Lipase bile salt-stimulated,

Mechref, Y., Chen, P, and Novotny, M. V., Structural characterization of the N-linked oligosaccharides in bile salt-stimulated lipase originated from human breast milk, Glycobiology, 9, 227, 1999. 

Warded, J.M., Wright, A.J., Bardsley, W.G. and D Souza, S.W. (1984) Bile salt-stimulated lipase and esterase activity in human milk after collection, storage, and heating nutritional implications. Pediatr. Res. 18, 382-386. 

Hernell, O. 1975. Human milk lipases. III. Physiological implications of the bile-salt stimulated lipase. Eur. J. Clin. Invest. 5, 267. 

Hernell, O. and Olivecrona, T. 1974B. Human milk lipases. II. Bile salt-stimulated lipase. Biochem. Biophys. Acta 369, 234-244. 

Howies, P.N., Carter, C.P., and Hui, D.Y. 1996. Dietary free and esterified cholesterol absorption in cholesterol esterase (bile salt-stimulated lipase) gene-targeted mice. J. Biol. Chem. 271, 7196-7202. 

S. Iverson, C. Kirk, M. Hamosh, and J. Newsome. Milk lipid digestion in the neonatal dog the combined actions of gastric and bile salt stimulated lipases. Bhcflim, Blopkys. Ada J083 109 (1991). 

Bemback, L fiiacabcig, and G. Hcmcli. The compieie digestion of human milk triacylglyccxol In vitro requires gastric lipase, pancreatic colipase-depcndent lipase and bile salt-stimulated lipase. J. Clio. Invest. Jf5 1221 (1990). 

Bernback, S., Blackberg, L., Hernell, O. 1989. The complete digestion of human milk triacyl-glycerol in vitro requires gastric lipase, pancreatic colipase-dependent lipase, and bile salt-stimulated lipase.. / Clin. Invest. 85, 1221-1226. 

Human milk differs from cows milk in that it contains two lipases, a lipoprotein lipase and a bile salt-stimulated lipase. The ability of the latter to cause considerable hydrolysis of ingested milk lipids has important nutritional implications. 

There were several new developments during the 1970s. Of particular importance was the purification and characterization of a lipoprotein lipase (LPL) and the acceptance of the postulate that this was the major, if not the only, lipase in cows milk (Olivecrona, 1980). Similarly, the elucidation of the lipase system in human milk as consisting of an LPL and a bile salt-stimulated lipase, and the possible role of the latter in infant nutrition, were noteworthy (Fredrikzon et al, 1978). Also, microbial lipolysis assumed substantial significance with the widespread use of low-temperature storage of raw milk and the recognition that heat-stable lipases produced by psychrotrophic bacteria were a major cause of flavor problems in stored dairy products (Law, 1979). 

Human milk differs from cows milk in that it contains, in addition to an LPL similar to that in cows milk, a bile salt-stimulated lipase (BSSL), which appears to have no counterpart in cows milk (Hernell and Blackberg, 1994). In addition, a third lipase known as platelet-activating factor acet-ylhydrolase activity (PAF-AH) has been demonstrated in human milk the activity is absent, or extremely low in cows milk (Furukawa, et al., 1994). 

Cows milk LPL has phospholipase Ai activity (Scow and Egelrud, 1976), but its action on milk phospholipids has not been recorded. Freshly secreted goats milk has been shown to have phospholipase A activity (Long and Patton, 1978) but it is not known whether this can be attributed to the LPL of that milk. Human milk contains an acid sphingomylinase C, as well as ceramidase activity provided by the bile salt-stimulated lipase present (Nyberg et al., 1998). 

Other factors. A cow s hormonal balance can affect the susceptibility of her milk to spontaneous lipolysis (Fredeen et al., 1951 Kastli et al., 1967 Bachman et al., 1988). The oestrus cycle appears to have little effect on spontaneous lipolysis (Fredeen et al, 1951) but may affect lipase activity in the milk (Kelly, 1945). In contrast, treatment of cows with oestradiol and progesterone has been shown to lead to increased lipolysis in the milk (Bachman, 1982 Heo, 1983 Bachmann eta/., 1985) but no change (Bachman, 1982) or a transient increase (Bachmann et al., 1985) in total lipase activity. It appears that the increased lipolysis in milk following hormonal treatment, or in milk from cows with ovarian cysts, may not be typical spontaneous lipolysis as cooling is not needed to initiate it (Bachman, 1982) a lipase other than lipoprotein lipase, possibly a bile salt-stimulated lipase, may be responsible for such lipolysis (Heo, 1983 Bachmann et al., 1985). Treatment of cows with bovine somatotropin has been reported to have no significant effect on milk lipoprotein lipase activity (Azzara et al., 1987). 

Blackberg, L., Angquist, K.A., Hernell, O. 1987. Bile salt-stimulated lipase in human milk evidence for its synthesis in the lactating mammary gland. FEBS Letts 217, 37 11. 

Ellis, L.A., Hamosh, M. 1992. Bile salt stimulated lipase comparative studies in ferret milk and lactating mammary gland. Lipids 27, 917-922. 

Freed, L.M., York, C.M., Hamosh, P., Mehta, N.R., Hamosh, M. 1987. Bile salt-stimulated lipase of human milk characteristics of the enzyme in the milk of mothers of premature and full-term infants. J. Pediat. Gastroenterol. Nutr. 6, 598-604. 

Hernell, O. 1985. Specificity of human milk bile salt-stimulated lipase. J. Pediatr. Gastroenterol. Nutr. 4, 517-519. 

Hernell, O., Blackberg, L. 1994. Human milk bile salt-stimulated lipase functional and molecular aspects. J. Pediatr. 125 (Suppl. 2), S56-S61. 

McKillop, A M., O Hare, M.M.T., Craig, J.S., Halliday, H.L. 2004. Characterization of the C-terminal region of molecular forms of human milk bile salt-stimulated lipase. Acta Paediatr. 93, 10-16. 

Swan, J.S., Hoffman, M.M., Lord, M.L., Poechmann, J.L. 1992. Two forms of human milk bile-salt-stimulated lipase. Biochem. J. 283, 119-122. 

Wang, C.-S., Kuksis, A., Manganaro, F., Myher, J.J., Downs, D., Bass, H.B. 1983. Studies on the substrate specificity of purified human milk bile salt-stimulated lipase. J. Biol. Chem. 258, 9197-9202. 

Lipases. Some lipases, especially the bile-salt-stimulated lipases in human milk, destroy the protozoan Giardia Iambiia (58) The free fatty acids are responsible for the action. This was shown by the requirement for incubation of the cream with the skim to develop the inhibitor. Studies with the addition of Giardia to milk (59) showed that preincubation was necessary to get a good kill of the added cells. There was substantially no change in viable count without cholate, whereas with cholate the viable count went to virtually zero over the two hours. 

J.A. Contreras, M. Karlsson, T. Osterlund, H. Laurell, a. Svensson, and C. Holm, Hormone-sensitive lipase is structurally related to acetylcholinesterase, bile salt-stimulated lipase, and several fungal lipases building of a three-dimensional model for the catalytic domain of hormone-sensitive lipase, J. Biol. Chem., 1996, 273, 31426-31430. 

J. Nilsson, L. Blackberg, P. Carlsson, S. Enerback, O. Hemell, and G. Bjursell. cDNA cloning of human-milk bile-salt-stimulated lipase and evidence for its identity to pancreatic carboxylic ester hydrolase. Eur. J. Biochem. 792 543 (1990). 

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