Key result
Proteomic analysis of human chylomicron remnants identified 42 associated proteins, revealing that HDL-associated proteins and apoC-I are significantly more abundant in chylomicron remnants than in VLDL remnants.
Why the study?
Structural and functional characterization of atherogenic chylomicron remnants has remained unclear due to difficulties separating them from VLDL remnants.
Observational (n=8)
No
The first proteomic characterization of human chylomicron remnants reveals enrichment of specific apolipoproteins and acute-phase proteins, providing mechanistic insights into their atherogenic properties.
Should not yet alter lipid management; leaves open mechanistic roles of remnant proteins in atherosclerosis.
AIM: Postprandial hypertriglyceridemia (PHTG) is an independent risk factor for coronary heart diseases. PHTG exhibits accumulation of apoB-48 containing chylomicron remnants (CM-Rs) and apoB-100 containing VLDL remnants (VLDL-Rs), which are both known to be atherogenic. However, unlike VLDL-Rs, structural and functional characterization of CM-Rs remains to be elucidated due to challenges in separating CM-Rs from VLDL-Rs. Recently, we successfully isolated CM-Rs and VLDL-Rs utilizing anti-apoB-48 or apoB-100 specific antibodies. This study aimed to characterize the proteome of CM-Rs along with that of VLDL-Rs. METHODS: Eight healthy subjects were enrolled. Venous blood was drawn 3 hours after high-fat-containing meals. We isolated CM-Rs and VLDL-Rs from sera through combination of ultracentrifugation and immunoprecipitation using apoB-48 or apoB-100 specific antibodies, followed by shotgun proteomic analysis. RESULTS: We identified 42 CM-Rs or VLDL-Rs-associated proteins, including 11 potential newly identified proteins such as platelet basic protein (PPBP) and platelet factor 4, which are chemokines secreted from platelets. ApoA-I, apoA-IV, and clusterin, which are also known as HDL-associated proteins, were significantly more abundant in CM-Rs. Interestingly, apoC-I, which reduces the activity of lipoprotein lipase and eventually inhibits catabolism of remnant proteins, was also more abundant in CM-Rs. Moreover, we identified proteins involved in complement regulation such as complement C3 and vitronectin, and those involved in acute-phase response such as PPBP, serum amyloid A protein 2, and protein S100-A8, in both CM-Rs and VLDL-Rs. CONCLUSIONS: We have firstly characterized the proteome of CM-Rs. These findings may provide an explanation for the atherogenic properties of CM-Rs.
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Masuda et al. (2024) conducted an observational in Healthy subjects (n=8). Chylomicron remnants (CM-Rs) vs. VLDL remnants (VLDL-Rs) was evaluated on Identification and relative quantification of CM-R and VLDL-R associated proteins. Proteomic analysis of human chylomicron remnants identified 42 associated proteins, revealing that HDL-associated proteins and apoC-I are significantly more abundant in chylomicron remnants than in VLDL remnants.
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