THE HUMAN GLUCOCEREBROSIDASE GENE HAS 2 FUNCTIONAL ATG INITIATOR CODONS
- 1 December 1987
- journal article
- research article
- Vol. 41 (6) , 1016-1024
Abstract
Gaucher disease is due to a deficiency in the activity of the enzyme glucocerebrosidase. Glucocerebrosidase is a lysosomal enzyme that presumably requires a signal peptide for transport across the membrane of the rough endoplasmic reticulum and glycosylation for transport into lysosomes. Human glucocerebrosidase cDNA contains two potential ATG start codons in its long open reading frame. The signal peptides that are initiated from each ATG are quite different in their hydrophobicity. We demonstrate that either ATG can function independently to produce active glucocerebrosidase enzyme in cultured fibroblasts. The glucocerebrosidase activity produced from translation products initiated at either ATG is found predominantly in the lysosomes.This publication has 16 references indexed in Scilit:
- Gaucher Disease: Retrovirus-mediated Correction of the Enzymatic Defect in Cultured CellsCold Spring Harbor Symposia on Quantitative Biology, 1986
- Trafficking of lysosomal enzymes in normal and disease states.Journal of Clinical Investigation, 1986
- Molecular cloning and nucleotide sequence of human glucocerebrosidase cDNA.Proceedings of the National Academy of Sciences, 1985
- Amphotropic retrovirus vector system for human cell gene transfer.Molecular and Cellular Biology, 1984
- SYNTHESIS AND USE OF SYNTHETIC OLIGONUCLEOTIDESAnnual Review of Biochemistry, 1984
- Initiation of translation at internal AUG codons in mammalian cellsNature, 1984
- Compilation and analysis of sequences upstream from the translational start site in eukaryotic mRNAsNucleic Acids Research, 1984
- A simple method for displaying the hydropathic character of a proteinJournal of Molecular Biology, 1982
- LEUKOCYTE BETA-GLUCOSIDASE IN HOMOZYGOTES AND HETEROZYGOTES FOR GAUCHER DISEASE1980
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970