Cell surface human αâLâfucosidase
2001
Cordero, Oscar J. | Merino, Ana | de la Cadena, María Páez | Bugía, Begoña | Nogueira, Montserrat | Viñuela, Juan E. | MartínezâZorzano, Vicenta S. | de Carlos, Alejandro | RodríguezâBerrocal, F Javier
The acid αâlâfucosidase is usually found as a soluble component of lysosomes where fucoglycoconjugates are degraded. In the present investigation, we have demonstrated the existence of a cell surface protein with enzymatic αâlâfucosidase activity that crossreacts specifically with a rabbit antiâ(αâlâfucosidase) Ig. By different approaches, this αâlâfucosidase, which represents 10–20% of the total cellular fucosidase activity, was detected in all the tested human cells (hemopoietic, epithelial, mesenchymal). Two bands of ≈â43–49âkDa were observed, although theoretical data support the possibility of having the same genetic origin that the known 50 to 55âkDa Mrαâlâfucosidase. We speculate about an alternative traffic pathway for the plasma membrane αâlâfucosidase to work on the rapid turnover of glycoproteins.
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