메뉴 건너뛰기




Volumn 1768, Issue 1, 2007, Pages 90-99

Atomic force microscope visualization of lipid bilayer degradation due to action of phospholipase A2 and Humicola lanuginosa lipase

Author keywords

Atomic force microscopy; Enzyme kinetics; Humicola lanuginose lipase; Phospholipase A2; Supported bilayers

Indexed keywords

PHOSPHOLIPASE A2; TRIACYLGLYCEROL LIPASE;

EID: 33845465498     PISSN: 00052736     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbamem.2006.09.028     Document Type: Article
Times cited : (28)

References (37)
  • 3
    • 0034743149 scopus 로고    scopus 로고
    • Surface biology of DNA by atomic force microscopy
    • Hansma H.G. Surface biology of DNA by atomic force microscopy. Annu. Rev. Phys. Chem. 52 (2001) 71-92
    • (2001) Annu. Rev. Phys. Chem. , vol.52 , pp. 71-92
    • Hansma, H.G.1
  • 4
    • 0033520116 scopus 로고    scopus 로고
    • Imaging real-time proteolysis of single collagen I molecules with an atomic force microscope
    • Lin H., Clegg D.O., and Lal R. Imaging real-time proteolysis of single collagen I molecules with an atomic force microscope. Biochemistry-US 38 (1999) 9956-9963
    • (1999) Biochemistry-US , vol.38 , pp. 9956-9963
    • Lin, H.1    Clegg, D.O.2    Lal, R.3
  • 5
    • 0028031337 scopus 로고
    • Direct observation of enzyme activity with the atomic-force microscope
    • Radmacher M., Fritz M., Hansma H.G., and Hansma P.K. Direct observation of enzyme activity with the atomic-force microscope. Science 265 (1994) 1577-1579
    • (1994) Science , vol.265 , pp. 1577-1579
    • Radmacher, M.1    Fritz, M.2    Hansma, H.G.3    Hansma, P.K.4
  • 6
    • 0031980118 scopus 로고    scopus 로고
    • Atomic force microscope imaging of phospholipid bilayer degradation by phospholipase A(2)
    • Grandbois M., Clausen-Schaumann H., and Gaub H.E. Atomic force microscope imaging of phospholipid bilayer degradation by phospholipase A(2). Biophys. J. 74 (1998) 2398-2404
    • (1998) Biophys. J. , vol.74 , pp. 2398-2404
    • Grandbois, M.1    Clausen-Schaumann, H.2    Gaub, H.E.3
  • 7
    • 0032794188 scopus 로고    scopus 로고
    • Lag-burst kinetics in phospholipase A(2) hydrolysis of DPPC bilayers visualized by atomic force microscopy
    • Nielsen L.K., Risbo J., Callisen T.H., and Bjørnholm T. Lag-burst kinetics in phospholipase A(2) hydrolysis of DPPC bilayers visualized by atomic force microscopy. BBA-Biomembr. Acta 1420 (1998) 266-271
    • (1998) BBA-Biomembr. Acta , vol.1420 , pp. 266-271
    • Nielsen, L.K.1    Risbo, J.2    Callisen, T.H.3    Bjørnholm, T.4
  • 8
    • 0036840323 scopus 로고    scopus 로고
    • Influence of product phase separation on phospholipase A2 hydrolysis of supported phospholipid bilayers studied by force microscopy
    • Nielsen L.K., Balashev K., Callisen T.H., and Bjørnholm T. Influence of product phase separation on phospholipase A2 hydrolysis of supported phospholipid bilayers studied by force microscopy. Biophys. J. 83 (2002) 2617-2624
    • (2002) Biophys. J. , vol.83 , pp. 2617-2624
    • Nielsen, L.K.1    Balashev, K.2    Callisen, T.H.3    Bjørnholm, T.4
  • 9
    • 0042009289 scopus 로고    scopus 로고
    • Humicola lanuginosa lipase hydrolysis of mono-oleoyl-rac-glycerol at the lipid-water interface observed by atomic force microscopy
