Major apolipoprotein B-100 mutations in lipoprotein metabolism and atherosclerosis

Title:

Major apolipoprotein B-100 mutations in lipoprotein metabolism and atherosclerosis

Creator:

Michal Vrablík, Richard Češka, and Aleš Hořínek

Identifier:

https://cdk.lib.cas.cz/client/handle/uuid:a827cd5a-4a94-418e-a6ff-6ad05318471f
uuid:a827cd5a-4a94-418e-a6ff-6ad05318471f
issn:0862-8408

Subject:

Fyziologie člověka a srovnávací fyziologie, hyperlipidémie, ateroskleróza, hyperlipidemia, atherosclerosis, apolipoprotein B-100, mutations, 14, and 612

Type:

article, články, model:article, and TEXT

Format:

print, bez média, and svazek

Description:

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., M. Vrablík, R. Češka, A. Hořínek., and Obsahuje bibliografii

Language:

English

Rights:

http://creativecommons.org/licenses/by-nc-sa/4.0/
policy:public

Source:

Physiological research | 2001 Volume:50 | Number:4

Harvested from:

CDK

Metadata only:

false