Serum alpha <scp>l</scp>‐fucosidase enzyme activity in ovarian and other female genital tract tumors

Abdel‐Aleem, Hany; Ahmed, Amany A.; Sabra, A.M.; Zakhari, Madeha; Soliman, Mona; Hamed, Hossam O.

doi:10.1016/s0020-7292(96)02770-1

Cited by 29 publications

(12 citation statements)

References 6 publications

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“…This has been attributed to variations in the sialic acid content as well as the two different alleles and polymorphisms within the FUC1 gene. The serum ALF activity in normal individuals is reported to be 381U/ml ±10.86 4.…”

Section: Introductionmentioning

confidence: 99%

“…A syndrome previously known as leukocyte adhesion deficiency II is now recognised as a generalized metabolic disease caused by severe hypofucosylation of glycoconjugates including selectin ligands 7. Further to this, alterations in levels of ALF have been reported in the plasma and/or serum of patients with endometrial, hepatocellular and colorectal cancer 8,4,9.…”

Section: Introductionmentioning

confidence: 99%

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Leukocyte Extravasation: An Immunoregulatory Role for α-l-Fucosidase?

Ali

Jenkins

Kirkley

et al. 2008

The Journal of Immunology

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Fucosylated oligosaccharides and glycoconjugates have been implicated in several biological events, including the cell-cell adhesion processes which mediate inflammation. Alpha-L-fucosidase (ALF) is an exoglycosidase which is involved in the hydrolytic degradation of α-L-fucose from glycoconjugates. In this study we investigated the potential role of ALF in regulation of leukocyte migration. Measurement of trans-endothelial migration in response to CCL5 demonstrated that pre-treatment of monocytic cells with ALF reduced migration (p=0.0004) to a greater extent than treatment of the endothelial monolayer (p=0.0374). Treatment with ALF significantly reduced the adhesion of monocytic cells to immobilized P-selectin.Fc. A murine model of experimental autoimmune uveitis was then used to show that treatment of splenic cells with ALF produced an 8.6-fold decrease in rolling and a 3.2-fold decrease in cell migration across the retinal vasculature. Further in vitro studies demonstrated that treatment of monocytes with the chemokines CCL3 or CCL5 increased the level of mRNA encoding ALF; this was accompanied by the detection of significant increases in both the 51kDa and 56kDa components of ALF by Western blotting. Treatment of monocytic cells with ALF for 2h significantly reduced the cell-surface expression of CD31, with a further decrease in expression observed after 5h (p=0.002). Thus, CD31 and fucosylated ligands of P-selectin seem to be the candidates through which ALF mediates its effect in vitro. These data identify a previously unrecognized immunoregulatory role for ALF in late stages of inflammation.

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Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Leukocyte Extravasation: An Immunoregulatory Role for α-l-Fucosidase?

Ali

Jenkins

Kirkley

et al. 2008

The Journal of Immunology

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“…Furthermore, altered expression of ␣-L-fucosidases and corresponding changes in fucosylation levels are seen in many carcinomas (20,21). Accordingly, the presence of human ␣-L-fucosidase in the serum can be used as an early detection marker for several carcinomas (22)(23)(24). Additionally, ␣-Lfucosidases have been used to determine the function of particular L-fucose residues.…”

mentioning

confidence: 99%

Structural Basis of the Catalytic Reaction Mechanism of Novel 1,2-α-L-Fucosidase from Bifidobacterium bifidum

