Transporting mitochondrion-targeting photosensitizers into cancer cells by low-density lipoproteins for fluorescence-feedback photodynamic therapy

Nanoscale ◽  
2021 ◽  
Author(s):  
Chao Wang ◽  
Xianhao Zhao ◽  
Haoyu Jiang ◽  
Jiaxin Wang ◽  
Weixiu Zhong ◽  
...  

Low-density lipoproteins (LDLs) reconstituted with a multifunctional mitochondrion-targeting photosensitizer are able to achieve fluorescence-feedback photodynamic therapy of LDL receptor-overexpressing cancer cells.

1999 ◽  
Vol 77 (2) ◽  
pp. 157-163 ◽  
Author(s):  
Louise Brissette ◽  
Marie-Claude Charest ◽  
Louise Falstrault ◽  
Julie Lafond ◽  
David Rhainds ◽  
...  

Selective uptake of cholesteryl esters (CE) from lipoproteins by cells has been extensively studied with high density lipoproteins (HDL). It is only recently that such a mechanism has been attributed to intermediate and low density lipoproteins (IDL and LDL). Here, we compare the association of proteins and CE from very low density lipoproteins (VLDL), IDL, LDL and HDL3 to HepG2 cells. These lipoproteins were either labelled in proteins with 125I or in CE with 3H-cholesteryl oleate. We show that, at any lipoprotein concentration, protein association to the cells is significantly smaller for IDL, LDL, and HDL3 than CE association, but not for VLDL. At a concentration of 20 µg lipoprotein/mL, these associations reveal CE-selective uptake in the order of 2-, 4-, and 11-fold for IDL, LDL, and HDL3, respectively. These studies reveal that LDL and HDL3 are good selective donors of CE to HepG2 cells, while IDL is a poor donor and VLDL is not a donor. A significant inverse correlation (r2 = 0.973) was found between the total lipid/protein ratios of the four classes of lipoproteins and the extent of CE-selective uptake by HepG2 cells. The fate of 3H-CE of the two best CE donors (LDL and HDL3) was followed in HepG2 cells after 3 h of incubation. Cells were shown to hydrolyze approximately 25% of the 3H-CE of both lipoproteins. However, when the cells were treated with 100 µM of chloroquine, a lysosomotropic agent, 85 and 40% of 3H-CE hydrolysis was lost for LDL and HDL3, respectively. The fate of LDL and HDL3-CE in HepG2 cells deficient in LDL-receptor was found to be the same, indicating that the portion of CE hydrolysis sensitive to chloroquine is not significantly linked to LDL-receptor activity. Thus, in HepG2 cells, the magnitude of CE-selective uptake is inversely correlated with the total lipid/protein ratios of the lipoproteins and CE-selective uptake from the two best CE donors (LDL and HDL3) appears to follow different pathways.Key words: lipoprotein, receptor, HepG2 cell, selective uptake, lipid, cholesterol, binding.


2016 ◽  
Vol 510 (1) ◽  
pp. 240-249 ◽  
Author(s):  
Nathalia Luiza Andreazza ◽  
Christine Vevert-Bizet ◽  
Geneviève Bourg-Heckly ◽  
Franck Sureau ◽  
Marcos José Salvador ◽  
...  

2004 ◽  
Vol 10 (24) ◽  
pp. 8275-8283 ◽  
Author(s):  
Iris J. Edwards ◽  
Isabelle M. Berquin ◽  
Haiguo Sun ◽  
Joseph T. O’Flaherty ◽  
Larry W. Daniel ◽  
...  

1984 ◽  
Vol 218 (1) ◽  
pp. 101-111 ◽  
Author(s):  
A K Soutar ◽  
B L Knight

Human blood monocyte-derived macrophages that had been cultured in medium containing human serum for 7 days degraded the abnormal very-low-density lipoproteins (VLDL) from the plasma of subjects with type III hyperlipoproteinaemia by two distinct saturable processes. One process was stimulated when cells from normal subjects were preincubated with lipoprotein-free medium, was inhibited by excess unlabelled low-density lipoproteins (LDL) and was absent from cells from subjects with homozygous familial hypercholesterolaemia; on these criteria it was identified as an LDL-receptor-dependent process. Degradation by the second process was of equal magnitude in both cell types and was unaffected by excess unlabelled LDL or acetylated LDL. The activity of this process was reduced when the cells were preincubated in lipoprotein-free medium. The abnormal VLDL from the plasma of cholesterol-fed rabbits were also degraded by this process, which was similar to that in mouse peritoneal macrophages mediated by the receptor for VLDL of beta-electrophoretic mobility [Goldstein, Ho, Brown, Innerarity & Mahley (1980) J. Biol. Chem. 255, 1839-1848].


2017 ◽  
Vol 56 (35) ◽  
pp. 10399-10402 ◽  
Author(s):  
Chunlei Zhu ◽  
Pallab Pradhan ◽  
Da Huo ◽  
Jiajia Xue ◽  
Song Shen ◽  
...  

2011 ◽  
Vol 2011 ◽  
pp. 1-10 ◽  
Author(s):  
Fatemeh Moheimani ◽  
Joanne T. M. Tan ◽  
Bronwyn E. Brown ◽  
Alison K. Heather ◽  
David M. van Reyk ◽  
...  

During atherosclerosis monocyte-derived macrophages accumulate cholesteryl esters from low-density lipoproteins (LDLs) via lectin-like oxidised LDL receptor-1 (LOX-1) and class AI and AII (SR-AI, SR-AII) and class B (SR-BI, CD36) scavenger receptors. Here we examined the hypothesis that hyperglycaemia may modulate receptor expression and hence lipid accumulation in macrophages. Human monocytes were matured into macrophages in 30 versus 5 mM glucose and receptor expression and lipid accumulation quantified. High glucose elevated LOX1 mRNA, but decreased SR-AI, SR-BI, LDLR, and CD36 mRNA. SR-BI and CD36 protein levels were decreased. Normo- and hyperglycaemic cells accumulated cholesteryl esters from modified LDL to a greater extent than control LDL, but total and individual cholesteryl ester accumulation was not affected by glucose levels. It is concluded that, whilst macrophage scavenger receptor mRNA and protein levels can be modulated by high glucose, these are not key factors in lipid accumulation by human macrophages under the conditions examined.


2005 ◽  
Vol 386 (5) ◽  
Author(s):  
Alexander D. Dergunov ◽  
Alexey V. Novoselov ◽  
Sophie Visvikis ◽  
Gerard Siest ◽  
Vladimir V. Yakushkin ◽  
...  

1985 ◽  
Vol 79 (1) ◽  
pp. 317-325
Author(s):  
J. Gaffney ◽  
D. West ◽  
F. Arnold ◽  
A. Sattar ◽  
S. Kumar

Acetylated low density lipoprotein (Ac-LDL) is taken up by bovine aortic and adrenal capillary cells but not by brain capillary cells. This indicates that the uptake of Ac-LDL is not a feature of all types of endothelial cell. A quantitative examination of lipoprotein uptake by flow cytometry showed cells in G2M took up 45% more Ac-LDL than those in G1S. Compared with confluent cultures, sub-confluent bovine aortic cells took up three times as much LDL but Ac-LDL uptake was increased by only 34%. This indicates that the Ac-LDL receptor is not down-regulated to the same extent as that for LDL.


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