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The Journal of Neuroscience, November 1, 1998, 18(21):8682-8691

Purification from Bovine Serum of a Survival-Promoting Factor for Cultured Central Neurons and Its Identification as Selenoprotein-P

Jun Yan and John N. Barrett

Department of Physiology and Biophysics, University of Miami School of Medicine, Miami, Florida 33101

We purified from bovine serum a glycoprotein that promotes the survival of rat embryonic neurons cultured from septum and other brain regions. A 40,000-fold purification was achieved by using a combination of ammonium sulfate precipitation, Zn²⁺ affinity chromatography, Cibacron blue 3-GA dye affinity chromatography, ABx ion exchange chromatography, and preparative PAGE. The active protein had an apparent molecular weight of 50-60 kDa. The concentration required for half-maximal survival (EC₅₀) was 12 ng/ml (~200 pM) for the final fraction. Amino acid sequencing after cyanogen bromide cleavage yielded two sequences that are homologous to regions of deduced sequence of the selenoprotein-P (SPP) family in bovine, rat, and human. Antibodies against a synthetic peptide within the bovine SPP sequence immunoprecipitated and inhibited the survival-promoting activity of a partially purified serum fraction. The purified protein supported neuronal survival more effectively than inorganic selenium. These results suggest that SPP or an SPP-like protein contributes to the neuronal survival-promoting activity of serum.

Key words: central neurons; neuronal survival; selenium; selenoprotein-P; serum; neurotrophic factor

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Copyright © 1998 Society for Neuroscience  0270-6474/98/18218682-10$05.00/0

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