Relationships between bile salts hydrophilicity and phospholipid composition in bile of various animal species

Alvaro, Domenico; Cantàfora, Alfredo; Attili, A.F.; Corradini, Stefano Ginanni; Luca, Chiara De; Minervini, G.; Blase, A. Di; Angélico, M.

doi:10.1016/0305-0491(86)90295-6

Cited by 87 publications

(67 citation statements)

References 16 publications

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“…The predominant (Ͼ95%) biliary phospholipid is PC, while sphingomyelin (SM) is present only in trace amounts in bile. 35 The profile of choline phospholipids secreted by ABCB4 in the presence of NaTC was analyzed by using electrospray ionization mass spectrometry. (Fig.…”

Section: Effects Of Verapamil On Abcb4-mediated Lipidmentioning

confidence: 99%

Bile salt–dependent efflux of cellular phospholipids mediated by ATP binding cassette protein B4

et al. 2007

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Section: Effects Of Verapamil On Abcb4-mediated Lipidmentioning

confidence: 99%

Bile salt–dependent efflux of cellular phospholipids mediated by ATP binding cassette protein B4

et al. 2007

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“…every day (24), mainly the palmitoyl and stearoyl species (25). The brush border of the mucosal cells is rich in sphingolipids and is an additional source of endogenous SM.…”

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confidence: 99%

Absorption and lipoprotein transport of sphingomyelin

Nilsson

Duan

2006

Journal of Lipid Research

227

201

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Dietary sphingomyelin (SM) is hydrolyzed by intestinal alkaline sphingomyelinase and neutral ceramidase to sphingosine, which is absorbed and converted to palmitic acid and acylated into chylomicron triglycerides (TGs). SM digestion is slow and is affected by luminal factors such as bile salt, cholesterol, and other lipids. In the gut, SM and its metabolites may influence TG hydrolysis, cholesterol absorption, lipoprotein formation, and mucosal growth. SM accounts for z20% of the phospholipids in human plasma lipoproteins, of which two-thirds are in LDL and VLDL. It is secreted in chylomicrons and VLDL and transferred into HDL via the ABCA1 transporter. Plasma SM increases after periods of large lipid loads, during suckling, and in type II hypercholesterolemia, cholesterol-fed animals, and apolipoprotein E-deficient mice. SM is thus an important amphiphilic component when plasma lipoprotein pools expand in response to large lipid loads or metabolic abnormalities. It inhibits lipoprotein lipase and LCAT as well as the interaction of lipoproteins with receptors and counteracts LDL oxidation. The turnover of plasma SM is greater than can be accounted for by the turnover of LDL and HDL particles. Some SM must be degraded via receptor-mediated catabolism of chylomicron and VLDL remnants and by scavenger receptor class B type I receptor-mediated transfer into cells. Sphingomyelin (SM) in mammalian cells is colocalized with cholesterol mainly in the plasma membrane and in lysosomal and Golgi membranes. It interacts strongly with cholesterol, and the regulation of SM and cholesterol metabolism are in part coordinated (1, 2). In plasma lipoproteins, SM is the second most abundant polar lipid after phosphatidylcholine (PC). The size of the plasma lipoprotein SM pool in humans is 1-1.5 g, of which approximately two-thirds are in apolipoprotein B (apoB)-containing triglyceride (TG)-rich lipoproteins and LDL. The SM content in most extraneural tissues is 1-2 g/kg. Factors regulating plasma SM concentration have received little attention. It was early shown that the level of SM is increased in hypercholesterolemia and that SM-rich lipoproteins accumulate in arteriosclerotic lesions (3-5). Plasma SM is thus a risk factor for ischemic heart disease (6), and the apoE-deficient (apoE 2/2 ) mouse, which accumulates SM-rich remnant particles in blood (7), has emerged as an important model for studying the role of SM in atherogenesis. The effects of lipoprotein SM in the arterial wall during atherogenesis may be related both to the modification of lipoproteins and to the generation of sphingolipid messengers (i.e., ceramide, ceramide-1-phosphate, sphingosine, and sphingosine-1-phosphate) initiated by SM hydrolysis (8-10). The role of SM metabolites in cell signaling has been the subject of several recent reviews (11)(12)(13)(14)(15)(16). Sphingolipid signals are triggered by numerous stimuli and mediate effects on cell growth and apoptosis and on the activities of inflammatory cells that may be pathogenic as well as protect...

