Transferrin protein and iron uptake by cultured hepatocytes
Jean‐Claude Sibille, Jean‐Noël Octave, Yves‐Jacques Schneider, André Trouet, Robert R. Crichton
Abstract
Jean‐Claude Sibille, Jean‐Noël Octave, Yves‐Jacques Schneider, André Trouet, Robert R. Crichton
Abstract
The binding and uptake of 59Fe-loaded 3H-labelled rat transferrin by cultured rat hepatocytes was investigated. At 4 degrees C, there is no evidence for a specific binding of transferrin which could be related to the association of neo-synthesized transferrin with plasma membrane receptors. At 37 degrees C, iron uptake is much more important than transferrin uptake; it proceeds linearly over the time of incubation, is largely proportional to the extracellular transferrin concentration, and is compatible with uptake by fluid phase endocytosis. The difference observed between iron and transferrin uptake implies the existence of a mechanism allowing the reutilization of transferrin after iron delivery.
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The binding and uptake of 59Fe-loaded 3H-labelled rat transferrin by cultured rat hepatocytes was investigated. At 4 degrees C, there is no evidence for a specific binding of transferrin which could be related to the association of neo-synthesized transferrin with plasma membrane receptors. At 37 degrees C, iron uptake is much more important than transferrin uptake; it proceeds linearly over the time of incubation, is largely proportional to the extracellular transferrin concentration, and is compatible with uptake by fluid phase endocytosis. The difference observed between iron and transferrin uptake implies the existence of a mechanism allowing the reutilization of transferrin after iron delivery.
Key concepts: Transferrin, Endocytosis, Transferrin receptor, Extracellular, Chemistry, Incubation, Biochemistry, Receptor