Abstract

Using the method of ATP luminometry it is shown that crude membrane preparations from human and rat hepatocytes accumulate ATP 20–100 nmol/mg protein during a 1-min incubation under conditions of oxidative phosphorylation. Application of appropriate inhibitors shows that a possible contamination of the membrane preparations with mitochondria does not contribute to this ATP accumulation. Phosphatidylcholine, tumor necrosis factor, and cell proliferation factor markedly stimulate the accumulation of ATP by plasma membraneenriched particles isolated from rat and human liver. The hepatocyte plasma membrane is shown to be able to synthesize ATP from inorganic phosphate and ADP using the aerobic mechanism. ATP in the plasma membrane is assumed to participate in the transmembrane signal transduction from growth factors to the cell effector systems.

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