    • Balashev K., Gudmand M., Iversen L., Callisen T.H., Svendsen A., and Bjørnholm T. Humicola lanuginosa lipase hydrolysis of mono-oleoyl-rac-glycerol at the lipid-water interface observed by atomic force microscopy. BBA-Biomembranes 1615 (2003) 93-102
    • (2003) BBA-Biomembranes , vol.1615 , pp. 93-102
    • Balashev, K.1    Gudmand, M.2    Iversen, L.3    Callisen, T.H.4    Svendsen, A.5    Bjørnholm, T.6
  • 10
    • 0032139532 scopus 로고    scopus 로고
    • Enzyme-assisted nanoscale lithography in lipid membranes
    • Clausen-Schaumann H., Grandbois M., and Gaub H.E. Enzyme-assisted nanoscale lithography in lipid membranes. Adv. Mater. 10 12 (1999) 49
    • (1999) Adv. Mater. , vol.10 , Issue.12 , pp. 49
    • Clausen-Schaumann, H.1    Grandbois, M.2    Gaub, H.E.3
  • 11
    • 0016904284 scopus 로고
    • Interfacial enzyme-kinetics of lipolysis
    • Verger R., and deHaas G.H. Interfacial enzyme-kinetics of lipolysis. Annu. Rev. Biophys. Bio. 5 (1976) 77-117
    • (1976) Annu. Rev. Biophys. Bio. , vol.5 , pp. 77-117
    • Verger, R.1    deHaas, G.H.2
  • 12
    • 0028820956 scopus 로고
    • Interfacial enzymology of glycerolipid hydrolases: lessons from secreted phospholipases A2
    • Gelb M.H., Jain M.K., Hanel A.M., and Berg O.G. Interfacial enzymology of glycerolipid hydrolases: lessons from secreted phospholipases A2. Annu. Rev. Biochem. 64 (1995) 653-688
    • (1995) Annu. Rev. Biochem. , vol.64 , pp. 653-688
    • Gelb, M.H.1    Jain, M.K.2    Hanel, A.M.3    Berg, O.G.4
  • 15
    • 0025734607 scopus 로고
    • Monolayer techniques for studying phospholipase kinetics
    • Ransac S., Moreau H., Riviere C., and Verger R. Monolayer techniques for studying phospholipase kinetics. Method Enzymol. 197 (1991) 49-65
    • (1991) Method Enzymol. , vol.197 , pp. 49-65
    • Ransac, S.1    Moreau, H.2    Riviere, C.3    Verger, R.4
  • 16
    • 0031246438 scopus 로고    scopus 로고
    • Enzymatic activity of a Phospholipase A2: an electrochemical approach
    • Chen S., and Abruna H.D. Enzymatic activity of a Phospholipase A2: an electrochemical approach. Langmuir 13 (1997) 5969-5973
    • (1997) Langmuir , vol.13 , pp. 5969-5973
    • Chen, S.1    Abruna, H.D.2
  • 17
    • 0027424229 scopus 로고
    • Spectroscopic properties of the states of pig pancreatic phospholipase A2 at interfaces and their possible molecular origin
    • Jain M.K., and Maliwal B.P. Spectroscopic properties of the states of pig pancreatic phospholipase A2 at interfaces and their possible molecular origin. Biochemistry-US 32 (1993) 11838-11846
    • (1993) Biochemistry-US , vol.32 , pp. 11838-11846
    • Jain, M.K.1    Maliwal, B.P.2
  • 18
    • 0025267451 scopus 로고
    • Hydrolytic action of phospholipase A2 in monolayer phase transition region: direct observation of enzyme domain formation using fluorescence microscopy
    • Grainger D.W., Reichert A., Ringsdorf H., and Salesse C. Hydrolytic action of phospholipase A2 in monolayer phase transition region: direct observation of enzyme domain formation using fluorescence microscopy. BBA-Biomembranes 1023 (1990) 365-379
    • (1990) BBA-Biomembranes , vol.1023 , pp. 365-379
    • Grainger, D.W.1    Reichert, A.2    Ringsdorf, H.3    Salesse, C.4
  • 19
    • 0020482178 scopus 로고
    • Origin of the latency phase during the action of phospholipase A2 on unmodified phosphatidylcholine vesicles
    • Apitz-Castro R., Jain M.K., and De Haas G.H. Origin of the latency phase during the action of phospholipase A2 on unmodified phosphatidylcholine vesicles. BBA-Biomembranes 688 (1982) 349-356
