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Volumn 1771, Issue 5, 2007, Pages 633-640

Comparative study on digestive lipase activities on the self emulsifying excipient Labrasol®, medium chain glycerides and PEG esters

Author keywords

Digestive enzyme; Lipase; Lipid excipient; Lipolysis; Oral drug delivery

Indexed keywords

ACYLGLYCEROL; CARBOXYL ESTER HYDROXYLASE; EXCIPIENT; HYDROLASE; LABRASOL; MACROGOL; PANCREATIC LIPASE RELATED PROTEIN 2; TRIACYLGLYCEROL; TRIACYLGLYCEROL LIPASE; UNCLASSIFIED DRUG;

EID: 34247638077     PISSN: 13881981     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbalip.2007.02.009     Document Type: Article
Times cited : (111)

References (50)
  • 1
    • 1842684453 scopus 로고    scopus 로고
    • Self-emulsifying drug delivery systems (SEDDS) for improved oral delivery of lipophilic drugs
    • Gursoy R.N., and Benita S. Self-emulsifying drug delivery systems (SEDDS) for improved oral delivery of lipophilic drugs. Biomed. Pharmacother. 58 (2004) 173-182
    • (2004) Biomed. Pharmacother. , vol.58 , pp. 173-182
    • Gursoy, R.N.1    Benita, S.2
  • 2
    • 0028000096 scopus 로고
    • Rationale for the development of Sandimmune Neoral
    • Vonderscher J., and Meinzer A. Rationale for the development of Sandimmune Neoral. Transplant. Proc. 26 (1994) 2925-2927
    • (1994) Transplant. Proc. , vol.26 , pp. 2925-2927
    • Vonderscher, J.1    Meinzer, A.2
  • 4
    • 0021140493 scopus 로고
    • The effect of different oils on the absorption of probucol in the rat
    • Palin K.J., and Wilson C.G. The effect of different oils on the absorption of probucol in the rat. J. Pharm. Pharmacol. 36 (1984) 641-643
    • (1984) J. Pharm. Pharmacol. , vol.36 , pp. 641-643
    • Palin, K.J.1    Wilson, C.G.2
  • 5
    • 0018081953 scopus 로고
    • Enhancement of bioavailability of a hydrophobic amine antimalarial by formulation with oleic acid in a soft gelatin capsule
    • Stella V., Haslam J., Yata N., Okada H., Lindenbaum S., and Higuchi T. Enhancement of bioavailability of a hydrophobic amine antimalarial by formulation with oleic acid in a soft gelatin capsule. J. Pharm. Sci. 67 (1978) 1375-1377
    • (1978) J. Pharm. Sci. , vol.67 , pp. 1375-1377
    • Stella, V.1    Haslam, J.2    Yata, N.3    Okada, H.4    Lindenbaum, S.5    Higuchi, T.6
  • 6
    • 0037371606 scopus 로고    scopus 로고
    • Separation and characterization of the colloidal phases produced on digestion of common formulation lipids and assessment of their impact on the apparent solubility of selected poorly water-soluble drugs
    • Kossena G.A., Boyd B.J., Porter C.J., and Charman W.N. Separation and characterization of the colloidal phases produced on digestion of common formulation lipids and assessment of their impact on the apparent solubility of selected poorly water-soluble drugs. J. Pharm. Sci. 92 (2003) 634-648
    • (2003) J. Pharm. Sci. , vol.92 , pp. 634-648
    • Kossena, G.A.1    Boyd, B.J.2    Porter, C.J.3    Charman, W.N.4
  • 7
    • 0019783683 scopus 로고
    • Aqueous lipid phases of relevance to intestinal fat digestion and absorption
    • Lindstrom M., Ljusberg-Wahren H., Larsson K., and Borgstrom B. Aqueous lipid phases of relevance to intestinal fat digestion and absorption. Lipids 16 (1981) 749-754
    • (1981) Lipids , vol.16 , pp. 749-754
    • Lindstrom, M.1    Ljusberg-Wahren, H.2    Larsson, K.3    Borgstrom, B.4
  • 8
    • 33751014029 scopus 로고    scopus 로고
    • Formulation of poorly water-soluble drugs for oral administration: physicochemical and physiological issues and the lipid formulation classification system
    • Pouton C.W. Formulation of poorly water-soluble drugs for oral administration: physicochemical and physiological issues and the lipid formulation classification system. Eur. J. Pharm. Sci. (2006)
    • (2006) Eur. J. Pharm. Sci.