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“…[13][14][15] However, while bile salts clearly influence the overall rate of phospholipid secretion, differences in hydrophobicity provide a very incomplete explanation for selection of particular PC species. 6,[17][18][19] Robins et al suggested that PC hydrophobicity may influence selection, but that differences in acyl chain length appear to play a more important role in the selection process. 16 However, the ability to understand how differences in PC selection might be related to structure is complicated by the close interrelatedness of the independent variables.…”

Section: Discussionmentioning

confidence: 99%

“…Hepatocytes contain substantial amounts of a variety of phospholipid classes, 4,5 but diacylphosphatidylcholines (PC) are by far the predominant class in bile, accounting for more than 95% of secreted phospholipids. 4,6 Not only is the PC class selected for secretion into bile, but certain molecular species of PC appear to be secreted preferentially, because they are more abundant in bile than in liver on a relative molar basis. 4,[7][8][9] The distinctive composition of biliary PC was initially attributed to its origination from a small pool in the liver that was specifically destined for biliary secretion.…”

mentioning

confidence: 99%

“…[9][10][11] It was further postulated that the more hydrophilic PC species were selected for secretion, 12 possibly as a consequence of physical-chemical interactions of bile salts with hepatic membranes. [13][14][15] However, other observations indicate that differences in hydrophobicity provide, at best, an incomplete explanation for PC selection, 6,17,18 and that other factors, such as differences in acyl chain length, may correlate with selection. 16 We used regression analysis to investigate the relationship between PC acyl structure and the ''selection'' of individual molecular species of PC into bile and found that most of the differences in likelihood of secretion are related in a predictable way to differences in PC acyl structure.…”

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Determinants of the selection of phosphatidylcholine molecular species for secretion into bile in the rat

1998

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Certain phosphatidylcholine (PC) molecular species appear to be secreted into bile preferentially, but the mechanism for this selection remains obscure. We used multivariate analysis to examine the relationship between PC structure and the odds of secretion for individual PC species secreted into bile. PC was isolated from Folch extracts of bile and liver from rats, and individual molecular species of PC were quantified with reverse-phase highperformance liquid chromatography (HPLC). The odds of secretion for a given PC species were quantified as the ratio of its mole % in bile/mole % in liver. Regression analysis indicated that the odds of secretion were significantly related to length of both the sn-1 and sn-2 acyl chains (P F .0001 for both) and to relative hydrophobicity as determined by reverse-phase HPLC (P F .0001). In addition, the relationship between odds of secretion and sn-1 chain length was best described by a parabolic function. Considered together, these characteristics accounted for 88% of the observed differences in odds of secretion. This relationship between PC structure and odds of secretion was strikingly similar to the relationship between PC structure and affinity for bovine PC transfer protein. When multivariate models were used to predict both the odds of secretion and the affinity for PC transfer protein for a set of biologically plausible PC species, there was a linear relationship between the two. The likelihood of a given PC species being secreted into bile can be related to the structural characteristics of the acyl chains without having to postulate the existence of a special pool of PC destined for biliary secretion. Second, the structural characteristics that dictate selection of PC species for secretion into bile are similar to those that determine binding affinity for PC transfer protein, suggesting that the likelihood of a PC being secreted into bile is, in fact, closely related to its binding affinity for PC transfer protein (PC-TP). (HEPATOLOGY 1998;28:631-637.)There is abundant evidence that the biliary secretion of bile salts, phospholipids, and cholesterol are intimately linked, [1][2][3]

show abstract

Relationships between bile salts hydrophilicity and phospholipid composition in bile of various animal species

Cited by 87 publications

References 16 publications

Bile salt–dependent efflux of cellular phospholipids mediated by ATP binding cassette protein B4

Bile salt–dependent efflux of cellular phospholipids mediated by ATP binding cassette protein B4

Absorption and lipoprotein transport of sphingomyelin

Determinants of the selection of phosphatidylcholine molecular species for secretion into bile in the rat

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