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  • 1.
    Andersson, Eva-Lotta
    et al.
    Umeå universitet, Medicinska fakulteten, Institutionen för klinisk vetenskap, Pediatrik.
    Hernell, Olle
    Umeå universitet, Medicinska fakulteten, Institutionen för klinisk vetenskap, Pediatrik.
    Bläckberg, Lars
    Umeå universitet, Medicinska fakulteten, Institutionen för medicinsk biovetenskap, Fysiologisk kemi.
    Fält, Helen
    Umeå universitet, Medicinska fakulteten, Institutionen för klinisk vetenskap, Pediatrik.
    Lindquist, Susanne
    Umeå universitet, Medicinska fakulteten, Institutionen för klinisk vetenskap, Pediatrik.
    Bile salt-stimulated lipase and pancreatic lipase-related protein 2: key enzymes for lipid digestion in the newborn examined using the Caco-2 cell line2011Ingår i: Journal of Lipid Research, ISSN 0022-2275, E-ISSN 1539-7262, Vol. 52, nr 11, s. 1949-1956Artikel i tidskrift (Refereegranskat)
    Abstract [en]

    In rodents, bile salt-stimulated lipase (BSSL) and pancreatic lipase-related protein 2 (PLRP2) are the dominant lipases expressed in the exocrine pancreas in early life, when milk is the main food. The aim of the present study was to evaluate if BSSL and PLRP2 are also key enzymes in neonatal intestinal fat digestion. Using Caco-2 cells as a model for the small intestinal epithelium, purified human enzymes were incubated in the apical chamber with substrates and bile salt concentrations resembling the milieu of the small intestine of newborn infants. BSSL and PLRP2 hydrolyzed triglycerides (TG) to free fatty acids (FA) and glycerol. The cells took up the FA, which were reesterfied to TG. Together, BSSL and PLRP2 have a synergistic effect, increasing cellular uptake 4-fold compared to the sum of each lipase alone. A synergistic effect was also observed with retinyl ester as a substrate. PLRP2 hydrolyzed cholesteryl ester but not as efficiently as BSSL, and the two had an additive rather than synergistic effect. We conclude the key enzymes in intestinal fat digestion are different in newborns than later in life. Further studies are needed to fully understand this difference and its implication for designing optimal neonatal nutrition.

  • 2.
    Andersson, Y
    et al.
    Umeå universitet, Medicinsk fakultet, Klinisk vetenskap, Pediatrik.
    Sävman, K
    Bläckberg, L
    Hernell, O
    Umeå universitet, Medicinsk fakultet, Klinisk vetenskap, Pediatrik.
    Pasteurization of mother's own milk reduces fat absorption and growth in preterm infants.2007Ingår i: Acta paediatrica, ISSN 0803-5253, Vol. 96, nr 10, s. 1445-9Artikel i tidskrift (Refereegranskat)
    Abstract [en]

    Aim: A randomized study was conducted to evaluate whether pasteurized milk (Holder pasteurization 62.5 degrees C, 30 min) reduces fat absorption and growth in preterm infants. Methods: Preterm infants (825-1325 g) born with gestational age </=30 weeks were randomized into two groups, of which one started with pasteurized own mother's milk for 1 week and continued with raw milk the following week, and a second group was fed in reverse order. By using this design the infants served as their own controls. At the end of each week, a 72-h fat balance was performed and growth was monitored. Results: We found, on an average, 17% higher fat absorption with raw as compared to pasteurized milk. Infants gained more weight and linear growth assessed as knee-heel length was also greater during the week they were fed raw milk as compared to the week they were fed pasteurized milk. Conclusion: Feeding preterm infants pasteurized as compared to raw own mother's milk reduced fat absorption. When the infants were fed raw milk, they gained more in knee-heel length compared to when they were fed pasteurized milk.

  • 3.
    Blind, Per Jonas
    et al.
    Umeå universitet, Medicinska fakulteten, Institutionen för kirurgisk och perioperativ vetenskap, Kirurgi.
    Bläckberg, Lars
    Umeå universitet, Medicinska fakulteten, Institutionen för medicinsk biovetenskap, Fysiologisk kemi.
    Hernell, Olle
    Umeå universitet, Medicinska fakulteten, Institutionen för klinisk vetenskap, Pediatrik.
    Ljungberg, Börje
    Umeå universitet, Medicinska fakulteten, Institutionen för kirurgisk och perioperativ vetenskap, Urologi och andrologi.
    Carboxylic ester hydrolase: a serum marker of acute pancreatitis1987Ingår i: Pancreas, ISSN 0885-3177, E-ISSN 1536-4828, Vol. 2, nr 5, s. 597-603Artikel i tidskrift (Refereegranskat)
    Abstract [en]