    • (1982) BBA-Biomembranes , vol.688 , pp. 349-356
    • Apitz-Castro, R.1    Jain, M.K.2    De Haas, G.H.3
  • 21
    • 0028279834 scopus 로고
    • Evidence for a pancreatic lipase subfamily with new kinetic-properties
    • Thirstrup K., Verger R., and Carriere F. Evidence for a pancreatic lipase subfamily with new kinetic-properties. Biochemistry-US 33 (1994) 2748-2756
    • (1994) Biochemistry-US , vol.33 , pp. 2748-2756
    • Thirstrup, K.1    Verger, R.2    Carriere, F.3
  • 22
    • 0032510716 scopus 로고    scopus 로고
    • Interfacial activation of triglyceride lipase from thermomyces (Humicola) lanuginosa: kinetic parameters and a basis for control of the lid
    • Berg O.G., Cajal Y., Butterfoss G.L., Grey R.L., Alsina M.A., Yu B.Z., and Jain M.K. Interfacial activation of triglyceride lipase from thermomyces (Humicola) lanuginosa: kinetic parameters and a basis for control of the lid. Biochemistry-US 37 (1998) 6615-6627
    • (1998) Biochemistry-US , vol.37 , pp. 6615-6627
    • Berg, O.G.1    Cajal, Y.2    Butterfoss, G.L.3    Grey, R.L.4    Alsina, M.A.5    Yu, B.Z.6    Jain, M.K.7
  • 23
    • 0015576657 scopus 로고
    • Enzyme reactions in a membrane model: 1. New technique to study enzyme reactions in monolayers
    • Verger R., and deHaas G.H. Enzyme reactions in a membrane model: 1. New technique to study enzyme reactions in monolayers. Chem. Phys. Lipids 10 (1973) 127-136
    • (1973) Chem. Phys. Lipids , vol.10 , pp. 127-136
    • Verger, R.1    deHaas, G.H.2
  • 24
    • 0016413695 scopus 로고
    • Isobaric titration of reacting monolayers-kinetics of hydrolysis of glycerides by pancreatic lipase-B
    • Brockman H.L., Kezdy F.J., and Law J.H. Isobaric titration of reacting monolayers-kinetics of hydrolysis of glycerides by pancreatic lipase-B. J. Lipid Res. 16 (1975) 67-74
    • (1975) J. Lipid Res. , vol.16 , pp. 67-74
    • Brockman, H.L.1    Kezdy, F.J.2    Law, J.H.3
  • 25
    • 0030627885 scopus 로고    scopus 로고
    • Recovery of monomolecular films in studies of lipolysis
    • Momsen W.E., and Brockman H.L. Recovery of monomolecular films in studies of lipolysis. Method Enzymol. 286 (1997) 292-305
    • (1997) Method Enzymol. , vol.286 , pp. 292-305
    • Momsen, W.E.1    Brockman, H.L.2
  • 26
    • 0024806806 scopus 로고
    • Gastric lipases: biochemical and physiological studies
    • Gargouri Y., Moreau H., and Verger R. Gastric lipases: biochemical and physiological studies. BBA-Lipid Lipid Met. 1006 3 (1989) 255-271
    • (1989) BBA-Lipid Lipid Met. , vol.1006 , Issue.3 , pp. 255-271
    • Gargouri, Y.1    Moreau, H.2    Verger, R.3
  • 27
    • 0027163868 scopus 로고
    • Phase separated anionic domains in ternary mixed lipid monolayers at the air-water interface
    • Maloney K.M., and Grainger D.W. Phase separated anionic domains in ternary mixed lipid monolayers at the air-water interface. Chem. Phys. Lipids 65 (1993) 31-42
    • (1993) Chem. Phys. Lipids , vol.65 , pp. 31-42
    • Maloney, K.M.1    Grainger, D.W.2
  • 28
    • 0029021712 scopus 로고
    • Progress in high resolution atomic force microscopy in biology
    • Shao Z., and Yang J. Progress in high resolution atomic force microscopy in biology. Q. Rev. Biophys. 28 (1995) 195-251
    • (1995) Q. Rev. Biophys. , vol.28 , pp. 195-251
    • Shao, Z.1    Yang, J.2
