Apolipoprotein B-48 or Its Apolipoprotein B-100 Equivalent Mediates the Binding of Triglyceride-Rich Lipoproteins to Their Unique Human Monocyte-Macrophage Receptor

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Apolipoprotein B-48 or its apolipoprotein B-100 equivalent mediates the binding of triglyceride-rich lipoproteins to their unique human monocyte-macrophage receptor.

Studies in animals and humans have demonstrated uptake of plasma chylomicrons (triglyceride-rich lipoprotein [TGRLP] of Sf>400) by accessible macrophages in vivo. One potential mechanism is via a unique receptor pathway we previously identified in human blood and THP-1 monocytes and macrophages for the lipoprotein lipase (LpL)- and apolipoprotein (apo) E-independent, high-affinity, specific bin...

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Measurement of human apolipoprotein B-48 and B-100 kinetics in triglyceride-rich lipoproteins using [5,5,5-2H3]leucine.

A primed-constant infusion of deuterated leucine was used in humans to determine the maximal level of enrichment at plateau of apolipoprotein (apo)B-48 and apoB-100 which are synthesized in the intestine and liver, respectively, and to compare the kinetics of these two proteins under identical conditions. Eight normal subjects (four post-menopausal females and four males) over the age of 40 wer...

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Apolipoprotein B 100 and 48

Apolipoprotein B is the main structural surface protein found on all beta-lipoproteins (Chylomicrons, VLDLs, IDLs and LDLs). There is a single molecule of apoB on each of those lipoproteins. It is the only apolipoprotein that is not transferablei.e. it is with the particle from its birth till its death. Beta-lipoproteins are the lipoproteins capable of trafficking cholesterol into the artery wa...

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Determination of apolipoproteins B-48 and B-100 in triglyceride-rich lipoproteins by analytical SDS-PAGE.

The present work describes a procedure for determining apolipoproteins (apo) B-100 and B-48 in subfractions of triglyceride-rich lipoproteins by analytical sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) with Coomassie staining. The chromogenicity of the two apoB species was found to be almost equal, and independent of lipoprotein particle size. Both proteins were sensitive...

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Structure of apolipoprotein B-100 of human low density lipoproteins.

We have analyzed low density lipoproteins (LDL) apolipoprotein (apop) B structure by direct sequence analysis of LDL apo B-100 tryptic peptides. Native LDL were digested with trypsin, and the products were fractionated on a Sephadex G-50 column. The partially digested apo B-100 still associated with lipids was recovered in the void volume (designated trypsin-nonreleasable, TN, peptides). The re...

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ژورنال

عنوان ژورنال: Arteriosclerosis, Thrombosis, and Vascular Biology

سال: 1998

ISSN: 1079-5642,1524-4636

DOI: 10.1161/01.atv.18.6.968