Pancreatic lipase colipase and

Borgstrom, B. (1975) On the interactions between pancreatic lipase and colipase and the substrate, and the importance of bile salts. ). Lipids Res. 16, 411-417... 

Borgstrom, B. and Erlanson-Albert-son, C. (1973) Pancreatic lipase and colipase. Interactions and effects of bile salts and other detergents. Eur. J. Biochem. 

Chapus, C., Rovery, M., Sarda, L. and Verger, R. (1988) Minireview on pancreatic lipase and colipase. Biochirnie 70, 1223-1234... 

C. Chapus, M. Rovery, L. Sarda, and R. Verger. Minireview on pancreatic lipase and colipase. Biochimie 70 1223-1234 (1988). 

J, S, Patton, P, A. Albertsson, C. Erlanson. B, Borstrom. Binding of porcine pancreatic lipase and colipase in the absence of substrate studied by 2-phase partition and affinity cfiromaiography. J Biol Chem 253 4195-4202. 1978. 

Lowe, M.E. 1999. Assays for pancreatic triglyceride lipase and colipase. In Methods in Molecular Biology, Vol. 109 Lipase and Phospholipase Protocols (M.H. Doolittle and K. Reue, eds.) pp. 59-70. Humana Press, Totowa, N.J. 

The last point has been demonstrated in several contexts, most notably in protein kinase C [109, 110] and phospholipases [111-113], in coupling of G-proteins to their receptors [114], and in the activation of pancreatic lipase by colipase [115]. 

Larsson A and Erlansonalbertsson C. The Effect of Pancreatic Procolipase and Colipase on Pancreatic Lipase Activation. Biochim Biophys Acta 1991 1083 283-288. 

Figure 10 (Left) The rates of hydrolysis of emulsified long-chain triglycerides by pancreatic lipase. The highest rate occurs with triglycerides emulsified with gum arabic (no lecithin). All the other curves represent hydrolysis rates of triglycerides emulsified with long-chain lecithin. There is a long lag period and then a slight hydrolysis in the absence of additives. With added bile salts, the lag period is abolished, but the hydrolysis rates ate still low. Both colipase and colipase plus bile salts accelerate the hydrolytic rates. (Right) Concerted action of pancreatic lipase and phospholipase. Addition of phospholipase A2 hydrolyzes the phospholipid emulsifier (as indicated by the lysolecithin release), stops the lag phase, and initiates an accelerated triglyceride hydrolysis. (From Ref. 35.)...

Several enzymes involved in fat digestion act in the small intestine. These include the pancreatic enzymes lipase (and colipase), phospholipase A2, and... 

Patton, J.S. and Carey, M.C. 1981. Inhibition of human pancreatic lipase-colipase activity by mixed bile salt-phospholipid micelles. Am. J. Physiol. 241, G328-G336. 

Young, S.C. and Hui, D.Y. 1999. Pancreatic lipase/colipase-mediated triacylglycerol hydrolysis is required for cholesterol transport from lipid emulsions to intestinal cells. Biochem. J. 339,... 

As illustrated in Figure 2, human pancreatic lipase consists of two domains. The larger N-terminal domain, a mixed 0E,P-stmcture, comprises residues 1-335 and contains the catalytic triad and a calcium-banding site. The smaller C-terminal domain is formed by two layers of antiparallel -strands and presents a binding site for colipase. 

It is dear that the interconnection between the activities of the different lipolytic enzymes, where the first enzyme modifies the physicochemical state of the lipid substrate in such a way that it becomes available to another enzyme, is not only of prime importance for lipid digestion, but also results in a broad synergism between gastric lipase, colipase, pancreatic lipase, phospholipase As. calcium, caiboxylester Lipase, bite salts, and substrate interraecK tes [55,62-64]. 

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). 

The pancreas produces several lipases, the classical lipase (pancreatic lipase, PL) and the pancreatic lipase-related proteins 1 (PLRP1) and 2 (PLRP2). In addition there is a protein named colipase, which is necessary for the activity of PL. PLRP1 seems to be devoid of lipase activity, while PLRP2... 

Dietary triglycerides are hydrolyzed in the small intestine by pancreatic lipase. This enzyme action is associated with a cofactor, colipase, also a pancreatic protein, molecular weight (MW) 12,000, which helps to anchor lipase to the fat droplets. Without colipase, lipase is rapidly denatured. Colipase is apparently secreted by the pancreas as a zymogen and is activated to its active form in the small intestine by trypsin. Pancreatic lipase appears in the circulation in large amounts during acute pancreatitis. 

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. 

Apolipoprotein C-II serves as a cofactor for lipoprotein lipase. This situation resembles that of colipase, which is required for the activity of pancreatic lipase. When chylomicrons or VLDLs pass through the capillaries of an organ, they encounter lipoprotein lipase. About half the fatty acids liberated by the action of this enzyme are taken up by the tissue, whereas the rest remain in the circulation and return (bound to albumin) to the liver. Apo C-II is part of the structure of chylomicrons and VLDLs. 

Pancreatic lipase is one of the mammalian key digestive enzymes. It completes the dietary triacylglycerol breakdown initiated by preduode-nal lipases, including lingual and gastric enzymes, (see below). The enzyme is inhibited in the intestine by bile salts, but the activity is restored in the presence of colipase (CLP), a relatively short (95 residues) heat-stable polypeptide secreted by the pancreas (Semeriva and Desnuelle, 1979 Borgstrbm and Erlanson-Albertsson, 1984). The structural details of the interaction of colipase with lipase are described in Section III,C. 

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