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Minireview on pancreatic lipase and colipase
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Cited by 91 publications
(45 citation statements)
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Abstract
Smart CitationsHow this paper cites the one you are viewing
“…Even though porcine pancreatic lipase is the best studied triacylglycerol hydrolase, the lipolytic mechanism of this enzyme is still poorly understood. These results can be interpreted to indicate that pancreatic lipase is a serine-type esterase with Serl52 as the active site serine (Chapus et al, 1988;Guidoni et al, 1981). Inhibitors are bound as an ester to serine 152 of the lipase.…”
Section: Discussion
mentioning
confidence: 86%
Abstract
Smart CitationsHow this paper cites the one you are viewing
“…Even though porcine pancreatic lipase is the best studied triacylglycerol hydrolase, the lipolytic mechanism of this enzyme is still poorly understood. These results can be interpreted to indicate that pancreatic lipase is a serine-type esterase with Serl52 as the active site serine (Chapus et al, 1988;Guidoni et al, 1981). Inhibitors are bound as an ester to serine 152 of the lipase.…”
Section: Discussion
mentioning
confidence: 86%
Abstract
Smart CitationsHow this paper cites the one you are viewing
“…PNPLA1 catalyzes the synthesis of ω- O -acylceramides, which was not affected by NG-497 (Figure S3a). Furthermore, we did not observe inhibition of the more distantly related phospholipases PNPLA6, PNPLA7, PNPLA8, and PNPLA9 (Figure S3b–e), of the human acylglycerol hydrolases DDHD domain-containing protein 2 (DDHD2), HSL, and carboxylesterase 2 (CES2) (Figure S3f–h), as well as pancreatic lipase (Figure S3i), the major TAG lipase of the intestine . Finally, we did not observe inhibition of heparin-releasable TAG hydrolase activity in human serum (Figure S3j) suggesting that NG-497 does not affect the major circulating TAG hydrolases lipoprotein lipase (LPL) and hepatic lipase (HL) .…”
Section: Results
mentioning
confidence: 99%
Abstract
Smart CitationsHow this paper cites the one you are viewing
“…Pancreatic lipase is secreted from the pancreas and is the primary lipase that hydrolyzes dietary fats in the animal digestive system, converting triglyceride substrates in ingested oils to monoglycerides and free fatty acids . We previously demonstrated that TFA 3- O -gallate, ETFGg, and laccase-treated green tea extract dose-dependently inhibit porcine pancreatic lipase when triolate emulsion is used as a lipase substrate, whereas EGCg and ETFG negligibly inhibit lipase .…”
Section: Results
mentioning
confidence: 99%
Abstract
Smart CitationsHow this paper cites the one you are viewing
“…Even though porcine pancreatic lipase is the best studied triacylglycerol hydrolase, the lipolytic mechanism of this enzyme is still poorly understood. These results can be interpreted to indicate that pancreatic lipase is a serine-type esterase with Serl52 as the active site serine (Chapus et al, 1988;Guidoni et al, 1981). Inhibitors are bound as an ester to serine 152 of the lipase.…”
Section: Discussion
mentioning
confidence: 86%
Abstract
Smart CitationsHow this paper cites the one you are viewing
“…PNPLA1 catalyzes the synthesis of ω- O -acylceramides, which was not affected by NG-497 (Figure S3a). Furthermore, we did not observe inhibition of the more distantly related phospholipases PNPLA6, PNPLA7, PNPLA8, and PNPLA9 (Figure S3b–e), of the human acylglycerol hydrolases DDHD domain-containing protein 2 (DDHD2), HSL, and carboxylesterase 2 (CES2) (Figure S3f–h), as well as pancreatic lipase (Figure S3i), the major TAG lipase of the intestine . Finally, we did not observe inhibition of heparin-releasable TAG hydrolase activity in human serum (Figure S3j) suggesting that NG-497 does not affect the major circulating TAG hydrolases lipoprotein lipase (LPL) and hepatic lipase (HL) .…”
Section: Results
mentioning
confidence: 99%
Abstract
Smart CitationsHow this paper cites the one you are viewing
“…Pancreatic lipase is secreted from the pancreas and is the primary lipase that hydrolyzes dietary fats in the animal digestive system, converting triglyceride substrates in ingested oils to monoglycerides and free fatty acids . We previously demonstrated that TFA 3- O -gallate, ETFGg, and laccase-treated green tea extract dose-dependently inhibit porcine pancreatic lipase when triolate emulsion is used as a lipase substrate, whereas EGCg and ETFG negligibly inhibit lipase .…”
Section: Results
mentioning
confidence: 99%
Abstract
Smart CitationsHow this paper cites the one you are viewing
“…Even though porcine pancreatic lipase is the best studied triacylglycerol hydrolase, the lipolytic mechanism of this enzyme is still poorly understood. These results can be interpreted to indicate that pancreatic lipase is a serine-type esterase with Serl52 as the active site serine (Chapus et al, 1988;Guidoni et al, 1981). Inhibitors are bound as an ester to serine 152 of the lipase.…”
Section: Discussion
mentioning
confidence: 86%
Abstract
Smart CitationsHow this paper cites the one you are viewing
“…PNPLA1 catalyzes the synthesis of ω- O -acylceramides, which was not affected by NG-497 (Figure S3a). Furthermore, we did not observe inhibition of the more distantly related phospholipases PNPLA6, PNPLA7, PNPLA8, and PNPLA9 (Figure S3b–e), of the human acylglycerol hydrolases DDHD domain-containing protein 2 (DDHD2), HSL, and carboxylesterase 2 (CES2) (Figure S3f–h), as well as pancreatic lipase (Figure S3i), the major TAG lipase of the intestine . Finally, we did not observe inhibition of heparin-releasable TAG hydrolase activity in human serum (Figure S3j) suggesting that NG-497 does not affect the major circulating TAG hydrolases lipoprotein lipase (LPL) and hepatic lipase (HL) .…”
Section: Results
mentioning
confidence: 99%
Abstract
Smart CitationsHow this paper cites the one you are viewing
“…Pancreatic lipase is secreted from the pancreas and is the primary lipase that hydrolyzes dietary fats in the animal digestive system, converting triglyceride substrates in ingested oils to monoglycerides and free fatty acids . We previously demonstrated that TFA 3- O -gallate, ETFGg, and laccase-treated green tea extract dose-dependently inhibit porcine pancreatic lipase when triolate emulsion is used as a lipase substrate, whereas EGCg and ETFG negligibly inhibit lipase .…”
Section: Results
mentioning
confidence: 99%