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Control of [3H]ouabain binding to cerebromicrovascular (Na+ + K+)-ATPase by metal ions and proteins.

Abstract：

:The (Na+ + K+)-ATPase is localized to the cerebral endothelium, i.e. the blood-brain barrier, and is important for the maintenance of the brain electrolyte environment. Data from the present study indicate that Pb2+ inhibits the binding of [3H]ouabain to the cerebral microvascular (Na+ + K+)-ATPase in a time- and dose-dependent manner. Pb2(+)-induced inhibition developed slowly with a maximum obtained after 40 min. Inhibition of [3H]ouabain binding to the enzyme was 48% at 10 microM Pb2+ and appeared maximal (89%) at 100 microM Pb2+ when compared to [3H]ouabain binding in untreated microvessels at 40 min. In contrast, 100 microM Al3+ caused a 55% increase in [3H]ouabain binding to the (Na+ + K+)-ATPase, relative to untreated microvessels at 40 min. Insulin or bovine serum albumin stimulated [3H]ouabain binding to the enzyme when added at similar concentrations. However, the addition of both insulin and bovine serum albumin did not result in an additive effect. These results show that insulin exerts a nonspecific effect on [3H]ouabain binding to the (Na+ + K+)-ATPase similar to that evoked by bovine serum albumin. However, the metal ions Pb2+ and Al3+ provoke selective alterations in the cerebromicrovascular (Na+ + K+)-ATPase with Pb2+ inhibiting and Al3+ stimulating [3H]ouabain binding.

journal_name

Biochem Pharmacol

journal_title

Biochemical pharmacology

authors

Caspers ML,Kwaiser TM,Grammas P

doi

10.1016/0006-2952(90)90606-l

subject

Has Abstract

pub_date

1990-06-15 00:00:00

pages

1891-5

issue

12

eissn

0006-2952

issn

1873-2968

pii

0006-2952(90)90606-L

journal_volume

39

pub_type

杂志文章

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