    • Pouton, C.W.1
  • 10
  • 11
    • 0034602595 scopus 로고    scopus 로고
    • NMR characterisation and transdermal drug delivery potential of microemulsion systems
    • Kreilgaard M., Pedersen E.J., and Jaroszewski J.W. NMR characterisation and transdermal drug delivery potential of microemulsion systems. J. Control. Release 69 (2000) 421-433
    • (2000) J. Control. Release , vol.69 , pp. 421-433
    • Kreilgaard, M.1    Pedersen, E.J.2    Jaroszewski, J.W.3
  • 12
    • 0037413364 scopus 로고    scopus 로고
    • Enhanced intestinal absorption of vancomycin with Labrasol and d-alpha-tocopheryl PEG 1000 succinate in rats
    • Prasad Y.V., Puthli S.P., Eaimtrakarn S., Ishida M., Yoshikawa Y., Shibata N., and Takada K. Enhanced intestinal absorption of vancomycin with Labrasol and d-alpha-tocopheryl PEG 1000 succinate in rats. Int. J. Pharm. 250 (2003) 181-190
    • (2003) Int. J. Pharm. , vol.250 , pp. 181-190
    • Prasad, Y.V.1    Puthli, S.P.2    Eaimtrakarn, S.3    Ishida, M.4    Yoshikawa, Y.5    Shibata, N.6    Takada, K.7
  • 14
    • 1142309794 scopus 로고    scopus 로고
    • In situ intestinal absorption studies on low molecular weight heparin in rats using labrasol as absorption enhancer
    • Rama Prasad Y.V., Minamimoto T., Yoshikawa Y., Shibata N., Mori S., Matsuura A., and Takada K. In situ intestinal absorption studies on low molecular weight heparin in rats using labrasol as absorption enhancer. Int. J. Pharm. 271 (2004) 225-232
    • (2004) Int. J. Pharm. , vol.271 , pp. 225-232
    • Rama Prasad, Y.V.1    Minamimoto, T.2    Yoshikawa, Y.3    Shibata, N.4    Mori, S.5    Matsuura, A.6    Takada, K.7
  • 16
    • 0035798071 scopus 로고    scopus 로고
    • A novel emulsifier, labrasol, enhances gastrointestinal absorption of gentamicin
    • Hu Z., Tawa R., Konishi T., Shibata N., and Takada K. A novel emulsifier, labrasol, enhances gastrointestinal absorption of gentamicin. Life Sci. 69 (2001) 2899-2910
    • (2001) Life Sci. , vol.69 , pp. 2899-2910
    • Hu, Z.1    Tawa, R.2    Konishi, T.3    Shibata, N.4    Takada, K.5
  • 17
    • 0027250231 scopus 로고
    • Secretion and contribution to lipolysis of gastric and pancreatic lipases during a test meal in humans
    • Carriere F., Barrowman J.A., Verger R., and Laugier R. Secretion and contribution to lipolysis of gastric and pancreatic lipases during a test meal in humans. Gastroenterology 105 (1993) 876-888
    • (1993) Gastroenterology , vol.105 , pp. 876-888
    • Carriere, F.1    Barrowman, J.A.2    Verger, R.3    Laugier, R.4
  • 20
  • 21
    • 0026671201 scopus 로고
    • Two novel human pancreatic lipase related proteins, hPLRP1 and hPLRP2. Differences in colipase dependence and in lipase activity
    • Giller T., Buchwald P., Blum-Kaelin D., and Hunziker W. Two novel human pancreatic lipase related proteins, hPLRP1 and hPLRP2. Differences in colipase dependence and in lipase activity. J. Biol. Chem. 267 (1992) 16509-16516
    • (1992) J. Biol. Chem. , vol.267 , pp. 16509-16516
    • Giller, T.1    Buchwald, P.2    Blum-Kaelin, D.3    Hunziker, W.4
  • 22
    • 0032497330 scopus 로고    scopus 로고
    • Pancreatic lipase-related protein 1 (PLRP1) is present in the pancreatic juice of several species
