TY - JOUR
T1 - Characterization of the stimulation of neuronal Na+, K+-ATPase activity by low concentrations of ouabain
AU - Lichtstein, D.
AU - Samuelov, S.
AU - Bourrit, A.
PY - 1985
Y1 - 1985
N2 - Low concentrations (< 10-7 M) of ouabain stimulate the activity of Na+, K+-ATPase in whole homogenates of rat brain. The magnitude of this stimulation varies from 5 to 70%. The concentrations of ouabain which induces maximal stimulation is also highly variable and ranges between 10-9 to 10-7 M. The ouabain stimulation disappears following 1:50 dilution and 2 h preincubation or freezing and thawing of the membranes or their treatment with deoxycholate. "Aging" of a preparation of ATPase also results in loss of its ability to be stimulated by ouabain but ouabain inhibition is preserved. No stimulation of enzyme activity by ouabain is observed in rat brain microsomal fraction. The β-adrenergic blocker propranolol does not inhibit the ouabain induced stimulation of ATPase activity. It is suggested that the stimulation of Na+, K+-ATPase activity by low concentrations of cardiac glycosides if a result of either the displacement of an endogenous ouabain-like compound from the enzyme or an indirect effect by changing membrane surrounding environment of the Na+, K+-ATPase.
AB - Low concentrations (< 10-7 M) of ouabain stimulate the activity of Na+, K+-ATPase in whole homogenates of rat brain. The magnitude of this stimulation varies from 5 to 70%. The concentrations of ouabain which induces maximal stimulation is also highly variable and ranges between 10-9 to 10-7 M. The ouabain stimulation disappears following 1:50 dilution and 2 h preincubation or freezing and thawing of the membranes or their treatment with deoxycholate. "Aging" of a preparation of ATPase also results in loss of its ability to be stimulated by ouabain but ouabain inhibition is preserved. No stimulation of enzyme activity by ouabain is observed in rat brain microsomal fraction. The β-adrenergic blocker propranolol does not inhibit the ouabain induced stimulation of ATPase activity. It is suggested that the stimulation of Na+, K+-ATPase activity by low concentrations of cardiac glycosides if a result of either the displacement of an endogenous ouabain-like compound from the enzyme or an indirect effect by changing membrane surrounding environment of the Na+, K+-ATPase.
UR - http://www.scopus.com/inward/record.url?scp=0022254432&partnerID=8YFLogxK
U2 - 10.1016/0197-0186(85)90069-5
DO - 10.1016/0197-0186(85)90069-5
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AN - SCOPUS:0022254432
SN - 0197-0186
VL - 7
SP - 709
EP - 715
JO - Neurochemistry International
JF - Neurochemistry International
IS - 4
ER -