Vol. 157, No. 3, 1988
December 30, 1988
BIOCHEMICAL AND BIOPHYSICALRESEARCH COMMUNICATIONS
Pages 867-874
CHARACTERIZATION OF THE CALPASTATIN DEFECT IN ERYTHROCYTES FROM PATIENTS WITH
ESSENTIAL HYPERTENSION
Pontremoli, S., Salamino, F., Sparatore, B., De Tullio, R., Pontremoli, R.*,
and Melloni, E.
Institute of Biological Chemistry, University of Genoa, Viale Benedetto XV/1,
16132 Genoa, Italy
*ISMI, Section of Nephrology, University of Genoa, Viale Benedetto XV/6, 16132
Genoa, Italy
Received November 8, 1988
In erythrocytes of patients with essential hypertension the level of cal-
pastatin activity was found to be significantly lower than in red cells of nor-
motensive subjects (i). We now demonstrate, by Western blot analysis, that the
decreased inhibitory activity is due to a corresponding decrease in the amount
of the inhibitor protein. This is also supported by the observation that calpa-
statins isolated and purified from erythrocytes of normotensive and hyperten-
sive patients, have identical specific activity. Data are presented indicating
that the decreased level of calpastatin cannot be ascribed to an accelerated
decay of the inhibitor during the erythrocyte life span. Taken together the
previous and pre~ent results further emphasize that an umbalanced proteolytic
system may represent one of the molecular mechanisms responsible for those mem-
brane abnormalities underlying the development of essential hypertension and
its clinical complications. ~ 1988AcademicPress, Inc.
It is generally accepted that in humans with essential hypertension and in
rats with spontaneous hypertension (2) the red cell membrane structure and fun-
ctions are significantly altered. This conclusion is supported by experimental
data indicating= a decreased intracellular Na + content and cell volume (3), an
enhanced phosphorylation of the anion transport protein (4) and an altered
transport of cations (5-7) possibly resulting in an intracellular increase of
free Ca 2+ (8, 9). Furthermore we have demonstrated that in erythrocytes of pa-
tients with essential hypertension and also of genetically hypertensive rats,
the level of calpastatin activity is profoundly reduced in comparison to red
cells of normotensive controls (1, i0, 11). Based on these observations, a de-
fective regulation of calpain resulting from a decreased activity of its natu-
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