Ceruloplasmin Anticuerpos

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Ceruloplasmin (CP) is a blue plasma glycoprotein that is synthesized in hepatocytes and transports copper throughout the body. Also known as ferroxidase, ceruloplasmin is the product of an intragenic triplication and is composed of three homologous domains. Two splice variants, CP-1 and CP-2, have differential expression in specific tissues. Ceruloplasmin mRNAs are expressed in human liver, macrophages and lymphocytes. Ceruloplasmin binds copper and has six or seven cupric ions per molecule. It is involved in peroxidation of Fe(II) transferrin to form Fe(III) transferrin. Ceruloplasmin is proteolytically degraded to a short form, which still possesses ferroxidase activity. However, only the intact long form is able to catalyze iron loading into ferritin, indicating that the structural integrity of ceruloplasmin is essential for the enzyme to effectively catalyze iron loading into ferritin. Ceruloplasmin also induces low density lipoprotein oxidation in vitro, an action that depends on the presence of a single, chelatable Cu atom. A glycosyl phosphatidylinositol (GPI)-anchored form of ceruloplasmin is expressed by Sertoli cells, which may be the dominant form in Sertoli cells.