Abstract
Mutations in the ATP-binding cassette (ABC) proteins ABCG5 or ABCG8 cause sitosterolemia, a condition with increased accumulation of plant sterols. Upon high level expression of the ABCG5 and ABCG8 proteins in baculovirus-Sf9 cell expression system we found a distinct, vanadate sensitive ATPase activity in isolated membrane preparations only when the two proteins were co-expressed. This ATPase activity was significantly stimulated by the addition of certain androgen hormones and analogs, and was effectively inhibited by progesterone. Our results provide a new aspect of biochemical and functional characterization of the ABCG5/ABCG8 proteins and their possible involvement in steroid hormone transport or regulation.
Publication types
-
Research Support, Non-U.S. Gov't
MeSH terms
-
ATP Binding Cassette Transporter, Subfamily G, Member 5
-
ATP Binding Cassette Transporter, Subfamily G, Member 8
-
ATP-Binding Cassette Transporters / genetics
-
ATP-Binding Cassette Transporters / physiology*
-
Adenosine Triphosphatases / metabolism*
-
Androgens / pharmacology
-
Androstanes / pharmacology*
-
Animals
-
Cell Line
-
Hormones / metabolism
-
Humans
-
Insecta
-
Lipoproteins / genetics
-
Lipoproteins / physiology*
-
Membrane Proteins
-
Progesterone / pharmacology
-
Transduction, Genetic
-
Vanadates
Substances
-
ABCG5 protein, human
-
ABCG8 protein, human
-
ATP Binding Cassette Transporter, Subfamily G, Member 5
-
ATP Binding Cassette Transporter, Subfamily G, Member 8
-
ATP-Binding Cassette Transporters
-
Androgens
-
Androstanes
-
Hormones
-
Lipoproteins
-
Membrane Proteins
-
Vanadates
-
Progesterone
-
Adenosine Triphosphatases