Please use this identifier to cite or link to this item:
Type: Artigo de periódico
Title: Phospholipid Transfer Protein Activity In Two Cholestatic Patients.
Author: de Faria, Eliana Cotta
Gebrin, Adriana Celeste
Nadruz Júnior, Wilson
Castilho, Lucia Nassi
Abstract: Plasma phospholipid transfer protein mediates the transfer of phospholipids from triglyceride-rich lipoproteins, very low density lipoproteins and low density lipoproteins to high density lipoproteins, a process that is also efficient between high density lipoprotein particles. It promotes a net movement of phospholipids, thereby generating small lipid-poor apolipoprotein AI that contains particles and subfractions that are good acceptors for cell cholesterol efflux. We measured the activity of plasma phospholipid transfer protein in two cholestatic patients, assuming that changes in activity would occur in serum that was positive for lipoprotein X. Both patients presented severe hypercholesterolemia, high levels of low density lipoprotein cholesterol and, in one case, low levels of high density lipoprotein cholesterol and high levels of phospholipid serum. The phospholipid transfer activity was close to the lower limit of the reference interval. To our knowledge, this is the first time such results have been presented. We propose that phospholipid transfer protein activity becomes reduced under cholestasis conditions because of changes in the chemical composition of high density lipoproteins, such as an increase in phospholipids content. Also, lipoprotein X, which is rich in phospholipids, could compete with high density lipoproteins as a substrate for phospholipid transfer protein.
Subject: Adult
Electrophoresis, Agar Gel
Middle Aged
Phospholipid Transfer Proteins
Citation: São Paulo Medical Journal = Revista Paulista De Medicina. v. 122, n. 4, p. 175-7, 2004-Jul.
Rights: aberto
Identifier DOI: /S1516-31802004000400009
Date Issue: 2004
Appears in Collections:Unicamp - Artigos e Outros Documentos

Files in This Item:
File SizeFormat 
pmed_15543374.pdf306.2 kBAdobe PDFView/Open

Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.