    By use of an enzyme-linked immunosorbent assay we established serum reference values of carboxylic ester hydrolase, a pancreatic secretory lipolytic enzyme, and explored to see if a raised serum level is indicative of acute pancreatitis. Postoperative elevation of carboxylic ester hydrolase was observed in seven out of ten patients who underwent pancreatic surgery. Serum levels of carboxylic ester hydrolase and amylase were determined in 129 patients admitted due to abdominal emergency conditions. Amylase was elevated in 27 patients, and in 20 of these raised carboxylic ester hydrolase levels affirmed the diagnosis acute pancreatitis. In five out of the seven patients with elevated amylase alone no etiologic factor of acute pancreatitis was found. Another 11 patients had raised carboxylic ester hydrolase levels without concomitant elevation of amylase. In all these patients, a likely cause of pancreatic inflammation was identifiable. Hence, a raised carboxylic ester hydrolase level, even in presence of normal amylase, could be indicative of acute pancreatic inflammation.

  • 4. Blind, Per-Jonas
    et al.
    Büchler, M
    Bläckberg, Lars
    Umeå universitet, Medicinska fakulteten, Institutionen för medicinsk biovetenskap, Fysiologisk kemi.
    Andersson, Yvonne
    Umeå universitet, Medicinska fakulteten, Institutionen för klinisk vetenskap, Pediatrik.
    Uhl, W
    Beger, H G
    Hernell, Olle
    Umeå universitet, Medicinska fakulteten, Institutionen för klinisk vetenskap, Pediatrik.
    Carboxylic ester hydrolase. A sensitive serum marker and indicator of severity of acute pancreatitis.1991Ingår i: International journal of Pancreatology, ISSN 0169-4197, Vol. 8, nr 1, s. 65-73Artikel i tidskrift (Refereegranskat)
    Abstract [en]

    When using clinical criteria, both falsely positive and falsely negative diagnoses of acute pancreatitis (AP) are often made. Based on a clinical study, elevated serum levels of the pancreatic lipolytic enzyme carboxylic ester hydrolase (CEH) was recently suggested to be a highly specific marker of acute pancreatitis. To determine the sensitivity of the test for AP, a study on patients with the diagnosis set objectively was necessary. In the present study, AP was diagnosed by contrast-enhanced computed tomography in 64 patients, and histopathological examination of tissue removed at laparotomy in 18 of them. By these criteria, 42 patients suffered from acute interstitial pancreatitis (AIP), and 22 patients from necrotizing pancreatitis (NP). Based on the CEH concentrations in the first serum sample obtained in each patient, the sensitivity of CEH for pancreatitis was 98%. From the second day after admission, CEH levels in patients with NP were significantly higher than in patients with AIP. Furthermore, in patients with NP, CEH values remained at a raised level for the following 10 d, whereas a significant decrease of CEH values was noted in patients with AIP. In contrast, total serum amylase activities were higher in patients suffering of AIP than in patients suffering of NP during the observation period. We conclude, that the sensitivity of the CEH test is very high for AP. CEH concentrations remaining at a high level are suggestive of NP, whereas diminishing CEH levels are suggestive of AIP.

  • 5.
    Bläckberg, Lars
    Umeå universitet, Medicinska fakulteten, Institutionen för medicinsk biovetenskap, Fysiologisk kemi.
    Fat digestion in the newborn infant: with special reference to the bile salt-stimulated lipase and the milk fat globule1981Doktorsavhandling, sammanläggning (Övrigt vetenskapligt)
  • 6.
    Bläckberg, Lars
    et al.
    Umeå universitet, Medicinska fakulteten, Institutionen för medicinsk biovetenskap.
    Hernell, Olle
    Umeå universitet, Medicinska fakulteten, Institutionen för klinisk vetenskap, Pediatrik.
    Bile salt-stimulated lipase in human milk. Evidence that bile salt induces lipid binding and activation via binding to different sites.1993Ingår i: FEBS Letters, ISSN 0014-5793, E-ISSN 1873-3468, Vol. 323, nr 3, s. 207-210Artikel i tidskrift (Refereegranskat)
    Abstract [en]

    Human milk bile salt-stimulated lipase ensures efficient triacylglycerol utilization in breast-fed newborns. For activity against long-chain triacylglycerol, primary bile salts are a prerequisite. Bile salts also protect the enzyme from inactivation by intestinal proteases. We have studied the effect of different bile salts on activation, protease protection, lipid binding, and enzyme inactivation, caused by an arginine modifying agent. Based on the results we propose a model involving two bile salt binding sites; one activation-site specific for primary bile salt, and another, less specific, lipid binding promoting site at which also secondary bile salt binds. Binding to this latter site induces binding of enzyme to emulsified substrates but binding promoting site at which also secondary bile salt binds. Binding to this latter site induces binding of enzyme to emulsified substrates but without subsequent lipolysis.

