By John B. Lloyd (auth.), John B. Lloyd, Robert W. Mason (eds.)
From a preview of a prior volume:
`The heterogeneity of topics...is very bold, and the result's, total, profitable end result of the prime quality of the person contributions...highly recommended.'
`Well written and timely...of curiosity to all these taken with the examine of this organelle and for these drawn to the clinical and genetic facets of lysosomal disorders...recommended.'
Journal of clinical Genetics
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Extra info for Biology of the Lysosome
The cellular localization of the oligosaccharide sulfotransferase and the possible role of sulfate groups in hydrolase sorting have not been investigated. A key step in targeting of newly synthesized soluble hydrolases to the lysosome is the formation of phosphomannosyl residues on high-mannose oligosaccharides. The initial transfer of GlcNac-l-phosphate to mannose, forming al,6-linked branches of the carbohydrate chains, may occur in the intermediate compartment (Hauri and Schweizer, 1992). A second phosphorylation can occur on mannoses, forming al,3-linked branches, after the removal of terminal mannose residues by an a-mannosidase in the cis-Golgi.
Although phosphorylation of arylsulfatase B in vitro causes changes in the enzyme activity toward an artificial substrate, it remains to be determined whether protein phosphorylation of lysosomal enzymes is a common modification and related to enzymatic regulation in vivo. , 1995a). The cysteine residue is converted into a 2-amino-3-oxopropionic acid residue that is required to generate catalytically active sulfatases, and this modification is lacking in arylsulfatase A and B from cells of patients with multiple sulfatase deficiency.
1992). , 1992). , 1990). 1 and Chapter 3 of this volume). For the two MPRs it has been demonstrated that deletion of the carboxyterminal four or five amino acids of the cytoplasmic domains containing dileucine motifs leads to a decrease in sorting efficiency of lysosomal enzymes (Johnson and Kornfeld, 1992a,b). Since the recycling of these mutant receptors from the plasma membrane to the Golgi was unaffected, the authors suggested that additional signals for efficient sorting may overlap with the internalization sequences.