Two genetically different MU-NANA neuraminidases in human leucocytes

Verheijen, Frans W.; Janse, H.C.; Diggelen, O. P. van; Bakker, H. D.; Loonen, M. C. B.; Durand, P.; Galjaard, H.

doi:10.1016/0006-291x(83)91224-x

Cited by 35 publications

(24 citation statements)

References 21 publications

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“…These findings also raise the possibility that the sialidase activity recovered from neutrophils may be derived from multiple enzyme species that occupy distinct functional compartments. Although our studies did not reveal clear differences in the biochemical characteristics ofsialidase activities recovered from different subcellular compartments, they did not rule out this possibility; indeed, others have reported that neutrophils contain at least two distinct isoforms of sialidase (16). Sialidase activity was also found to appear rapidly on the surface ofintact neutrophils during activation, coincident with a loss oftotal cell-associated sialic acid and release ofsialic acid into the extracellular medium, and with kinetics that differed depending on the stimulus employed.…”

Section: Discussioncontrasting

confidence: 87%

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Mobilization of sialidase from intracellular stores to the surface of human neutrophils and its role in stimulated adhesion responses of these cells.

Cross¹,

Wright²

1991

J. Clin. Invest.

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Desialation of cell surfaces has been associated with the initiation or modification of diverse cellular functions. In these studies we have examined the subcellular distribution of sialidase (SE) in human neutrophils as well as the mobilization of this enzyme following neutrophil activation. Separation of subcellular fractions by density gradient centrifugation showed that SE is present not only in neutrophil primary and secondary granule populations, like lysozyme, but also in plasma membrane fractions. Neutrophil activation was associated with a redistribution of SE from secondary granule-enriched fractions to the plasma membrane. Furthermore, SE activity detected on the surface of intact neutrophils with a fluorescent SE substrate increased rapidly after activation with kinetics that matched both the loss of total cell-associated sialic acid and release of free sialic acid from the cells. These activation-dependent events were in each case blocked by incubation of neutrophils with the SE inhibitor, 2-deoxy-N-acetyl-neuraminic acid. Aggregation responses of neutrophils as well as adhesion responses to nylon and plastic surfaces were also inhibited by 2-deoxyNANA. Our findings indicate that the activation-dependent desialation of the neutrophil surface is associated with mobilization of an endogenous SE to the plasma membrane and has a role in stimulated adhesion responses of these cells. (J.

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Section: Discussioncontrasting

confidence: 87%

“…Human neutrophils have been shown by several laboratories to contain sialidase activity (15,16). Moreover, studies of the appearance of sialidase activity during induced maturation of the myeloid leukemia cell line, HL60, have suggested that neutrophil sialidase is acquired during the latter phases of neutrophilic maturation (15).…”

Section: Introductionmentioning

confidence: 99%

Mobilization of sialidase from intracellular stores to the surface of human neutrophils and its role in stimulated adhesion responses of these cells.

Cross¹,

Wright²

1991

J. Clin. Invest.

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“…Sialidase is targeted to the endosomal-lysosomal compartment as an integral membrane protein by vesicular transport, which involves association of the adapter proteins with a tyrosine-containing internalization signal at the C-terminus of the enzyme [Lukong et al, 2001]. It is likely that the transmembrane domain in the lysosome is cleaved similarly to that of acid phosphatase, resulting in the appearance in the cell of two pools of lysosomal sialidase, soluble and membraneassociated, which are both absent in cultured cells of sialidosis patients [Verheijen et al, 1983;Miyagi et al, 1990Miyagi et al, , 1992Miyagi et al, , 1993. Immunoelectron microscopy demonstrated that, in addition to the lysosomal membrane and lysosomal lumen, NEU1 sialidase is present on the plasma membrane and in intracellular (possibly endocytic) vesicles [Vinogradova et al, 1998].…”

Section: Introductionmentioning

confidence: 99%

Molecular pathology of NEU1 gene in sialidosis

Poupětová²,

et al. 2003

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Communicated by Mark H. PaalmanLysosomal sialidase (EC 3.2.1.18) has a dual physiological function; it participates in intralysosomal catabolism of sialylated glycoconjugates and is involved in cellular immune response. Mutations in the sialidase gene NEU1, located on chromosome 6p21.3, result in autosomal recessive disorder, sialidosis, which is characterized by the progressive lysosomal storage of sialylated glycopeptides and oligosaccharides. Sialidosis type I is a milder, late-onset, normosomatic form of the disorder. Type I patients develop visual defects, myoclonus syndrome, cherry-red macular spots, ataxia, hyperreflexia, and seizures. The severe early-onset form, sialidosis type II, is also associated with dysostosis multiplex, Hurler-like phenotype, mental retardation, and hepatosplenomegaly. We summarize information on the 34 unique mutations determined so far in the sialidase gene, including four novel missense and one novel nonsense mutations found in two Czech and two French sialidosis patients. The analysis of sialidase mutations in sialidosis revealed considerable molecular heterogeneity, reflecting the diversity of clinical phenotypes that make molecular diagnosis difficult. The majority of sialidosis patients have had missense mutations, many of which have been expressed; their effects on activity, stability, intracellular localization, and supramolecular organization of sialidase were studied. A structural model of sialidase allowed us to localize mutations in the sialidase molecule and to predict their impact on the tertiary structure and biochemical properties of the enzyme. Hum Mutat 22:343-352,

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“…Substrates of lysosomal and membrane-bound sialidases such as ganglioside (11,12) and glycoprotein (13) have been shown to be responsible for tissue-specific and cellular physiological properties such as adhesion (14), development (15) and proliferation (16). Genetic diseases of sialidosis, galactosialidosis and sialolipidosis (17) are caused by lysosomal and ganglioside-specific sialidase genes, but the disease caused by cytosolic sialidase gene is not known. Though cytosolic sialidase hydrolyzes the sialylated compounds in the cytosol or on intracellular membranes, the physiological function, isomer and expressional mechanism are still not clear (5).…”

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confidence: 99%