  • 7.
    Bläckberg, Lars
    et al.
    Umeå universitet, Medicinska fakulteten, Institutionen för medicinsk biovetenskap.
    Hernell, Olle
    Umeå universitet, Medicinska fakulteten, Institutionen för klinisk vetenskap, Pediatrik.
    Further characterization of the bile salt-stimulated lipase in human milk1983Ingår i: FEBS Letters, ISSN 0014-5793, E-ISSN 1873-3468, Vol. 157, nr 2, s. 337-341Artikel i tidskrift (Refereegranskat)
    Abstract [en]

    Bile salt-stimulated lipase is a milk enzyme unique to the higher primates. Its molecular and kinetic characteristics differ greatly from other lipolytic enzymes; e.g., pancreatic lipase and lipoprotein lipase. It has a much higher app. Mr, 310000 on gel filtration and 100000 after denaturation. It requires primary bile salts for optimal activity and bile salts also protect the enzyme from proteolytic and heat inactivation. It may, due to its low substrate specificity, contribute to the utilization of a variety of milk lipids. Since it lacks positional specificity, digestion of milk triglycerides should be complete, which may explain why fat absorption is more efficient in breast-fed than in formula-fed infants.

  • 8.
    Hernell, Olle
    et al.
    Umeå universitet, Medicinska fakulteten, Institutionen för klinisk vetenskap, Pediatrik.
    Bläckberg, Lars
    Umeå universitet, Medicinska fakulteten, Institutionen för medicinsk biovetenskap, Fysiologisk kemi.
    Bernbäck, S
    Digestion of human milk fat in early infancy1989Ingår i: Acta paediatrica Scandinavica. Supplement, ISSN 0300-8843, Vol. 351, s. 57-62Artikel i tidskrift (Refereegranskat)
  • 9.
    Hernell, Olle
    et al.
    Umeå universitet, Medicinska fakulteten, Institutionen för klinisk vetenskap, Pediatrik.
    Bläckberg, Lars
    Umeå universitet, Medicinska fakulteten, Institutionen för medicinsk biovetenskap.
    Chen, Q
    Sternby, B
    Nilsson, A
    Does the bile salt-stimulated lipase of human milk have a role in the use of the milk long-chain polyunsaturated fatty acids?1993Ingår i: Journal of Pediatric Gastroenterology and Nutrition - JPGN, ISSN 0277-2116, E-ISSN 1536-4801, Vol. 16, nr 4, s. 426-431Artikel i tidskrift (Refereegranskat)
    Abstract [en]

    Long-chain polyunsaturated (LCP) fatty acids derived from linoleic (18:2 n-6) and alpha-linolenic (18:3 n-3) acids are considered essential nutrients in preterm infants. The efficiency by which such fatty acids are released as absorbable products from triacylglycerol was explored in vitro using rat chylomicron triacylglycerol as substrate. When incubated with purified human pancreatic colipase-dependent lipase and colipase, arachidonic acid (20:4 n-6) was released less efficiently than linoleic acid from such triacylglycerol. This difference was not seen when purified human milk bile salt-stimulated lipase (BSSL) was incubated with the triacylglycerol substrate, and it was almost abolished when colipase-dependent lipase (with colipase) and BSSL acted simultaneously, as they do in breast-fed infants. There was no difference in arachidonic acid and eicosapentaenoic acid (20:5 n-3) release rates with either colipase-dependent lipase or BSSL, albeit the release was more rapid with the milk enzyme than with colipase-dependent lipase. Again, the most efficient release as absorbable free fatty acids was achieved when the two lipases operated together. The relative resistance to hydrolysis of arachidonic acid and eicosapentaenoic acid by colipase-dependent lipase was best explained by the localization of the first double bond to the delta-5 position of the respective fatty acid. The results obtained suggest that BSSL is of importance for the efficient use of human milk LCP fatty acids.

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