  • 29
    • 0029734665 scopus 로고    scopus 로고
    • Biological atomic force microscopy: what is achieved and what is needed
    • Shao Z., Mou J., Czajkowsky D.M., Yang J., and Yuan J.Y. Biological atomic force microscopy: what is achieved and what is needed. Adv. Phys. 45 (1996) 1-86
    • (1996) Adv. Phys. , vol.45 , pp. 1-86
    • Shao, Z.1    Mou, J.2    Czajkowsky, D.M.3    Yang, J.4    Yuan, J.Y.5
  • 32
    • 0026587917 scopus 로고
    • Spontaneous domain formation of phospholipase A2 at interfaces: fluorescence microscopy of the interaction of phospholipase A2 with mixed monolayers of lecithin, lysolecithin and fatty acid
    • Riechert A., Ringsdorf H., and Wagenknecht A. Spontaneous domain formation of phospholipase A2 at interfaces: fluorescence microscopy of the interaction of phospholipase A2 with mixed monolayers of lecithin, lysolecithin and fatty acid. BBA-Biomembranes 1106 (1992) 178-188
    • (1992) BBA-Biomembranes , vol.1106 , pp. 178-188
    • Riechert, A.1    Ringsdorf, H.2    Wagenknecht, A.3
  • 33
    • 0034739443 scopus 로고    scopus 로고
    • Do membrane bound enzymes access their substrates from the membrane or aqueous phase: interfacial versus noninterfacial enzymes
    • Gelb M.H., Min J.H., and Jain M.K. Do membrane bound enzymes access their substrates from the membrane or aqueous phase: interfacial versus noninterfacial enzymes. BBA-Mol. Cell. Biol. L. 1488 (2000) 20-27
    • (2000) BBA-Mol. Cell. Biol. L. , vol.1488 , pp. 20-27
    • Gelb, M.H.1    Min, J.H.2    Jain, M.K.3
  • 34
    • 0037107824 scopus 로고    scopus 로고
    • Surface fluorescence resonance energy transfer studies on interfacial adsorption of thermomyces (Humicola) lanuginosa lipase, using monomolecular films of cis-parinaric acid
    • Yapoudjian S., Ivanova M., Douchet I., Zenatti A., Sentis M., Marine W., Svendsen A., and Verger R. Surface fluorescence resonance energy transfer studies on interfacial adsorption of thermomyces (Humicola) lanuginosa lipase, using monomolecular films of cis-parinaric acid. Biopolymers 65 2 (2002) 121-128
    • (2002) Biopolymers , vol.65 , Issue.2 , pp. 121-128
    • Yapoudjian, S.1    Ivanova, M.2    Douchet, I.3    Zenatti, A.4    Sentis, M.5    Marine, W.6    Svendsen, A.7    Verger, R.8
  • 35
    • 0025485241 scopus 로고
    • Interactions of lipases with lipid monolayers. Facts and fictions
    • Pieroni G., Gargouri Y., Sarda L., and Verger R. Interactions of lipases with lipid monolayers. Facts and fictions. Adv. Colloid Interface 32 (1990) 341-378
    • (1990) Adv. Colloid Interface , vol.32 , pp. 341-378
    • Pieroni, G.1    Gargouri, Y.2    Sarda, L.3    Verger, R.4
  • 36
    • 0033659686 scopus 로고    scopus 로고
    • Kinetic behavior of the pancreatic lipase-colipase-lipid system
    • Brockman H.L. Kinetic behavior of the pancreatic lipase-colipase-lipid system. Biochimie 82 (2000) 987-995
    • (2000) Biochimie , vol.82 , pp. 987-995
    • Brockman, H.L.1
  • 37
    • 0024314803 scopus 로고
    • Lipid-lipid interactions as regulators of carboxylester lipase activity
    • Tsujita T., Muderhwa J.M., and Brockman H.L. Lipid-lipid interactions as regulators of carboxylester lipase activity. J. Biol. Chem. 264 (1989) 8612-8618
    • (1989) J. Biol. Chem. , vol.264 , pp. 8612-8618
    • Tsujita, T.1    Muderhwa, J.M.2    Brockman, H.L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.