    • De Caro J., Carrière F., Barboni P., Giller T., Verger R., and De Caro A. Pancreatic lipase-related protein 1 (PLRP1) is present in the pancreatic juice of several species. Biochim. Biophys. Acta 1387 (1998) 331-341
    • (1998) Biochim. Biophys. Acta , vol.1387 , pp. 331-341
    • De Caro, J.1    Carrière, F.2    Barboni, P.3    Giller, T.4    Verger, R.5    De Caro, A.6
  • 24
    • 0018877342 scopus 로고
    • Studies on the substrate specificity of a carboxyl ester hydrolase from human pancreatic juice: I. Action on carboxyl esters, glycerides and phospholipids
    • Lombardo D., Fauvel J., and Guy O. Studies on the substrate specificity of a carboxyl ester hydrolase from human pancreatic juice: I. Action on carboxyl esters, glycerides and phospholipids. Biochim. Biophys. Acta 611 (1980) 136-146
    • (1980) Biochim. Biophys. Acta , vol.611 , pp. 136-146
    • Lombardo, D.1    Fauvel, J.2    Guy, O.3
  • 25
    • 0014458576 scopus 로고
    • Purification from porcine pancreas of two molecular species with lipase activity
    • Verger R., de Haas G.H., and Sarda L. Purification from porcine pancreas of two molecular species with lipase activity. Biochim. Biophys. Acta 188 (1969) 272-282
    • (1969) Biochim. Biophys. Acta , vol.188 , pp. 272-282
    • Verger, R.1    de Haas, G.H.2    Sarda, L.3
  • 26
    • 0017184389 scopus 로고
    • A rapid and sensitive method for quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M.M. A rapid and sensitive method for quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72 (1976) 248-254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 27
    • 0014721067 scopus 로고
    • Tributyrin as a substrate for determination of lipase activity of pancreatic juice and small intestinal content
    • Erlanson C., and Borgström B. Tributyrin as a substrate for determination of lipase activity of pancreatic juice and small intestinal content. Scand. J. Gastroenterol. 5 (1970) 293-295
    • (1970) Scand. J. Gastroenterol. , vol.5 , pp. 293-295
    • Erlanson, C.1    Borgström, B.2
  • 29
    • 5644294406 scopus 로고    scopus 로고
    • Solubilisation of poorly water-soluble drugs during in vitro lipolysis of medium- and long-chain triacylglycerols
    • Christensen J.O., Schultz K., Mollgaard B., Kristensen H.G., and Mullertz A. Solubilisation of poorly water-soluble drugs during in vitro lipolysis of medium- and long-chain triacylglycerols. Eur. J. Pharm. Sci. 23 (2004) 287-296
    • (2004) Eur. J. Pharm. Sci. , vol.23 , pp. 287-296
    • Christensen, J.O.1    Schultz, K.2    Mollgaard, B.3    Kristensen, H.G.4    Mullertz, A.5
  • 30
    • 1242291941 scopus 로고    scopus 로고
    • Drug solubilization behavior during in vitro digestion of suspension formulations of poorly water-soluble drugs in triglyceride lipids
    • Kaukonen A.M., Boyd B.J., Charman W.N., and Porter C.J. Drug solubilization behavior during in vitro digestion of suspension formulations of poorly water-soluble drugs in triglyceride lipids. Pharm. Res. 21 (2004) 254-260
    • (2004) Pharm. Res. , vol.21 , pp. 254-260
    • Kaukonen, A.M.1    Boyd, B.J.2    Charman, W.N.3    Porter, C.J.4
  • 31
    • 1242292226 scopus 로고    scopus 로고
