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Cell surface human alpha-L-fucosidase.

O J Cordero1, A Merino, M Páez de la Cadena

  • 1Department of Biochemistry and Molecular Biology, University of Santiago de Compostela, Faculty of Biology, Santiago de Compostela, Spain. bnojcord@usc.es

European Journal of Biochemistry
|June 8, 2001
PubMed
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Researchers discovered a cell surface alpha-L-fucosidase enzyme in human cells, distinct from the lysosomal form. This enzyme constitutes 10-20% of total cellular fucosidase activity and may have a unique pathway for glycoprotein degradation.

Area of Science:

  • Biochemistry
  • Cell Biology
  • Enzymology

Background:

  • Acid alpha-L-fucosidase is typically a lysosomal enzyme involved in fucoglycoconjugate degradation.
  • The precise localization and function of all alpha-L-fucosidase isoforms are not fully understood.

Purpose of the Study:

  • To investigate the presence and characteristics of alpha-L-fucosidase activity on the cell surface.
  • To determine the contribution of cell surface alpha-L-fucosidase to total cellular enzymatic activity.

Main Methods:

  • Utilized specific antibodies against alpha-L-fucosidase for cross-reactivity studies.
  • Employed various biochemical approaches to detect and characterize the enzyme in different human cell types.
  • Analyzed protein bands using gel electrophoresis.

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Main Results:

  • Demonstrated a cell surface protein with enzymatic alpha-L-fucosidase activity.
  • This cell surface enzyme represents 10-20% of total cellular fucosidase activity.
  • Detected in hemopoietic, epithelial, and mesenchymal human cells, appearing as two bands (43-49 kDa).

Conclusions:

  • Identified a novel cell surface alpha-L-fucosidase in human cells.
  • This enzyme likely originates from the same genetic source as the known lysosomal form but follows an alternative trafficking pathway.
  • Speculated role in the rapid turnover of cell surface glycoproteins.