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Abstract
Two human monocyte-macrophage (HMM) membrane binding proteins, (MBP) 200 and 235, are receptor candidates that bind to the apolipoprotein (apo)B-48 domain in triglyceride-rich lipoproteins for uptake independent of apoE. Microsequence analysis of the purified reduced MBP 200R characterized tryptic peptides of MBP 200R. A synthetic peptide mimicking a unique, unambiguous 10-residue sequence (AEGLMVTGGR) induced antipeptide antibodies that specifically recognized MBP 200, 235 and 200R, in 1- and 2-dimensional analyses, indicating 1) the ligand binding protein was sequenced and 2) MBP 200 and 235 yielded MBP 200R upon reduction. These antibodies identified the MBPs in human blood-borne, THP-1, U937 MMs, and endothelial cells (EC) but not in human fibroblasts or Chinese hamster ovary (CHO) cells. Fluorescence activated cell sorting (FACS) analysis located the MBPs on the MM surface as necessary for receptor function. The 10-residue, unambiguous MBP 200-derived sequence is unique, with no matches in extant protein databases. Antipeptide antibodies bind to the MBPs in reticuloendothelial cells that have this receptor activity, but not to proteins in cells that lack this receptor activity. These studies provide the first direct protein sequence and immunochemical data that a new, unique apoB receptor for triglyceride-rich lipoproteins exists in human monocytes, macrophages, and endothelial cells.—Bradley, W. A., M. L. Brown, M. P. Ramprasad, R. Li, R. Song, and S. H. Gianturco. Antipeptide antibodies reveal interrelationships of MBP 200 and MBP 235: unique apoB-specific receptors for triglyceride-rich lipoproteins on human monocyte-macrophages. J. Lipid Res. 1999. 40: 744–752.
Highlights
Two human monocyte-macrophage (HMM) membrane binding proteins, (MBP) 200 and 235, are receptor candidates that bind to the apolipoproteinB-48 domain in triglyceride-rich lipoproteins for uptake independent of apoE
We have described an apoE, lipoprotein lipase (LpL), and heparan sulfate proteoglycan (HSPG)independent, high affinity receptor pathway for the receptormediated uptake of triglyceride-rich lipoproteins (TGRLP) in both murine macrophages [6,7,8] and human monocyte-macrophages (MM) and THP-1 cells [9] that leads to lipid accumulation and foam cell formation in vitro
Back calculations from the yield of tryptic fragments indicated that approximately 50 picomoles of protein had been digested, which corresponded to estimates based upon the Ponceau red staining of the MBP 200R on the nitrocellulose used for the amino acid sequence analysis
Summary
Two human monocyte-macrophage (HMM) membrane binding proteins, (MBP) 200 and 235, are receptor candidates that bind to the apolipoprotein (apo)B-48 domain in triglyceride-rich lipoproteins for uptake independent of apoE. A synthetic peptide mimicking a unique, unambiguous 10-residue sequence (AEGLMVTGGR) induced antipeptide antibodies that recognized MBP 200, 235 and 200R, in 1- and 2-dimensional analyses, indicating 1 ) the ligand binding protein was sequenced and 2 ) MBP 200 and 235 yielded MBP 200R upon reduction. Antipeptide antibodies bind to the MBPs in reticuloendothelial cells that have this receptor activity, but not to proteins in cells that lack this receptor activity These studies provide the first direct protein sequence and immunochemical data that a new, unique apoB receptor for triglyceride-rich lipoproteins exists in human monocytes, macrophages, and endothelial cells.—Bradley, W.
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