Lipoprotein lipase (LpL) on the surface of cardiomyocytes increases lipid uptake and produces a cardiomyopathy
J. Clin. Invest. Hiroaki Yagyu, et al. 111:419 doi:10.1172/JCI16751 [Go to this article.]

Figure 8
Mechanisms of LpL mediated lipid uptake from TG-rich particles in the heart. (a) Cardiomyocytes express LpL that dissociates from the cell surface and migrates to the luminal surface of capillary endothelial cells. At this location, LpL attaches to heparan sulfate proteoglycans (HSPG) and is able to interact with circulating TGRP. FFAs are released that cross the endothelial barrier and are acquired by myocytes. (b) Our studies show that LpL associated with the cardiomyocyte surface, in this case via a GPI anchor, also promotes lipid uptake. For this to occur, some TGRP, perhaps lipoproteins that are partially digested by endothelial-associated LpL, must exit the vasculature, enter the subendothelial space, and directly interact with cardiomyocytes. It should be noted that LpL is found on both endothelial and cardiomyocyte surfaces. Thus, the LpL-mediated interactions shown in both a and b are likely to occur in the hLpL^GPI mice and may play a role in normal physiology.