Characterization of subspecies of apolipoprotein A-I-containing lipoprotein in homozygotes for familial lecithin:cholesterol acyltransferase deficiency
| Autor: | Ichiro Matsuda, Seikoh Horiuchi, Yasushi Saito, Kyoko Takata, Takao Ohta, Y Ikeda, J Frohlich, Rie Nakamura, Shinzaburo Hattori |
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| Rok vydání: | 1994 |
| Předmět: |
Adult
Male medicine.medical_specialty food.ingredient Apolipoprotein B Lipoproteins Sterol O-acyltransferase Biology Lecithin Phosphatidylcholine-Sterol O-Acyltransferase food Lecithin Cholesterol Acyltransferase Deficiency Internal medicine medicine Humans Incubation chemistry.chemical_classification Electrophoresis Agar Gel Lecithin cholesterol acyltransferase deficiency Apolipoprotein A-I Esterification Homozygote Middle Aged medicine.disease Lipids Enzyme Endocrinology chemistry biology.protein lipids (amino acids peptides and proteins) Electrophoresis Polyacrylamide Gel Female Phosphatidylcholine—sterol O-acyltransferase Cholesterol Esters biological phenomena cell phenomena and immunity Cardiology and Cardiovascular Medicine Apolipoprotein A-II Lipoprotein |
| Zdroj: | Arteriosclerosis and thrombosis : a journal of vascular biology. 14(7) |
| ISSN: | 1049-8834 |
| Popis: | We characterized the two species of lipoproteins containing apolipoprotein A-I (apoA-I), one containing only apoA-I (LpA-I) and the other containing apoA-I and apoA-II (LpA-I/A-II), in four homozygotes for familial lecithin: cholesterol acyltransferase (LCAT) deficiency. Two homozygotes lacked both LCAT mass and activity, whereas the other two had some residual LCAT mass and activity. In these patients, the amount of all apoA-I-containing lipoproteins was one fourth that of normal control subjects, and > 60% was LpA-I. The chemical composition of both LpA-I and LpA-I/A-II is characterized by markedly decreased ratios of neutral to polar lipids compared with those of normals and the sizes of LpA-I and LpA-I/A-II particles are shifted to smaller and larger diameter ranges when compared with those of normal particles. Changes in particle diameter are also reflected in slower electrophoretic mobilities of both LpA-I and LpA-I/A-II particles. All of these abnormalities were more evident in the two homozygotes who lacked LCAT activity. Incubation of LCAT-deficient plasma with LCAT markedly corrected the chemical and physical abnormalities in both LpA-I and LpA-I/A-II particles. These data, taken together, emphasize the importance of LCAT in modifying the chemical composition, size, and shape of LpA-I and LpA-I/A-II particles. |
| Databáze: | OpenAIRE |
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