Lung lamellar bodies lack certain key enzymes of phospholipid metabolism.
Palmitoyl CoA-glycerol-3-phosphate acyltransferase, phosphatidate phosphohydrolase, and phospholipase A were assayed in subcellular fractions of rat lung, including lamellar bodies, the putative site of storage and secretion of lung surfactant. The specific activity of each of these enzymes in lamellar bodies was relatively low and could be entirely accounted for by a small contamination of the lamellar bodies fraction by microsomes, as quantitated by the presence of the microsomal marker reduced triphosphopyridine nucleotide cytochrome c reductase. These data indicate that lamellar bodies are not the site of synthesis of the lipid component of pulmonary surfactant by pathways involving these enzymes.
D000217:Acyltransferases / Q000032:analysis*; D000818:Animals; D005992:Glycerol-3-Phosphate O-Acyltransferase / Q000032:analysis*; D008168:Lung / Q000201:enzymology* / Q000648:ultrastructure; D008297:Male; D008861:Microsomes / Q000201:enzymology; D008928:Mitochondria / Q000201:enzymology; D008995:Monoamine Oxidase / Q000032:analysis; D009251:NADPH-Ferrihemoprotein Reductase / Q000032:analysis; D010740:Phospholipases / Q000032:analysis*; D010743:Phospholipids / Q000378:metabolism*; D010744:Phosphoric Monoester Hydrolases / Q000032:analysis*; D051381:Rats; D013347:Subcellular Fractions / Q000201:enzymology
D010743:Phospholipids; D008995:Monoamine Oxidase; D009251:NADPH-Ferrihemoprotein Reductase; D000217:Acyltransferases; D005992:Glycerol-3-Phosphate O-Acyltransferase; D010740:Phospholipases; D010744:Phosphoric Monoester Hydrolases