    • Drug solubilization behavior during in vitro digestion of simple triglyceride lipid solution formulations
    • Kaukonen A.M., Boyd B.J., Porter C.J., and Charman W.N. Drug solubilization behavior during in vitro digestion of simple triglyceride lipid solution formulations. Pharm. Res. 21 (2004) 245-253
    • (2004) Pharm. Res. , vol.21 , pp. 245-253
    • Kaukonen, A.M.1    Boyd, B.J.2    Porter, C.J.3    Charman, W.N.4
  • 32
    • 4344578729 scopus 로고    scopus 로고
    • Susceptibility to lipase-mediated digestion reduces the oral bioavailability of danazol after administration as a medium-chain lipid-based microemulsion formulation
    • Porter C.J., Kaukonen A.M., Boyd B.J., Edwards G.A., and Charman W.N. Susceptibility to lipase-mediated digestion reduces the oral bioavailability of danazol after administration as a medium-chain lipid-based microemulsion formulation. Pharm. Res. 21 (2004) 1405-1412
    • (2004) Pharm. Res. , vol.21 , pp. 1405-1412
    • Porter, C.J.1    Kaukonen, A.M.2    Boyd, B.J.3    Edwards, G.A.4    Charman, W.N.5
  • 33
    • 0034898463 scopus 로고    scopus 로고
    • A dynamic in vitro lipolysis model: I. Controlling the rate of lipolysis by continuous addition of calcium
    • Zangenberg N.H., Mullertz A., Kristensen H.G., and Hovgaard L. A dynamic in vitro lipolysis model: I. Controlling the rate of lipolysis by continuous addition of calcium. Eur. J. Pharm. Sci. 14 (2001) 115-122
    • (2001) Eur. J. Pharm. Sci. , vol.14 , pp. 115-122
    • Zangenberg, N.H.1    Mullertz, A.2    Kristensen, H.G.3    Hovgaard, L.4
  • 34
    • 0342339130 scopus 로고
    • Composition et stabilité de l'équipement enzymatique du pancréas de l'homme et de divers animaux
    • Figarella C. Composition et stabilité de l'équipement enzymatique du pancréas de l'homme et de divers animaux. Bull. Soc. Chim. Biol. 48 (1966) 97-115
    • (1966) Bull. Soc. Chim. Biol. , vol.48 , pp. 97-115
    • Figarella, C.1
  • 35
    • 0019429205 scopus 로고
    • The proteins of human pancreatic external secretion
    • Guy O., and Figarella C. The proteins of human pancreatic external secretion. Scand. J. Gastroenterol., Suppl. 67 (1981) 59-61
    • (1981) Scand. J. Gastroenterol., Suppl. , vol.67 , pp. 59-61
    • Guy, O.1    Figarella, C.2
  • 36
    • 0003022666 scopus 로고
    • Pancreatic carboxyl ester lipase (cholesterol esterase)
    • Brockman H.L. (Ed), Elsevier Science Publishers, Amsterdam
    • Rudd E.A., and Brockman H.L. Pancreatic carboxyl ester lipase (cholesterol esterase). In: Brockman H.L. (Ed). Lipases (1984), Elsevier Science Publishers, Amsterdam 185-204
    • (1984) Lipases , pp. 185-204
    • Rudd, E.A.1    Brockman, H.L.2
  • 37
    • 0024422703 scopus 로고
    • Cloning of the bovine pancreatic cholesterol esterase/lysophospholipase
    • Kyger E.M., Wiegand R.C., and Lange L.G. Cloning of the bovine pancreatic cholesterol esterase/lysophospholipase. Biochem. Biophys. Res. Commun. 164 (1989) 1302-1309
    • (1989) Biochem. Biophys. Res. Commun. , vol.164 , pp. 1302-1309
    • Kyger, E.M.1    Wiegand, R.C.2    Lange, L.G.3
  • 38
    • 0025183485 scopus 로고
