A comparison of α-<scp>l</scp>-fucosidase activity in normal and chronic-lymphocytic-leukaemia lymphocytes

Crockard, A. D.; Bridges, J. M.; Lewis, Maxwell H. R.

doi:10.1042/bst0080439

Cited by 4 publications

(2 citation statements)

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“…Basso et a1 [63] have concluded that this finding indicates that the T cells in T-CLL are fairly mature since, as previously mentioned, this enzyme appears late during T-cell maturation [ 5 5 ] . Similar patterns in CLL have been found for P-glucuronidase [57,62] and a-fucosidase [64]. This latter enzyme has also been reported to have an isoenzyme abnormality similar to hexosaminidase in A + patients with ALL [60].…”

Section: Hexosaminidase and Other Lysosomal Enzymessupporting

confidence: 71%

Enzyme alterations in leukemic cells

Dunn

Maurer

1982

American J Hematol

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Recently, much attention has been focused on various enzyme alterations found in leukemic cells. Most of the data generated thus far has involved the study of terminal deoxynucleotidyl transferase, the purine pathway enzymes, and hexosaminidase and other lysosomal enzymes. Differences in both total enzyme activities and isoenzyme patterns have been found to occur among the various leukemia types and subtypes. These changes may prove to be useful aids in diagnosing, classifying, detecting subclinical recurrent or residual disease, and as therapeutic determinants in hematopoietic neoplasia, especially in the lymphoid malignancies.

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Section: Hexosaminidase and Other Lysosomal Enzymessupporting

confidence: 71%

Enzyme alterations in leukemic cells

Dunn

Maurer

1982

American J Hematol

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“…AFUs increase activities in human tonsil B lymphocytes undergoing in vitro spontaneous apoptosis [63]. The activity of AFUs is decreased in B cells of chronic lymphocytic leukaemia when compared with control or other leukaemic lymphoid cells [64].…”

Section: Immune Cellsmentioning

confidence: 99%

Dual role of fucosidase in cancers and its clinical potential

Fu¹,

Guo²,

Feng³

et al. 2022

J. Cancer

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Glycosidases and glycosyltransferases greatly impact malignant phenotype of tumors though genetics and epigenetics mechanisms. As the member of glycoside hydrolase (GH) families 29A, α-L-fucosidases (AFUs) are involved in the hydrolysis of terminal L-fucose residues linked via α-1,2, α-1,3, α-1,4 or α-1,6 to the reducing end of N-acetyl glucosamine (GlcNAc) of oligosaccharide chains. The defucosylation process mediated by AFUs contributes to the development of various diseases, such as chronic inflammatory diseases, immune disorders, and autoimmune diseases by reducing the interaction between fucosylated adhesion molecules supporting leukocyte extravasation. AFUs also impair crucial cell-extracellular matrix (ECM) interactions and presumably subsequent cell signaling pathways, which lead to changes in tumor function and behavior. There are two isoforms of AFUs in human, namely α-L-fucosidase 1 (FUCA1) and α-L-fucosidase 2 (FUCA2), respectively. FUCA1 is a p53 target gene and can hydrolyze different fucosylation sites on epidermal growth factor receptor (EGFR), thereby determining the activation of EGFR. FUCA2 mediates the adhesion between Helicobacter pylori and gastric mucosa and is upregulated in 24 tumor types. Besides, based on the participation of AFU in signaling pathways and tumor progression, we discuss the prospect of AFU as a therapeutic target.

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