Determinants of the selection of phosphatidylcholine molecular species for secretion into bile in the rat.
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 high-performance 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 < .0001 for both) and to relative hydrophobicity as determined by reverse-phase HPLC (P < .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).
LaMorte
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Department of Surgery, Boston University Medical Center, MA, USA.
Booker
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ML
Kay
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D000727:Androgen-Binding Protein; D000818:Animals; D001646:Bile / Q000378:metabolism*; D002352:Carrier Proteins / Q000378:metabolism; D015999:Multivariate Analysis; D010713:Phosphatidylcholines / Q000737:chemistry / Q000378:metabolism*; D049294:Phospholipid Transfer Proteins; D060789:Prostatein; D051381:Rats; D017207:Rats, Sprague-Dawley; D012044:Regression Analysis; D060765:Secretoglobins; D014598:Uteroglobin; D060788:Mammaglobin B
D000727:Androgen-Binding Protein; D002352:Carrier Proteins; D010713:Phosphatidylcholines; D049294:Phospholipid Transfer Proteins; D060789:Prostatein; D060765:Secretoglobins; D014598:Uteroglobin; C511484:Scgb1d2 protein, rat; C511483:Scgb1d4 protein, rat; C556468:Scgb2a1 protein, rat; D060788:Mammaglobin B