In vivo biosynthesis of ceruloplasmin (Cp), a copper-containing glycoprotein, which plays an important role in copper transfer between organs and bidirectional iron transport in vertebrates, was studied in 7-day old rats, which are characterized by the embryonic type of copper metabolism. In addition to the liver, Cp is synthesized in the lungs, brain, and kidneys. In “pulse-chase” experiments it was demonstrated that [14C]-Cp appearance in the blood coincides with the secretion ofde novo synthesized Cp from the liver. [14C]-Cp is taken up from the blood stream by cells of the heart, lung, and kidneys and binds to red blood cells, while Cp polypeptide chain is not taken up by the brain cells. Immunoreactive polypeptides of the Cp receptor were found using immunoblotting in plasma membranes of the heart, liver, kidneys, and red blood cells, rather than in the brain. Using the RT-PCR method with selective primers, it was shown that these cells contain molecular forms of Cp-mRNAs programming the synthesis of both secretory Cp and Cp bound to the plasma membrane via a glycosyl phosphatidylinositol anchor. After switching to the adult type of copper metabolism, the blood serum contents of copper and Cp sharply increase, while the Cp content in the cerebrospinal fluid, as measured according to the oxidase and antigen activities, and copper concentration, as determined by atomic absorption spectroscopy, remain low. Ontogenetic features of the system ensuring the copper homeostasis in mammals are discussed.
Russian Journal of Developmental Biology – Springer Journals
Published: Oct 18, 2004
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