Binding of HDL to basolateral membranes of the renal cortex. Evidence for two components in the HDL-membrane association

Senault, Claude; Vacher, D; Sakr, Sana W.; Girard-Globa, Anik

doi:10.1016/0005-2736(94)90062-0

Cited by 4 publications

(2 citation statements)

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“…van Tol and colleagues [14] have identified a low-affinity non-saturating and a high-affinity saturating rat HDL binding to partially purified rat kidney membranes or kidney homogenates. Senault and co-workers [25] have described a two-component association of porcine 125 I-HDL with basolateral membranes of the porcine renal cortex; a high-affinity, lower-capacity interaction associated with a 95 kDa receptor and a low-affinity, highercapacity interaction that appeared to be a non-specific lipid-lipid interaction. Kozyraki and co-workers [9] identified a high-affinity interaction between human 125 I-HDL and cubilin, a 460 kDa receptor purified from the human as well as the rabbit renal cortex.…”

Section: Discussionmentioning

confidence: 99%

“…Competitive binding assays showed that 125 I-HDL can efficiently bind to the HKC-8 cells, as evident from the saturable and high specific-binding component of the total 125 I-HDL cell association. Several laboratories have demonstrated 125 I-HDL binding to the membranes of the renal cortex in various species, including those of rat, porcine and human origin [9,14,25]. However, the findings in these studies differ enough to suggest that more than one HDL-binding receptor may be present in the kidneys.…”

Section: Discussionmentioning

confidence: 99%

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The lipid composition of high-density lipoprotein affects its re-absorption in the kidney by proximal tubule epithelial cells

Breznan

VEERESWARAN

VIAU

et al. 2004

Biochemical Journal

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The kidney is believed to play a major role in the clearance of apoA-I (apolipoprotein A-I) and HDL (high-density lipoprotein) particles from the bloodstream. Proximal tubule epithelial cells of the kidney appear to prevent the loss of these proteins in the urine by re-absorbing them from the urinary filtrate. Experiments were undertaken to investigate the factors that regulate the renal re-absorption of apoA-I and small HDL in a transformed human proximal tubule epithelial (HKC-8) cell line. Fluorescent microscopic studies show that HKC-8 cells can readily bind and take up HDL particles. Intracellular localization of fluorescently labelled native HDL shows its accumulation in endocytotic vesicles, in a perinuclear region after 1 h. Binding studies reveal a saturable cell association of (125)I-HDL with the HKC-8 cell surface after 2 h. HKC-8 cells do not degrade apoA-I or other HDL-apoproteins. The specific cell association of lipid-free apoA-I is approx. 2-fold less than that observed for native HDL. Similarly, reconstituted HDL prepared from HDL-apoproteins and pure phospholipids also exhibits a low cell association with the HKC-8 cells. In contrast, reconstituted HDL prepared with the extracted lipids of HDL and pure apoA-I exhibits an even higher cell association than that observed with the native lipoprotein. A detailed characterization of the major lipid classes in reconstituted HDL shows that only cholesteryl ester increases the cell association of the recombinant particles. These results show that the cholesteryl ester content of HDL may play an important role in the re-absorptive salvage of HDL by the proximal tubule cells of the kidney.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%