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J Biol Chem, Vol. 273, Issue 29, 18015-18018, July 17, 1998

COMMUNICATION
Characterization of the Human Analogue of a Scrapie-responsive Gene

Michel DronDagger , Françoise Dandoy-DronDagger , Frédéric GuilloDagger , Louisa BenboudjemaDagger , Jean-Jacques Hauw, Pierre Lebonparallel , Dominique Dormont**, and Michael G. ToveyDagger

From the Dagger  Laboratory of Viral Oncology CNRS UPR 9045, IFC1, 94801 Villejuif cedex, France, the  Laboratoire de Neuropathologie Raymond Escourolle, Groupe Hospitalier Pitié-Salpêtrière, INSERM U360, Association Claude Bernard, 75651 Paris cedex 13, France, the parallel  Laboratoire de Virologie, Hôpital Saint Vincent de Paul, 75674 Paris cedex 14, France, and the ** Laboratoire de Neurovirologie CEA, 92265 Fontenay aux Roses cedex, France

We have recently described a novel mRNA denominated ScRG-1, the level of which is increased in the brains of Scrapie-infected mice (Dandoy-Dron, F., Guillo, F., Benboudjema, L., Deslys, J.-P., Lasmézas, C., Dormont, D., Tovey, M. G., and Dron, M. (1998) J. Biol. Chem. 273, 7691-7697). The increase in ScRG-1 mRNA in the brain follows the accumulation of PrPSc, the proteinase K-resistant form of the prion protein (PrP), and precedes the widespread neuronal death that occurs in late stage disease. In the present study, we have isolated a cDNA encoding the human counterpart of ScRG-1. Comparison of the human and mouse transcripts firmly established that both sequences encode a highly conserved protein of 98 amino acids that contains a signal peptide, suggesting that the protein may be secreted. Examination of the distribution of human ScRG-1 mRNA in adult and fetal tissues revealed that the gene was expressed primarily in the central nervous system as a 0.7-kilobase message and was under strict developmental control.


Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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