A late developmental change in lysosomal enzyme sulfation specific to newly synthesized proteins in Dictyostelium discoideum |
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| Authors: | G P Livi N A Woychik R L Dimond |
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| Institution: | 1. Department of Medicine, University of Texas Health San Antonio, San Antonio, TX 78229, USA;2. Center for Mitochondrial Medicine, University of Texas Health San Antonio, San Antonio, TX 78229, USA;3. Institute for Regenerative Medicine, University of Pennsylvania, Philadelphia, PA 19104, USA;4. Department of Medicine, College of Physicians and Surgeons of Columbia University, 650 W 168 Street, New York, NY 10032, USA;5. Section of Human Biochemical Genetics, Medical Genetics Branch, National Human Genome Research Institute, National Institutes of Health, Bethesda, MD 20892, USA;6. NIH Undiagnosed Diseases Program, Office of the Clinical Director, National Human Genome Research Institute, and the Common Fund, National Institutes of Health, Bethesda, MD 20892, USA;7. Department of Physiology and Pharmacology, Western University, London, ON N6A 5C1, Canada;1. Department of Biological Science, USA;2. Center for Applied Biotechnology Studies, California State University Fullerton, CA, 92831, USA;1. Glycometabolic Biochemistry Laboratory, RIKEN-Cluster for Pioneering Research, Wako, Saitama, Japan;2. Bioscience and Biotechnology Center, Nagoya University, Chikusa, Nagoya, Japan;3. Institute for Glyco-core Research (iGCORE), Nagoya University, Chikusa, Nagoya, Japan;4. Discovery Concept Validation Function, KAN Research Institute, Inc, Kobe, Japan;5. Department of Clinical Laboratory Sciences, School of Health Sciences, Fukushima Medical University, Fukushima, Japan;6. Analytical & Measuring Instruments Division, Shimadzu Corporation, Kyoto, Japan |
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| Abstract: | During development in Dictyostelium discoideum, several lysosomal glycosidases undergo changes in post-translational modification that are thought to involve differences in the extent of sulfation or phosphorylation, and appear to be required for the maintenance of cellular enzyme activity late in development. We have used monoclonal antibodies specific to the lysosomal enzyme alpha-mannosidase-1 to study the major late (12 hr) developmental change in the modification system. Pulse-chase experiments performed both early and late in development reveal that the substrate for the late form of modification is restricted to newly synthesized alpha-mannosidase-1 precursor protein. We have identified one modification difference between the two developmentally distinct isozymes of alpha-mannosidase-1: 35SO4 pulse-chase data show that the newly synthesized "late" enzyme precursor is significantly undersulfated in comparison with the enzyme synthesized early in development. This apparent lack of sulfation is associated with the lack of acquisition of endoglycosidase H resistance. By contrast, an aggregation-deficient mutant, which is defective with regard to the accumulation of alpha-mannosidase-1 activity late in development, synthesizes the "early" sulfated form of the enzyme throughout development. We conclude that the late developmental change in post-translational modification specifically involves one of the biochemical steps in which the N-linked oligosaccharide side chains of the newly synthesized alpha-mannosidase-1 precursor are modified by sulfation. |
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