Serum β-N-acetylglucosaminidase, β-d-glucosidase, α-d-glucosidase, β-d-fucosidase, α-l-fucosidase and β-d-galactosidase levels in acute viral hepatitis, pancreatitis, myocardial infarction and breast cancer

Calvo, Pedro; Barba, JoséL.; Cabezas, JoséA.

doi:10.1016/0009-8981(82)90400-4

Cited by 28 publications

(9 citation statements)

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“…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 cautioned that studies in larger numbers of patients were needed before liver cancer specificity could be assigned to AFU.…”

mentioning

confidence: 51%

“…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).…”

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confidence: 59%

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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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confidence: 51%

mentioning

confidence: 59%

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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“…Although glycosidases may exist in serum, an interesting finding is that the levels of some glycosidases are actually reduced, and many do not appear to change in cancer patients (25). We plan to conduct more in depth analysis of the degradation of glycans in serum during our continuing testing and validation phases of this method.…”

Section: Discussionmentioning

confidence: 99%

A Serum Glycomics Approach to Breast Cancer Biomarkers

Kirmiz

et al. 2007

Molecular & Cellular Proteomics

215

207

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Because the glycosylation of proteins is known to change in tumor cells during the development of breast cancer, a glycomics approach is used here to find relevant biomarkers of breast cancer. These glycosylation changes are known to correlate with increasing tumor burden and poor prognosis. Current antibody-based immunochemical tests for cancer biomarkers of ovarian (CA125), breast (CA27.29 or CA15-3), pancreatic, gastric, colonic, and carcinoma (CA19-9) target highly glycosylated mucin proteins. However, these tests lack the specificity and sensitivity for use in early detection. This glycomics approach to find glycan biomarkers of breast cancer involves chemically cleaving oligosaccharides (glycans) from glycosylated proteins that are shed or secreted by breast cancer tumor cell lines. The resulting free glycan species are analyzed by MALDI-FT-ICR MS. Further structural analysis of the glycans can be performed in FTMS through the use of tandem mass spectrometry with infrared multiphoton dissociation. Glycan profiles were generated for each cell line and compared. These methods were then used to analyze sera obtained from a mouse model of breast cancer and a small number of serum samples obtained from human patients diagnosed with breast cancer or patients with no known history of breast cancer. In addition to the glycosylation changes detected in mice as mouse mammary tumors developed, glycosylation profiles were found to be sufficiently different to distinguish patients with cancer from those without. Although the small number of patient samples analyzed so far is inadequate to make any legitimate claims at this time, these promising but very preliminary results suggest that glycan profiles may contain distinct glycan biomarkers that may correspond to glycan "signatures of cancer." Molecular & Cellular Proteomics 6:43-55, 2007.

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“…At present, sensitive optimized and reproducin the diagnosis of a number of diseases (1)(2)(3)(4)(5)(6)(7). For ible fluorimetric methods are available for the determiinstance, the plasma levels of lysosomal enzymes have nation of lysosomal enzymes in plasma (17), including been shown to correlate with the metabolic control of the isozymes of N-acetyl-ß-£>-glucosaminidase (18).…”

Section: Introductionmentioning

confidence: 99%

Automated Fluorimetric Assay Procedure for Glucohydrolases Using a Routine Centrifugal Analyser Assay of Enzymes of Lysosomal Origin in Plasma, II

Goi¹,

Guagnellini²,

Besozzi

et al. 1995

CCLM

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Summary:The manual fluorimetric procedure, considered as a reference method for the determination of N-acetyl-ß-Z)-glucosaminidase, ß-D-glucuronidase and ß-£>-galactosidase in human plasma, was automated as a routine method, using the IL Monarch centrifugal analyser. Using a liquid standard with a known enzyme content, the automated assay correlated fairly well with the reference manual method (r values very close to 1). Its analytical imprecision was much lower than that of the manual method. The automated assay of N-acetyl-ß-£>-glucosaminidase, ß-D-glucuronidase and ß-D-galactosidase gave coefficients of variation of 5.7-6.9, 3.6-5.0 and 3.8-4.2%, respectively, detection limits of 4, 2 and 1 mU/1 plasma respectively, and linear responses of up to 73, 8.4 and 0.9 U/l of plasma respectively. Furthermore, the method required only small volumes of undiluted plasma (4-10 ). This method appears to be reliable, sensitive, simple enough for routine analyses and as cost effective as the most common routine serum enzyme assays.

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Serum β-N-acetylglucosaminidase, β-d-glucosidase, α-d-glucosidase, β-d-fucosidase, α-l-fucosidase and β-d-galactosidase levels in acute viral hepatitis, pancreatitis, myocardial infarction and breast cancer

Cited by 28 publications

References 11 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

A Serum Glycomics Approach to Breast Cancer Biomarkers

Automated Fluorimetric Assay Procedure for Glucohydrolases Using a Routine Centrifugal Analyser Assay of Enzymes of Lysosomal Origin in Plasma, II

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