    • cDNA cloning of human-milk bile-salt-stimulated lipase and evidence for its identity to pancreatic carboxylic ester hydrolase
    • Nilsson J., Blaeckberg L., Carlsson P., Enerbaeck S., Hernell O., and Bjursell G. cDNA cloning of human-milk bile-salt-stimulated lipase and evidence for its identity to pancreatic carboxylic ester hydrolase. Eur. J. Biochem. 192 (1990) 543-550
    • (1990) Eur. J. Biochem. , vol.192 , pp. 543-550
    • Nilsson, J.1    Blaeckberg, L.2    Carlsson, P.3    Enerbaeck, S.4    Hernell, O.5    Bjursell, G.6
  • 40
    • 0035929324 scopus 로고    scopus 로고
    • The structure of truncated recombinant human bile salt-stimulated lipase reveals bile salt-independent conformational flexibility at the active-site loop and provides insights into heparin binding
    • Moore S.A., Kingston R.L., Loomes K.M., Hernell O., Blackberg L., Baker H.M., and Baker E.N. The structure of truncated recombinant human bile salt-stimulated lipase reveals bile salt-independent conformational flexibility at the active-site loop and provides insights into heparin binding. J. Mol. Biol. 312 (2001) 511-523
    • (2001) J. Mol. Biol. , vol.312 , pp. 511-523
    • Moore, S.A.1    Kingston, R.L.2    Loomes, K.M.3    Hernell, O.4    Blackberg, L.5    Baker, H.M.6    Baker, E.N.7
  • 41
    • 0031081552 scopus 로고    scopus 로고
    • In vivo and in vitro studies on the stereoselective hydrolysis of tri- and diglycerides by gastric and pancreatic lipases
    • Carrière F., Rogalska E., Cudrey C., Ferrato F., Laugier R., and Verger R. In vivo and in vitro studies on the stereoselective hydrolysis of tri- and diglycerides by gastric and pancreatic lipases. Bioorg. Med. Chem. 5 (1997) 429-435
    • (1997) Bioorg. Med. Chem. , vol.5 , pp. 429-435
    • Carrière, F.1    Rogalska, E.2    Cudrey, C.3    Ferrato, F.4    Laugier, R.5    Verger, R.6
  • 45
    • 0033546322 scopus 로고    scopus 로고
    • Crystal structure of human gastric lipase and model of lysosomal acid lipase, two lipolytic enzymes of medical interest
    • Roussel A., Canaan S., Egloff M.P., Riviere M., Dupuis L., Verger R., and Cambillau C. Crystal structure of human gastric lipase and model of lysosomal acid lipase, two lipolytic enzymes of medical interest. J. Biol. Chem. 274 (1999) 16995-17002
    • (1999) J. Biol. Chem. , vol.274 , pp. 16995-17002
    • Roussel, A.1    Canaan, S.2    Egloff, M.P.3    Riviere, M.4    Dupuis, L.5    Verger, R.6    Cambillau, C.7
  • 47
    • 0028279834 scopus 로고
    • Evidence for a pancreatic lipase subfamily with new kinetic properties
    • Thirstrup K., Verger R., and Carrière F. Evidence for a pancreatic lipase subfamily with new kinetic properties. Biochemistry 33 (1994) 2748-2756
    • (1994) Biochemistry , vol.33 , pp. 2748-2756
    • Thirstrup, K.1    Verger, R.2    Carrière, F.3
  • 48
    • 0018801496 scopus 로고
    • Hydrolysis of mixed monomolecular films of triglyceride/lecithin by pancreatic lipase
    • Piéroni G., and Verger R. Hydrolysis of mixed monomolecular films of triglyceride/lecithin by pancreatic lipase. J. Biol. Chem. 254 (1979) 10090-10094
    • (1979) J. Biol. Chem. , vol.254 , pp. 10090-10094
    • Piéroni, G.1    Verger, R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.