Fucosidosis

Durand, P.; Borrone, C; Cella, G. Della

doi:10.1016/s0022-3476(69)80464-6

Cited by 191 publications

(45 citation statements)

References 23 publications

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“…As the word "mucolipidosis" does not correspond to any accepted term of nomenclature for glycoconjugates, we propose to call these three types of oligosaccharidosis "sialidosis", in regard to the nature of enzymatic defect and accumulated material as was done for mannosidosis [22] and fucosidosis [23].…”

Section: Discussionmentioning

confidence: 99%

Structure of Nine Sialyl-Oligosaccharides Accumulated in Urine of Eleven Patients with Three Different Types of Sialidosis. Mucolipidosis II and Two New Types of Mucolipidosis

et al. 1977

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Urines of 11 patients with three different types of mucolipidosis characterized by a total or partial sialidase deficiency, were studied. In all cases, we found an important accumulation of sialyl‐oligosaccharides. The structure of 9 of them has been determined: α‐AcNeu‐(2→3)‐β‐Gal‐(1→4)‐β‐GlcNAc‐(1→2)‐α‐Man‐(1→3)‐β‐Man‐(1→4)‐GlcNAc, α‐AcNeu‐(2→6)‐β‐Gal‐(1→4)‐β‐GlcNAc‐(1→2)‐α‐Man‐(1→3)‐β‐Man‐(1→4)‐GlcNAc, α‐AcNeu‐(2→6)‐β‐Gal‐(1→4)‐β‐GlcNAc‐(1→2)‐α‐Man‐(1→3)[α‐Man‐(1→6)]β‐Man‐(1→4)‐GlcNAc, α‐AcNeu‐(2→3)‐β‐Gal‐(1→4)‐β‐GlcNAc‐(1→2)‐α‐Man‐(1→3)[β‐Gal‐(1→4)‐β‐GlcNAc‐(1→2)‐α‐Man‐(1→6)]β‐Man‐(1→4)‐GlcNAc, α‐AcNeu‐(2→6)‐β‐Gal‐(1→4)‐β‐GlcNAc‐(1→2)‐α‐Man‐(1→3)[β‐Gal‐(1→4)‐β‐GlcNAc‐(1→2)‐α‐Man‐(1→6)]β‐Man‐(1→4)‐GlcNAc, α‐AcNeu‐(2→6)‐β‐Gal‐(1→4)‐β‐GlcNAc‐(1→2)[α‐AcNeu‐(2→3)‐β‐Gal‐(1→4)‐β‐GlcNAc‐(1→4)]α‐Man‐(1→3)‐β‐Man‐(1→4)‐GlcNAc, α‐AcNeu‐(2→3)‐β‐Gal‐(1→4)‐β‐GlcNAc‐(1→2)‐α‐Man‐(1→3)[α‐AcNeu‐(2→3)‐β‐Gal‐(1→4)‐β‐GlcNAc‐(1→2)‐α‐Man‐(1→6)]β‐Man‐(1→4)‐GlcNAc, α‐AcNeu‐(2→6)‐β‐Gal‐(1→4)‐β‐GlcNAc‐(1→2)‐α‐Man‐(1→3)[α‐AcNeu‐(2→3)‐β‐Gal‐(1→4)‐β‐GlcNAc‐(1→2)‐α‐Man‐(1→6)]β‐Man‐(1→4)‐GlcNAc, α‐AcNeu‐(2→6)‐β‐Gal‐(1→4)‐β‐GlcNAc‐(1→2)‐α‐Man‐(1→3)[α‐AcNeu‐(2→6)‐β‐Gal‐(1→4)‐β‐GlcNAc‐(1→2)‐α‐Man‐(1→6)]β‐Man‐(1→4)‐GlcNAc. All these compounds are products of incomplete catabolism of glycoproteins and result from the action of a new type of β‐endo‐N‐acetylglucosaminidase able to act on sialylated glycoproteins or glycopeptides. The term sialidosis is proposed for these three types of oligosaccharidosis.

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Section: Discussionmentioning

confidence: 99%

Structure of Nine Sialyl-Oligosaccharides Accumulated in Urine of Eleven Patients with Three Different Types of Sialidosis. Mucolipidosis II and Two New Types of Mucolipidosis

et al. 1977

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“…The occurrence of fucosidosis in Cuba is about 0.63 per 100,000 live births (Menéndez-Sainz et al, 2012). The disease is caused by a deficiency of a-L-fucosidase (EC 3.2.1.51) activity leading to the accumulation of fucose-containing glycolipids and glycoproteins in multiple tissues (Van Hoof and Hers, 1968;Durand et al, 1969). Its clinical phenotypes include progressive neurological deterioration, coarse facial features, hearing loss, growth retardation, visceromegaly, dysostosis multiplex, angiokeratoma corporis diffusum, recurrent infections, and seizures (Willems et al, 1991).…”

Section: Introductionmentioning

confidence: 99%

Novel mutations in the FUCA1 gene that cause fucosidosis

Panmontha¹,

Amarinthnukrowh²,

Damrongphol³

et al. 2016

Genet. Mol. Res.