Nagae

Tsuchiya

Katayama

et al. 2007

Journal of Biological Chemistry

118

101

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1,2-␣-L-Fucosidase (AfcA), which hydrolyzes the glycosidic linkage of Fuc␣1-2Gal via an inverting mechanism, was recently isolated from Bifidobacterium bifidum and classified as the first member of the novel glycoside hydrolase family 95. To better understand the molecular mechanism of this enzyme, we determined the x-ray crystal structures of the AfcA catalytic (Fuc) domain in unliganded and complexed forms with deoxyfuconojirimycin (inhibitor), 2-fucosyllactose (substrate), and L-fucose and lactose (products) at 1.12-2.10 Å resolution. The AfcA Fuc domain is composed of four regions, an N-terminal ␤ region, a helical linker, an (␣/␣) 6 helical barrel domain, and a C-terminal ␤ region, and this arrangement is similar to bacterial phosphorylases. In the complex structures, the ligands were buried in the central cavity of the helical barrel domain. Structural analyses in combination with mutational experiments revealed that the highly conserved Glu 566 probably acts as a general acid catalyst. However, no carboxylic acid residue is found at the appropriate position for a general base catalyst. Instead, a water molecule stabilized by Asn 423 in the substrate-bound complex is suitably located to perform a nucleophilic attack on the C1 atom of L-fucose moiety in 2-fucosyllactose, and its location is nearly identical near the O1 atom of ␤-L-fucose in the products-bound complex. Based on these data, we propose and discuss a novel catalytic reaction mechanism of AfcA.

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“…Besides, many studies on the relationships between the serum form of AFU and other diseases had been reported. The alterations of AFU activity and properties also possess a high clinical value in the diagnosis of colorectal cancer [ 25 ], ovarian cancer [ 26 ], chronic inflammation, and autoimmune disorders [ 27 ]. Moreover, a comprehensive research project that contains 188,077 patients with 64 clinically defined diseases and 9,519 healthy controls showed that serum AFU activities were higher in patients with preeclampsia, liver cancer, hepatitis, psoriasis, and multiple myeloma, while serum AFU activities were the lowest in patients with uremia, azotemia, myeloproliferative disorder, and Alzheimer's disease among the 64 diseases studied [ 28 ].…”

Section: Discussionmentioning

confidence: 99%

The Value of Preoperative Alpha-L-Fucosidase Levels in Evaluation of Malignancy and Differential Diagnosis of Urothelial Neoplasms

Chen

Xing

Cui³

et al. 2020

Journal of Oncology

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Purpose. To evaluate the role of Alpha-L-fucosidase (AFU) in diagnosis and differential diagnosis of pure urothelial carcinoma (UC), urothelial carcinoma with squamous differentiation (UCSD), and squamous cell carcinoma (SqCC). Methods. A retrospective study was performed for 599 patients who were histologically confirmed with urothelial tumor. Preoperative AFU levels were compared across the distinct subgroups with different clinicopathological parameters. ROC curve analysis and logistic regression analysis were performed to further evaluate the clinical application value of serum AFU levels in diagnosis and differential diagnosis of urothelial tumors. Results. There were no statistically significant differences in the AFU levels between different groups with different malignant degrees (UC versus papilloma and papillary urothelial neoplasm of low malignant potential [PUNLMP], high-grade UC versus low-grade UC, invasive versus noninvasive malignant uroepithelial tumor) and different pathological types (UC, UCSD, and SqCC) (all P>0.05). ROC curve analysis and logistic regression analysis showed that there was no statistically significant association between AFU levels and the tumor characteristics (all P>0.05). Conclusions. Preoperative AFU levels cannot serve as a reliable predictor for malignant degree and differential diagnosis, including pure UC, UCSD, and SqCC of urothelial tumors.

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Serum alpha l‐fucosidase enzyme activity in ovarian and other female genital tract tumors

Cited by 29 publications

References 6 publications

Leukocyte Extravasation: An Immunoregulatory Role for α-l-Fucosidase?

Leukocyte Extravasation: An Immunoregulatory Role for α-l-Fucosidase?

Structural Basis of the Catalytic Reaction Mechanism of Novel 1,2-α-L-Fucosidase from Bifidobacterium bifidum

The Value of Preoperative Alpha-L-Fucosidase Levels in Evaluation of Malignancy and Differential Diagnosis of Urothelial Neoplasms

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