β‐Galactosidase‐neuraminidase deficiency. Deficiency of a freeze‐labile neuraminidase in leukocytes and fibroblasts

Sakuraba, Hitoshi; Suzuki, Yuzuru; Fukuoka, Ken; Hayashi, Keijiro

doi:10.1007/bf01799996

Cited by 5 publications

(4 citation statements)

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“…affinities, pH optima, and other biochemical properties to be differentially associated with soluble and insoluble cell fractions or with specific membranes and cell organelles (e.g., Alhadeff and Wolfe, 1981;Zeigler and Bach, 1981;Ben Yoseph et al, 1982;McNamara et al, 1982;Yamada et al, 1983;Miyagi and Tsuiki, 1984;Chigorno et al, 1986; reviews given by Tettamanti et al, 1981) and to be differentially abundant in different cell types (Pallman and Sandhoff, 1980;Sakuraba et al, 1982;Suzuki et al, 1982;Tsuji et al, 1982;Verheijen et al, 1983). The NEU-1 and NEU-2 isozymes examined in the present study appear to correspond, respectively, with the particulate (primarily lysosomal) and soluble (cytosolie) fractions of rat liver neuraminidase activities originally described by Tulsiani and Carubelli (1970).…”

Section: Discussionmentioning

confidence: 98%

Biochemical characteristics and subcellular localizations of rat liver neuraminidase isozymes: A paradox resolved

1990

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A striking discrepancy in the abilities of two analytical approaches (fluorometric and electrophoretic) to detect the effect of a gene, Neu-2, on rat liver neuraminidase phenotypes led us to examine the biochemical and physical properties of the liver isozymes NEU-1 and NEU-2 that might be responsible for this difference. Cell fractionation via Percoll gradient centrifugation revealed NEU-1 activity almost exclusively in the lysosomal cell fraction, while NEU-2 was strictly cytosolic in distribution. The two isozymes were also found to differ in pH activity curves and optima (optima: 4.6-4.8 and 5.4-5.8 for NEU-1 and NEU-2, respectively) and in solubility characteristics (NEU-2 highly soluble; NEU-1 relatively insoluble but solubilized by freezing/thawing). Both isozymes were found to be freeze-thaw stable in crude, whole-cell extracts, but NEU-1 was destabilized in the enriched (partially purified) lysosomal subcellular fraction. Consideration of these properties relative to those described previously for unidentified cytosolic and membrane bound (lysosomal) rat liver neuraminidases (Tulsiani, D. R. P., and Carubelli, R., J. Biol. Chem. 245:1821, 1970) leads us to believe that NEU-2 also is destabilized by partial purification and that NEU-1 and NEU-2 have very different relative abundances within the cell. The biochemical and physical differences between NEU-1 and NEU-2 can account for the discrepant abilities of the fluorometric and electrophoretic approaches to detect the effects of Neu-2. Ways to increase the sensitivity of the fluorometric approach for quantitative assays of specific NEU-1 and NEU-2 activity are discussed.

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Section: Discussionmentioning

confidence: 98%

Biochemical characteristics and subcellular localizations of rat liver neuraminidase isozymes: A paradox resolved

1990

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“…Leupeptin protects ß-galactosidase against proteolysis at the position 82 residues upstream of the C-terminal. In fact, it restores ß-galactosidase activity in galactosialidosis fibroblasts [3,5,6,24,32]. This restoration is also observed in the presence of protective protein.…”

Section: Discussionmentioning

confidence: 99%

“…The level of intracellular β‐galactosidase activity is therefore regulated by lysosomal proteases responsible for maturation of the precursor and for ultimate degradation. Details of this molecular regulation are not known at present, but our previous studies indicated that two different proteases were suggested to be involved in processing of the enzyme: one inhibited by leupeptin and the other not inhibited by leupeptin [5, 6].…”

Section: Introductionmentioning

confidence: 99%

“…The level of intracellular ß-galactosidase activity is therefore regulated by lysosomal proteases responsible for maturation of the precursor and for ultimate degradation. Abbreviations: CA074, A'-(l,3-transpropylcarbamoyloxirane-2-carbonyl)-1 -isoleucyl-1 -proline; CA074Me, N-( 1,3-transpropylcarbamoyloxirane-2-carbonyl)-l-isoleucyl-l-proline methyl ester; E64-c, L-3carboxy-2,3-trans-epoxypropionyl-leucylamide-(3-methyl)butane; E64-d, {JV-[-(L-3-trans-ethoxycarbonyloxirane-2-carbonyl-L-leucyl]-3methyl-butylamine}; 4MU, 4-methylumbelliferone; Z-Arg-Arg-AMC, carboxybenzoyl-L-argininyl-L-arginine 4-methyl-coumaryl-7amide; CHO, Chinese hamster ovary; M6P, mannose 6-phosphate; MPR, mannose 6-phosphate receptor; DMSO, dimethyl sulfoxide this molecular regulation are not known at present, but our previous studies indicated that two different proteases were suggested to be involved in processing of the enzyme: one inhibited by leupeptin and the other not inhibited by leupeptin [5,6].…”

Section: Introductionmentioning

confidence: 99%

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Maturation and degradation of β‐galactosidase in the post‐Golgi compartment are regulated by cathepsin B and a non‐cysteine protease

et al. 1997

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Lysosomal ß-galactosidase precursor is processed to a mature form and associated with protective protein in lysosomes. In this study we used two cysteine protease proinhibitors, E64-d for cathepsins B, S, H, and L, and CA074Me for cathepsin B. They are converted intracellularly to active forms, E-64c and CA074, respectively. Both active compounds inhibited maturation of the exogenous ß-galactosidase precursor, but E-64c did not inhibit further degradation to an inactive 50-kDa product. We concluded that cathepsin B participated exclusively in maturation of ß-galactosidase, and a non-cysteine protease was involved in further degradation and inactivation of the enzyme molecule.

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Biochemical study of sialidosis type I in a Russian family

Tsvetkova¹,

Петушкова²,

Zolotuchina³

et al. 1986

J of Inher Metab Disea

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A 7-year-old boy from a Russian family with decreased vision and a cherry-red spot but without any somatic and mental abnormalities is described in this paper. The decreased neuraminidase activity in the child's leukocytes and cultured skin fibroblasts and his 10-fold increase in urinary sialyloligosaccharides allowed us to conclude that he was affected by type I sialidosis. Some other results of the biochemical study of this child and his parents are presented. It is the first case of sialidosis in the Russian population.

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β‐Galactosidase‐neuraminidase deficiency. Deficiency of a freeze‐labile neuraminidase in leukocytes and fibroblasts

Cited by 5 publications

References 1 publication

Biochemical characteristics and subcellular localizations of rat liver neuraminidase isozymes: A paradox resolved

Biochemical characteristics and subcellular localizations of rat liver neuraminidase isozymes: A paradox resolved

Maturation and degradation of β‐galactosidase in the post‐Golgi compartment are regulated by cathepsin B and a non‐cysteine protease

Biochemical study of sialidosis type I in a Russian family

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