Two forms of human milk bile-salt-stimulated lipase

Swan, James S.; Hoffman, M. M.; Lord, M.; Poechmann, J L

doi:10.1042/bj2830119

Cited by 27 publications

(12 citation statements)

References 20 publications

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“…Yet another possibility is that the level of circulating CEL in EKO-CEL mice achieved in our study was too low to exert a putative pro-atherogenic effect; we do not favor this explanation, however, because it was comparable to that in rats (16), and in excess of that observed in humans (15,33). …”

Section: Discussioncontrasting

confidence: 72%

“…Plasma CEL activities of EKO and EKO-CEL mice were measured radiometrically by using cholesteryl [1- 14 C] oleate as the substrate. EKO mice (n = 11; 6 male and 5 female) had very low to undetectable plasma CEL activity (0.5 ± 0.1 nm FA/h.ml plasma), whereas EKO-CEL mice (n = 14; 7 male and 7 female) had an activity of 50.1 ± 11.8 nmole FA/h.ml plasma, which is comparable to that found in rats (30 ∼ 90 nmole FA/h.ml plasma) (16) and about four-fold higher than that in human plasma (∼ 12 nmole FA/h.ml plasma) (15,33). These relative CEL activities among different species were also confirmed by assaying CEL activities in plasma samples from wild-type mice, EKO mice, EKO-CEL mice, rats, and humans in parallel in our laboratory.…”

Section: Resultssupporting

confidence: 53%

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Plasma carboxyl ester lipase activity modulates apolipoprotein B–containing lipoprotein metabolism in a transgenic mouse model

Weng

Harrison

et al. 2008

Metabolism

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Pancreatic carboxyl ester lipase (CEL) is in the plasma of many mammals, including humans and rats, but not mice. In vitro, CEL hydrolyzes cholesterol esters (CE) of apoB-containing lipoproteins (apoB-Lp). To study the effect of CEL on metabolism of apoB-Lp and atherosclerosis in vivo, apoEknockout (EKO) mice, which have high plasma levels of apoB-Lp and are prone to atherosclerosis, were made to secrete CEL into plasma by introducing a transgene containing a liver-specific promoter and rat CEL cDNA. Plasma CEL activity in EKO-CEL mice was comparable to that found in rats. Evidence of modification of apoB-Lp by plasma CEL in vivo was an increase in the free cholesterol:CE ratio of apoB-Lp from mice on chow or a Western-type diet. In addition, plasma total cholesterol levels were elevated in EKO-CEL mice, with the elevation found exclusively in the apoBLp fraction. Associated with the increase in steady-state apoB-Lp levels was an increase in the plasma half life of very low density lipoproteins (VLDL) in EKO-CEL mice, measured by the clearance rate of injected VLDL. Interestingly, in spite of the increase of apoB-lipoproteins, the atherosclerotic lesion did not differ between EKO and EKO-CEL mice on a Western-type diet. In summary, our results demonstrate that plasma CEL modulates apoB-Lp metabolism in vivo, resulting in reduced VLDL clearance and elevated plasma cholesterol levels.

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Section: Discussioncontrasting

confidence: 72%

Section: Resultssupporting

confidence: 53%

Plasma carboxyl ester lipase activity modulates apolipoprotein B–containing lipoprotein metabolism in a transgenic mouse model

Weng

Harrison

et al. 2008

Metabolism

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“…Two molecular forms (high and low M, forms) of human milk BSDL, which is very similar to the pancreatic BSDL [S], have been described [33]. These forms were present in milk of some subjects only, and the expression of codominant alleles was suggested as a possible explanation for this observation [33]. No further characterization was carried out on these two forms of milk BSDL.…”

Section: Discussionmentioning

confidence: 99%

Investigation of Two Glycosylated Forms of Bile‐Salt‐Dependent Lipase in Human Pancreatic Juice

