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Blood, 1 February 2002, Vol. 99, No. 3, pp. 1064-1070
RED CELLS
Acidic and neutral sialidase in the erythrocyte membrane of
type 2 diabetic patients
Bruno Venerando,
Amelia Fiorilli,
Gianluigi Croci,
Cristina Tringali,
Giancarlo Goi,
Laura Mazzanti,
Giovanna Curatola,
Giovanni Segalini,
Luca Massaccesi,
Adriana Lombardo, and
Guido Tettamanti
From the Department of Medical Chemistry and
Biochemistry School of Medicine, University of Milan; Diabetic Unit of
Bassini Hospital Cinisello Balsamo; both of Milan, Italy; and
Institute of Biochemistry, School of Medicine, University of Ancona,
Italy.
The behavior of the 2 sialidase forms present in the erythrocyte
membrane was investigated in 117 subjects with type 2 diabetes mellitus
versus 95 healthy controls. A significant increase of the acidic form
of sialidase, which is anchored to the membrane by a
glycosylphosphatidylinositol bridge, was observed in
erythrocyte resealed membranes. On the contrary, the neutral form of
the enzyme, the only one capable of removing lipid- and protein-bound
sialic acid from endogenous and exogenous sialoderivatives, was
significantly reduced with a consequent increase of erythrocyte
membrane total sialic acid content. Disease duration, therapy,
glycemia, parameters of metabolic control, and presence of
complications, except nephropathies, had no influence on the tested
enzyme activities. Diabetic subjects showed a different erythrocyte age
distribution, with an almost double proportion of young red cells and
only one quarter of senescent ones compared with controls. In young
erythrocytes, diabetic and control subjects had the same distribution
of the 2 enzymes, while in senescent cells the acidic enzyme was
increased 3.5-fold and the neutral form was reduced by half in the
diabetic subjects. The increase of both acidic sialidase and total
membrane-bound sialic acid, together with an overpresence of young
red cells in diabetics, suggests that in this pathological condition
there might be an altered aging process with a diminished expression of
the neutral form of the enzyme and an increase of bound sialic acid. It
has been suggested that the expression of the neutral enzyme requires
some activation mechanism that is impaired in diabetes.
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