ceruloplasiiniin

Ceruloplasmin is a blue-colored glycoprotein found in the blood plasma of vertebrates, including humans. It belongs to the multicopper oxidase family of enzymes and plays a crucial role in iron metabolism and antioxidant defense. The protein was first identified in 1946 by Swedish biochemist Carl-Axel Brink and was named for its characteristic blue color, derived from the copper ions it contains.

Ceruloplasmin constitutes approximately 90% of the copper in human plasma, with a typical concentration ranging from 20 to 40 mg/dL. It functions primarily as a ferroxidase, oxidizing ferrous iron (Fe²⁺) to ferric iron (Fe³⁺), which is essential for iron transport via transferrin. This process prevents the formation of free radicals that could damage cells. Additionally, ceruloplasmin contributes to oxidative stress regulation by catalyzing the oxidation of other substrates, such as amines and phenols.

Genetic mutations affecting ceruloplasmin can lead to Wilson’s disease, a rare autosomal recessive disorder characterized by excessive copper accumulation in tissues. In Wilson’s disease, ceruloplasmin levels are typically low or absent, impairing copper metabolism. Conversely, elevated ceruloplasmin levels may be observed in conditions such as inflammation, infection, or certain cancers.

Ceruloplasmin is synthesized primarily in the liver and is secreted into the bloodstream. Its structure includes six copper-binding sites, with five involved in electron transfer and one serving as a structural component. The protein’s copper content is tightly regulated, reflecting its importance in maintaining systemic copper homeostasis.

While ceruloplasmin’s exact physiological roles extend beyond iron metabolism, ongoing research continues to explore its potential involvement in immune function, angiogenesis, and other biological processes. Its diagnostic utility in monitoring copper-related disorders and inflammatory states remains well-established in clinical practice.