Mas¹,

Franc²,

Lecestre³

et al. 1997

European Journal of Biochemistry

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Pure human pancreatic bile-salt-dependent lipase, devoid of its oncofetal glycoform [Mas, E., Abouakil, N., Roudani, S., Miralles, F., Guy-Crotte, O., Figarella, C., Escribano, M. J. & Lombardo, D.(1993) Biochem. J. 289, 609-6151, was analyzed on immobilized concanavalin A (ConA). Two variants were separated : an unabsorbed ConA-unreactive fraction ; and an absorbed ConA-reactive fraction. Carbohydrate compositions of ConA-reactive and ConA-unreactive fractions were not significantly different, and analysis of 'H-labelled oligosaccharides liberated from these fractions on the ConA-Sepharose column indicated that the fractionation of the bile-salt-dependent lipase on this column depends upon oligosaccharide structures. The activity of the ConA-reactive fraction was however much lower, independent of the substrate (4-nitrophenyl hexanoate or cholesteryl esters), than that of the ConA-unreactive fraction. Therefore, catalytic constants for the hydrolysis of 4-nitrophenyl hexanoate were determined; both fractions had quite similar K,,, while the k,,, for the ConA-unreactive fraction was 3-4-fold higher than that of the ConA-reactive fraction. ConA-reactive and ConA-unreactive fractions were shown to have slightly different molecular masses and different amino acid compositions. Cleavage patterns after cyanogen bromide treatment of the ConA-reactive and ConA-unreactive fractions suggested that the ConA-reactive (high M , form) and ConA-unreactive (low M , form) forms could be different isoforms of the bile-saltdependent lipase secreted by the human pancreas.Keywords: bile-salt-dependent lipase; human pancreatic juice ; concanavalin A ; feto-acinar pancreatic protein; glycoform.Bile-salt-dependent lipase (BSDL ; also referred to as carboxylic ester hydrolase or carboxyl ester lipase) catalyzes the hydrolysis of lipid-ester substrates and is the only enzyme of the pancreatic juice capable of hydrolyzing fat-soluble vitamin esters (reviewed in [l-31). This enzyme is found in all examined species [l-41. Moreover the enzyme is also present in milk of some primates (51 and carnivore [6]. The enzyme is a prerequisite for full absorption of cholesterol and vitamins. Because of this important physiological role, studies of factors regulating the activity of BSDL are of great interest. Whatever their origin, BSDL are glycosylated and have an N-glycosylation site at As11187 [7], which is close to Ser194, which is involved in the active site [8]. Previous data indicated that the transfer en bloc of the oligosaccharide precursor to the nascent BSDL is essential for the correct folding of the enzyme and is required for its secretion [9]. In contrast, based on results obtained by site-di- is unclear [12]. In BSDL, 0-linked structures hypothetically mask PEST sequences [13] present on the tandemly repeated sequences [14]. These PEST sequences participate in targeting cell proteins into a degradative pathway [14].We have previously isolated an oncofetal glycoform of BSDL [I 51, further identified as the feto-acinar pancreatic protein...

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“…Originally discovered in milk of humans and various other primates (Swan & al., 1992), BSSL participates to the intestinal digestion of dietary lipids (Table 2). While colipase-dependent pancreatic lipase facilitates the uptake of fatty acids, bile-salt-stimulated lipase facilitates the uptake of free cholesterol from the intestinal lumen (Sahasrabudhe & al., 1998).…”

Section: Enzyme Name Substrate Specificity Referencesmentioning

confidence: 99%

Emerging Approaches for the Treatment of Fat Malabsorption Due to Exocrine Pancreatic Insufficiency

Turki¹,

Kallel²

2012

New Advances in the Basic and Clinical Gastroenterology

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Two forms of human milk bile-salt-stimulated lipase

Cited by 27 publications

References 20 publications

Plasma carboxyl ester lipase activity modulates apolipoprotein B–containing lipoprotein metabolism in a transgenic mouse model

Plasma carboxyl ester lipase activity modulates apolipoprotein B–containing lipoprotein metabolism in a transgenic mouse model

Investigation of Two Glycosylated Forms of Bile‐Salt‐Dependent Lipase in Human Pancreatic Juice

Emerging Approaches for the Treatment of Fat Malabsorption Due to Exocrine Pancreatic Insufficiency

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