Deglycosylation of apo B-containing lipoproteins increase their ability to aggregate and to promote intracellular cholesterol accumulation in vitro.

Sub-fractions of all apo B-100 containing lipoproteins (low density lipoproteins, very low density lipoproteins and intermediate density lipoproteins) with reduced contents of sialic acid were found in vivo in human blood. These lipoproteins were inclined to spontaneously form aggregates and were able to stimulate accumulation of cholesterol in cells cultured from human aortic intima. In vitro treatment of apo B-containing lipoproteins with 2,6- and 2,3-specific sialidases, alpha-mannosidase, endoglycosidases F1 or F2 or peptide-N-glycanase F also stimulated aggregation and increased the ability of these particles to potentiate cholesterol accumulation in cells of the intact human aortic intima. So, deglycosylation of various apo B-containing lipoproteins possibly occurs in the blood, decreases their resistance to aggregation and increases the ability of these particles to stimulate accumulation of cholesterol in human aortic intima cells, thereby increasing their atherogenic potential.

[The nature of phosphate residue binding in the phosphorylated form of succinyl-CoA-synthetase from pigeon breast muscle]. / Izuchenie prirody sviazyvaniia ostatkov fosfata v fosforilirovannoi forme suktsinil-CoA-sintetazy iz grudnoi myshtsy golubia.

The hydrolytic stability of phosphorylated pigeon breast muscle succinyl-CoA synthetase within a wide pH range was studied. It was found that within complex I the phosphate-protein bond is hydrolyzed at alkaline values of pH (11.0 and 13.0); at acidic pH values this bond is hydrolyzed by 50%. Within complex II the phosphate-protein bond is hydrolyzed at acidic pH values and is stable at alkaline pH values. The reaction of the phosphorylated enzyme with hydroxylamine and diisopropylfluorophosphate results in protein dephosphorylation by 50%. Ion-exchange chromatography of the radioactive phosphorylated enzyme II alkaline hydrolyzate (3 n NaOH, 3 hours, 100 degrees C) revealed that the radioactivity was distributed between 1-N-, 3-N-phosphohistidine and 1.3-N-diphosphohistidine fractions. The experimental results suggest that in the phosphorylated enzyme I phosphate is bound to the protein to form an acyl phosphate and phosphoester bonds, while in the phosphorylated enzyme II phosphate binding to the protein occurs with the formation of phosphoamide bonds.