Major Apolipoprotein B-100 Mutations in
Lipoprotein Metabolism and Atherosclerosis
M.
VRABLÍK, R. ČEŠKA,
A. HOŘÍNEK
Third
Internal Department, First Faculty of Medicine,
Charles University, Prague, Czech Republic
Received
September 13, 2000
Accepted December 15, 2000
Summary
Apolipoprotein
(apo) B-100 is a key protein compound of plasma
lipid metabolism. This protein, as a sole
component of LDL particles, to a great extent
controls the homeostasis of LDL cholesterol in
the plasma. Therefore, this protein and its
structural variants play an important role in
development of hyperlipidemia and
atherosclerosis. Intensive research into the
structure and biological functions of apoB-100
has led to identification of its complete
structure as well as the responsible binding
sites. With the development of the methods of
molecular biology, some structural variants of
the apoB-100 protein that directly affect its
binding properties have been described. These are
mutations leading to amino acid substitution at
positions 3500 (R3500Q and R3500W) and 3531
(R3531C) that have been shown to decrease the
binding affinity of apoB-100 in vitro. However,
only the former mutations have been unequivocally
demonstrated to cause hyperlipidemia in vivo.
This minireview is aimed to discuss the impact of
apoB-100 and its structural variants on plasma
lipid metabolism and development of
hyperlipidemia.
Key
words
Apolipoprotein
B-100 · Mutations · Hyperlipidemia ·
Atherosclerosis
Reprint
requests
Dr.
M. Vrablík, Third Internal Department, First
Faculty of Medicine, Charles University, U
nemocnice 1, 128 21 Prague 2, Czech Republic.
E-mail: vrablik.michal@post.cz
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