenol ethers of alpha mono- and diglycerides].

The addition of a second alpha-glyceryl to alpha-phenoxypropanediol strongly modifies the inhibitor actions on the synaptic transmission. These new di-ethers do not show solubility nor effect on the water superficial tension and simultaneously do not provoke any neurophysiological inhibitor effect. The ability of cellular penetration by lipidic solubility seems a necessary condition for pharmacological effect of alpha-glyceric ethers.

Animals↗
PubMedDate not supplied

[An increase of CDP-choline: diglyceride phosphocholine transferase reaction in microsome fraction and its decrease in nuclear membranes of the rat liver after treatment with hydrocortisone].

The availability of CDP-choline: diaglyceride phosphocholine transpherase activity in the rat liver nuclear membrane fraction is shown. It is established that the enzyme activity in nuclear membrane fraction makes up less than 1/3 of the analogous activity in microsomes. The hydrocortisone treatment of animals leads to an increase of the enzyme activity in microsomes and to a decrease in the nuclear membranes. The obtained data indicate the existence of the own enzyme of phosphatidyl choline synthesis in the nuclear membranes. This enzyme is, probably, responsible for the nuclear membrane structure when the functional status of cell changes.

Animals↗