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“…A number of isomers of the enzyme have been identified in human tissues, including two hepatic forms (Robinson & Thorpe, 1973). The clinical importance of AFU is indicated by the occurrence, albeit rare, of a deficiency state that results in a neurovisceral storage disease known as fucosidosis (Durand et al, 1969), and by the observation that women with low serum activity of the enzyme may be prone to ovarian carcinoma (Lynch et al, 1985). Raised serum concentrations of AFU have been described in patients with a variety of benign diseases, including diabetes, hyperthyroidism, toxic oil syndrome and, of particular relevance to the present study, cirrhosis, alcoholic hepatitis and acute viral hepatitis (Reglero et al, 1980;Calvo et al, 1982;Guillou et al, 1982;Cabezas-Delamore et al, 1983;Deugnier et al, 1984;DiCioccio et al, 1985).…”

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confidence: 99%

Alpha-L-fucosidase as a serum marker of hepatocellular carcinoma in southern African blacks

Bukofzer

Stass²,

Kew³

et al. 1989

Br J Cancer

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Summary The purpose of this study was to compare alpha-L-fucosidase and alpha-fetoprotein as serum markers of hepatocellular carcinoma in 72 southern African blacks with this tumour and 64 matched patients with benign hepatic diseases which might be mistaken clinically for hepatocellular carcinoma. Alpha-Lfucosidase activity was assayed using p-nitrophenyl-L-fucopyranoside (pNpf) as a substrate and alphafetoprotein concentrations were measured by radioimmunoassay. Serum alpha-L-fucosidase activity in the patients with hepatocellular carcinoma (mean 1,268, s.e.m. + 83.7, median 1,150 and range 38-3,698 nmol pNpfml -h -1) was significantly higher than that in the matched controls (mean 798, s.e.m. +65.8, median 648 and range 273-3,825nmol pNpfml-l h-1) (P=0.0001). However, alpha-L-fucosidase was both less sensitive (75 versus 87%) and less specific (70 versus 87%) than alpha-fetoprotein as a serum marker of hepatocellular carcinoma. When, in an endeavour to eliminate false-positive results, the diagnostic cut-off level for alpha-L-fucosidase was increased to 1,500nmol pNpfml-' h-1 and for alpha-fetoprotein to 400ngml-1, the sensitivity of alpha-L-fucosidase fell to 21% whereas that of alpha-fetoprotein remained satisfactory at 78%. If the two markers were used together, the number of false-negative alpha-fetoprotein results was reduced from 13 to 5.5%. We conclude that alpha-L-fucosidase is less useful than alphafetoprotein as a single marker of hepatocellular carcinoma in southern African blacks. However, the two markers can profitably be used together.The lysosomal hydrolase, alpha-L-fucosidase (alpha-Lfucoside fucohydrolase; 3.2.1.51; AFU), is present in many mammalian tissues where it degrades fucose-containing glycoconjugates. A number of isomers of the enzyme have been identified in human tissues, including two hepatic forms (Robinson & Thorpe, 1973). The clinical importance of AFU is indicated by the occurrence, albeit rare, of a deficiency state that results in a neurovisceral storage disease known as fucosidosis (Durand et al., 1969), and by the observation that women with low serum activity of the enzyme may be prone to ovarian carcinoma (Lynch et al., 1985). Raised serum concentrations of AFU have been described in patients with a variety of benign diseases, including diabetes, hyperthyroidism, toxic oil syndrome and, of particular relevance to the present study, cirrhosis, alcoholic hepatitis and acute viral hepatitis (Reglero et al., 1980;Calvo et al., 1982;Guillou et al., 1982;Cabezas-Delamore et al., 1983;Deugnier et al., 1984;DiCioccio et al., 1985). Increased AFU activity has also been reported in association with carcinoma of the lung, breast, stomach, ovary and uterus and, more recently, with hepatocellular carcinoma (HCC) (Reglero et al., 1980;Calvo et al., 1982;Deugnier et al., 1984;DiCioccio et al., 1985). Deugnier and his colleagues (1984) found serum levels of AFU to be raised in European patients with HCC more often than serum concentrations of alpha-fetoprotein (AFP), although they cauti...

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Fucosidosis

Cited by 191 publications

References 23 publications

Structure of Nine Sialyl-Oligosaccharides Accumulated in Urine of Eleven Patients with Three Different Types of Sialidosis. Mucolipidosis II and Two New Types of Mucolipidosis

Structure of Nine Sialyl-Oligosaccharides Accumulated in Urine of Eleven Patients with Three Different Types of Sialidosis. Mucolipidosis II and Two New Types of Mucolipidosis

Novel mutations in the FUCA1 gene that cause fucosidosis

Alpha-L-fucosidase as a serum marker of hepatocellular carcinoma in southern African blacks

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