Characterization of α-L-fucosidase from two different families with fucosidosis

Troost, J.; Heijden, M.C.M. van der; Staal, Gerard E.J.

doi:10.1016/0009-8981(76)90180-7

Cited by 63 publications

(31 citation statements)

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“…Normal serum AFU activity ranges between 350 and 660 nmol pNpfml -h - (Turner et al, 1975;Troost et al, 1976;Deugnier et al, 1984). Although not specified, these values were probably established in caucasian subjects.…”

Section: Discussionmentioning

confidence: 99%

“…The purpose of this study was to compare AFU and AFP as serum markers of HCC in southern African blacks, a population that has both a high incidence of the tumour and in which AFP is a more useful tumour marker than it is in 'western' populations with a low incidence of HCC (Kew & Newberne, 1982 clinical, ultrasonographic or scintigraphic evidence of a superimposed HCC. Blood for assay was drawn from the patients with HCC before cancer chemotherapy was started.Serum AFU activity was assayed using a method similar to that described by Troost et al (1976). A mixture of 0.25 ml of 4mM p-nitrophenyl-L-fucopyranoside (pNpf) (Sigma Chemical Co, St Louis, MO), 0.5 ml 0.2 M sodium acetate buffer (pH 5.5) and 0.125ml serum was made up to a final volume of 1 ml with distilled water.…”

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confidence: 99%

“…Serum AFU activity was assayed using a method similar to that described by Troost et al (1976). A mixture of 0.25 ml of 4mM p-nitrophenyl-L-fucopyranoside (pNpf) (Sigma Chemical Co, St Louis, MO), 0.5 ml 0.2 M sodium acetate buffer (pH 5.5) and 0.125ml serum was made up to a final volume of 1 ml with distilled water.…”

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confidence: 99%

“…However, DiCioccio et al (1985) were later unable to distinguish between HCC and cirrhosis in North American patients on the basis of serum AFU concentrations. The purpose of this study was to compare AFU and AFP as serum markers of HCC in southern African blacks, a population that has both a high incidence of the tumour and in which AFP is a more useful tumour marker than it is in 'western' populations with a low incidence of HCC (Kew & Newberne, 1982 Serum AFU activity was assayed using a method similar to that described by Troost et al (1976). A mixture of 0.25 ml of 4mM p-nitrophenyl-L-fucopyranoside (pNpf) (Sigma Chemical Co, St Louis, MO), 0.5 ml 0.2 M sodium acetate buffer (pH 5.5) and 0.125ml serum was made up to a final volume of 1 ml with distilled water.…”

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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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Section: Discussionmentioning

confidence: 99%

mentioning

confidence: 99%

mentioning

confidence: 99%

mentioning

confidence: 99%

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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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“…The N-acetyl-␤-D-glucosaminidase activity was measured according to the method of Troost et al (11). Lactic dehydrogenase, whose evaluation permits to verify the absence of cell lysis, was evaluated as described by Buhl et al (12).…”

Section: Methodsmentioning

confidence: 99%

The Binding of Type I Collagen to Lymphocyte Function-associated Antigen (LFA) 1 Integrin Triggers the Respiratory Burst of Human Polymorphonuclear Neutrophils

Garnotel

Monboisse

Randoux

et al. 1995

Journal of Biological Chemistry

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The transduction pathways depending on the ␣ L ␤ 2 integrin do not involve a G protein (ruled out by the use of cholera and pertussis toxins), whereas the cytoskeleton was found to participate in the process, as evidenced by inhibition by cytochalasin B. After collagen stimulation, cytoplasmic inositol trisphosphate and calcium ion increased sharply for less than 2 min. The use of the inhibitors staurosporine and calphostin C demonstrated that protein kinase C was involved. Evaluation of the activity of this enzyme showed that, upon stimulation of PMN with collagen I, it was translocated to plasma membrane.Acrylamide gel electrophoresis of the protein bands corresponding to the integrin ␣ L ␤ 2 , followed by immunoblotting using monoclonal antibodies to phosphotyrosine, permitted us to demonstrate that, prior to stimulation by type I collagen, there was no phosphorylation, whereas after stimulation, both ␣ L and ␤ 2 chains were stained by anti-phosphotyrosine antibodies. The adhesion of PMN to pepsinized type I collagen triggered tyrosine phosphorylation of the ␤ 2 chain of the integrin, without stimulating O 2 . production by these cells, whereas their stimulation by complete type I collagen induced the tyrosine phosphorylation of both ␣ L and ␤ 2 subunits. The tyrosine phosphorylation of both integrin subunits during transduction of stimuli is a heretofore undescribed phenomenon that may correspond to a new system of transmembrane communication.Type I collagen, a major component of the extra cellular matrix, promotes the adhesion of a variety of cells in solid tissues, influencing many processes such as proliferation, differentiation, migration, and cell shape changes (1). Several receptor molecules have been demonstrated as promoting the adhesion to type I collagen. Among these receptors, some belong to the family of integrins, for instance ␣ 1 ␤ 1 , ␣ 2 ␤ 1 , and ␣ 3 ␤ 1 (2). On the other hand, some types of mobile cells also interact with collagens, for instance polymorphonuclear neutrophils (PMN), 1 a variety of leukocytes circulating in blood, capable of crossing the vascular wall in order to invade the inflamed tissues and to participate in defenses against bacteria or foreign molecules through their property of phagocytosis. In several previous papers, we demonstrated that PMN and type I collagen do interact and began to describe their interactions (3-5).Purified type I collagen is able to bind to PMN in vitro. This binding is followed by the stimulation of some main functions of PMN, such as emission of pseudopods, secretion of lytic enzymes, and liberation of superoxide. We demonstrated that the stimulation of PMN by collagen occurs through two sequences of the ␣ 1 (I) chain, both located in the C-terminal region of the molecules, an RGD sequence corresponding to residues 915-917, and a DGGRYY sequence corresponding to residues 1034 -1039, located at the C-terminal extremity of the chain. The type I collagen molecule, either fibrillar or denatured, is active, whereas pepsinized collagen, lacking the C...

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Computerized Axial Tomography and Cerebral Scintigraphy in Leukodystrophy

Willemse¹

1978

Arch Neurol

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Characterization of α-L-fucosidase from two different families with fucosidosis

Cited by 63 publications

References 4 publications

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

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

The Binding of Type I Collagen to Lymphocyte Function-associated Antigen (LFA) 1 Integrin Triggers the Respiratory Burst of Human Polymorphonuclear Neutrophils

Computerized Axial Tomography and Cerebral Scintigraphy in Leukodystrophy

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