Cellular membranes and membrane-bound enzymes in vitamin E deficiency. A histochemical, cytochemical, biochemical, and morphologic study of the liver of the Pekin duckling.
The objective of this investigation was to find out whether vitamin E deficiency, apart from influencing the lipid component of cellular membranes, also influences the protein component. For that purpose a number of membrane-bound enzymes in the liver of the Pekin duckling were histochemically, cytochemically, and biochemically examined. Furthermore, cells, cellular membranes, and protein particles in membranes were morphometrically investigated. Histochemically five membrane-bound enzymes appeared to be stimulated in vitamin E deficiency: 5'-nucleotidase, glucose-6-phosphatase, isocitrate dehydrogenase (NADP), tetrazolium reductase (NADH), and tetrazolium reductase (NADPH). 5'-Nucleotidase and glucose-6-phosphatase were also investigated cytochemically and biochemically. The cytochemical localization of these enzymes was identical in control and vitamin E-deficient ducklings. Biochemically, a stimulation of these two enzymes also could be demonstrated. The increase per milligram of DNA appeared to be largest whereas the increase per milligram of protein, per milligram of phospholipid, and per milligram of RNA was only half of the increase per milligram of DNA. This can be explained by the 30 per cent increase of the cell volume in vitamin E deficiency leading to an increase of protein, phospholipid, and RNA per cell. The thickness of membranes and the diameter of protein particles in membranes were measured in liver parenchymal cells. In vitamin E deficiency the thickness of the outer mitochondrial membrane and the diameter of protein particles in this membrane were smaller whereas the thickness of the endoplasmic reticular membrane was larger. The increase of the activities of mitochondrial and microsomal enzymes and the decrease of the thickness of the outer mitochondrial membrane and of its protein particles are interpreted to be the result of the influence of free radicals on membranes with electron transport functions. The increase of 5'-nucleotidase activity in the plasma membrane is likely to have a different cause; it may be related to the transport of nucleotides across this membrane.
D000818:Animals; D001665:Binding Sites; D001693:Biological Transport, Active; D002462:Cell Membrane / Q000201:enzymology*; D002463:Cell Membrane Permeability; D004247:DNA / Q000378:metabolism; D004372:Ducks / Q000033:anatomy & histology*; D005609:Free Radicals; D005952:Glucose-6-Phosphatase / Q000378:metabolism; D007521:Isocitrate Dehydrogenase / Q000378:metabolism; D008099:Liver / Q000201:enzymology* / Q000648:ultrastructure; D008854:Microscopy, Electron; D009246:NADH Tetrazolium Reductase / Q000378:metabolism; D009708:Nucleotidases / Q000378:metabolism; D010743:Phospholipids / Q000378:metabolism; D011506:Proteins / Q000378:metabolism; D012313:RNA / Q000378:metabolism; D014811:Vitamin E Deficiency / Q000201:enzymology* / Q000473:pathology
D005609:Free Radicals; D010743:Phospholipids; D011506:Proteins; D012313:RNA; D004247:DNA; D007521:Isocitrate Dehydrogenase; D009246:NADH Tetrazolium Reductase; D009708:Nucleotidases; D005952:Glucose-6-Phosphatase