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  • 1
    Electronic Resource
    Electronic Resource
    Inactivation of chitin synthase in Saccharomyces cerevisiae (1974)
    Springer
    Archives of microbiology 101 (1974), S. 295-301 
    Details
    ISSN: 1432-072X
    Keywords: Chitin Synthase ; Proteinase B ; Saccharomyces cerevisiae ; Morphogenesis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The activity of chitin synthase extracted from whole cells of Saccharomyces cerevisiae shows reproducible changes during the course of batch cultivation. During exponential growth 5–10% of the enzyme occurs in the active form, whereas in the stationary phase no active enzyme can be detected. Of three yeast proteinases, A, B and C, only B is able to activate pre-chitin synthase and inactivate chitin synthase. A new model of the regulation is presented which accounts for the specific location as well as for termination of chitin synthesis during the budding cycle.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00455946
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  • 2
    Electronic Resource
    Electronic Resource
    Theearly andlate processing of lysosomal enzymes: Proteolysis and compartmentation (1992)
    Springer
    Cellular and molecular life sciences 48 (1992), S. 130-151 
    Details
    ISSN: 1420-9071
    Keywords: Lysosomes ; lysosomal enzymes ; maturation ; proteinases ; proteolysis ; secretion
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract Lysosomal enzymes are subjected to a number of modifications including carbohydrate restructuring and proteolytic maturation. Some of these reactions support lysosomal targeting, others are necessary for activation or keeping the enzyme inactive before being segregated, while still others may be adventitious. The non-segregated fraction of the enzyme is secreted and can be isolated from the medium. It is considered that the secreted lysosomal enzymes fulfill certain physiological and pathophysiological roles. By comparing the secreted and the intracellular enzymes it is possible to distinguish between the reactions that occur before and after the segregation. In this review the reactions that may influence the segregation are referred to as the early processing and those characteristic for the enzymes isolated from lysosomal compartments as the late processing. The early processing is characterized mainly by modifications of carbohydrate side chains. In the late processing, proteolytic fragmentation represents the most conspicuous changes. The review focuses on the compartmentation of the reactions and the proteolytic fragmentation of lysosomal enzyme precursors. While a plethora of proteolytic reactions are involved, our knowledge of the proteinases responsible for the particular maturation reactions remains very limited. The review points also to work with cells from patients affected with lysosomal storage disorders, which contributed to our understanding of the lysosomal apparatus.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01923507
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  • 3
    Electronic Resource
    Electronic Resource
    Human and hamster procathepsin D, although equally tagged with mannose-6-phosphate, are differentially targeted to lysosomes in transfected BHK cells (1998)
    Springer
    Cell & tissue research 292 (1998), S. 303-310 
    Details
    ISSN: 1432-0878
    Keywords: Key words Procathepsin D ; Lysosomes ; Endocytosis ; Baby hamster kidney (BHK) cells
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract  BHK cells transfected with human cathepsin D (CD) cDNA normally segregate the autologous hamster cathepsin D while secreting a large proportion of the human proenzyme. In the present work, we have utilized these transfectants to examine to what extent the mannose-6-phosphate-dependent pathway for lysosomal enzyme segregation contributes to the differential sorting of human and hamster CD. We report that, in recipient control BHK cells, the rate of mannose-6-phosphate-dependent endocytosis of human procathepsin D secreted by transfected BHK cells is lower than that of hamster procathepsin D and much lower than that of human arylsulphatase A. The missorted human enzyme bears phosphorylated oligosaccharides and most of its phosphate residues are “uncovered”, like the autologous enzyme. Thus, despite both the Golgi-associated modifications of oligosaccharides, i.e. the phosphorylation of mannose and the uncovering of mannose-6-phosphate residues, which proceed on human and hamster procathepsin D with comparable efficiency, only the latter is accurately packaged into lysosomes. Ammonium chloride partially affects the lysosomal targeting of cathepsin D in control BHK cells, whereas in transfected cells, this drug strongly inhibits the maturation of human procathepsin D and slightly enhances its secretion. These data indicate that: (1) over-expression of a lysosomal protein does not saturate the Golgi-associated reactions leading to the synthesis of mannose-6-phosphate; (2) a portion of cathepsin D is targeted independently of mannose-6-phosphate receptors in the transfected BHK cells; and (3) whichever mechanism for lysosomal delivery of autologous procathepsin D is involved, this is not saturated by the high rate of expression of human cathepsin D.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s004410051061
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