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Kinetic properties of pancreatic and intestinal sPLA2 from chicken and mammals using the monomolecular film technique

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Title: Kinetic properties of pancreatic and intestinal sPLA2 from chicken and mammals using the monomolecular film technique
Authors: Karray, Aida1, Zarai, Zied1, Gargouri, Youssef1, Verger, Robert2, Bezzine, Sofiane1 sofiane_bezzine@yahoo.com
Source: Journal of Colloid & Interface Science. Nov2011, Vol. 363 Issue 2, p620-625. 6p.
Subjects: Phospholipase A2, Enzyme kinetics, Monomolecular films, Lipids, Protein structure, Cyclodextrins, Chickens, Mammals
Abstract: Abstract: The interfacial kinetic and binding data for the pancreatic and intestinal sPLA2 from bird and mammals show that these enzymes have dramatically different ability to bind and hydrolyse phospholipids. The main conclusions from our experimental data indicate that phosphatidylcholine monolayers (PC), in contrast to phosphatidylethanolamine (PE) and phosphatidylglycerol (PG), were resistant to the hydrolysis by human intestinal sPLA2. Conversely, chicken intestinal sPLA2 was found to be able to hydrolyse all the phospholipids tested, including PC. The experiments show also that the interfacial penetrating ability of chicken sPLA2 (from intestine and pancreas) was higher than their mammalian’s orthologs. This observation is confirmed by the activity of pancreatic chicken PLA2 measured on PC film showing that the interfacial pressure window that permits sPLA2 activity was very large, between 5 and 20dynescm−1, compared with the porcine pancreatic sPLA2-IB which was inactive at pressure above 15dynescm−1. In trying to establish a structure–function relationship, we examined the surface electrostatic potentials of the various sPLA2 from chicken and mammals. We reported in this study that the binding, orientation and persistence of sPLA2 at the lipid–water interface is probably governed by the electrostatic and hydrophobic forces operative at this surface. These variations argue strongly that these enzymes are not isoforms and that they are expected to have functions other than the release of lipid mediators for the biosynthesis of the eicosanoids. [Copyright &y& Elsevier]
Copyright of Journal of Colloid & Interface Science is the property of Academic Press Inc. and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)
Database: Engineering Source
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DbLabel: Engineering Source
An: 65352109
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PubTypeId: academicJournal
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  Data: Kinetic properties of pancreatic and intestinal sPLA2 from chicken and mammals using the monomolecular film technique
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  Data: <searchLink fieldCode="AR" term="%22Karray%2C+Aida%22">Karray, Aida</searchLink><relatesTo>1</relatesTo><br /><searchLink fieldCode="AR" term="%22Zarai%2C+Zied%22">Zarai, Zied</searchLink><relatesTo>1</relatesTo><br /><searchLink fieldCode="AR" term="%22Gargouri%2C+Youssef%22">Gargouri, Youssef</searchLink><relatesTo>1</relatesTo><br /><searchLink fieldCode="AR" term="%22Verger%2C+Robert%22">Verger, Robert</searchLink><relatesTo>2</relatesTo><br /><searchLink fieldCode="AR" term="%22Bezzine%2C+Sofiane%22">Bezzine, Sofiane</searchLink><relatesTo>1</relatesTo><i> sofiane_bezzine@yahoo.com</i>
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  Data: <searchLink fieldCode="JN" term="%22Journal+of+Colloid+%26+Interface+Science%22">Journal of Colloid & Interface Science</searchLink>. Nov2011, Vol. 363 Issue 2, p620-625. 6p.
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  Data: <searchLink fieldCode="DE" term="%22Phospholipase+A2%22">Phospholipase A2</searchLink><br /><searchLink fieldCode="DE" term="%22Enzyme+kinetics%22">Enzyme kinetics</searchLink><br /><searchLink fieldCode="DE" term="%22Monomolecular+films%22">Monomolecular films</searchLink><br /><searchLink fieldCode="DE" term="%22Lipids%22">Lipids</searchLink><br /><searchLink fieldCode="DE" term="%22Protein+structure%22">Protein structure</searchLink><br /><searchLink fieldCode="DE" term="%22Cyclodextrins%22">Cyclodextrins</searchLink><br /><searchLink fieldCode="DE" term="%22Chickens%22">Chickens</searchLink><br /><searchLink fieldCode="DE" term="%22Mammals%22">Mammals</searchLink>
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  Label: Abstract
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  Data: Abstract: The interfacial kinetic and binding data for the pancreatic and intestinal sPLA2 from bird and mammals show that these enzymes have dramatically different ability to bind and hydrolyse phospholipids. The main conclusions from our experimental data indicate that phosphatidylcholine monolayers (PC), in contrast to phosphatidylethanolamine (PE) and phosphatidylglycerol (PG), were resistant to the hydrolysis by human intestinal sPLA2. Conversely, chicken intestinal sPLA2 was found to be able to hydrolyse all the phospholipids tested, including PC. The experiments show also that the interfacial penetrating ability of chicken sPLA2 (from intestine and pancreas) was higher than their mammalian’s orthologs. This observation is confirmed by the activity of pancreatic chicken PLA2 measured on PC film showing that the interfacial pressure window that permits sPLA2 activity was very large, between 5 and 20dynescm−1, compared with the porcine pancreatic sPLA2-IB which was inactive at pressure above 15dynescm−1. In trying to establish a structure–function relationship, we examined the surface electrostatic potentials of the various sPLA2 from chicken and mammals. We reported in this study that the binding, orientation and persistence of sPLA2 at the lipid–water interface is probably governed by the electrostatic and hydrophobic forces operative at this surface. These variations argue strongly that these enzymes are not isoforms and that they are expected to have functions other than the release of lipid mediators for the biosynthesis of the eicosanoids. [Copyright &y& Elsevier]
– Name: AbstractSuppliedCopyright
  Label:
  Group: Ab
  Data: <i>Copyright of Journal of Colloid & Interface Science is the property of Academic Press Inc. and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract.</i> (Copyright applies to all Abstracts.)
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RecordInfo BibRecord:
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      – Type: doi
        Value: 10.1016/j.jcis.2011.07.041
    Languages:
      – Code: eng
        Text: English
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      Pagination:
        PageCount: 6
        StartPage: 620
    Subjects:
      – SubjectFull: Phospholipase A2
        Type: general
      – SubjectFull: Enzyme kinetics
        Type: general
      – SubjectFull: Monomolecular films
        Type: general
      – SubjectFull: Lipids
        Type: general
      – SubjectFull: Protein structure
        Type: general
      – SubjectFull: Cyclodextrins
        Type: general
      – SubjectFull: Chickens
        Type: general
      – SubjectFull: Mammals
        Type: general
    Titles:
      – TitleFull: Kinetic properties of pancreatic and intestinal sPLA2 from chicken and mammals using the monomolecular film technique
        Type: main
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            NameFull: Karray, Aida
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            NameFull: Zarai, Zied
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            NameFull: Gargouri, Youssef
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            NameFull: Verger, Robert
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            NameFull: Bezzine, Sofiane
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              Text: Nov2011
              Type: published
              Y: 2011
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              Value: 363
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            – TitleFull: Journal of Colloid & Interface Science
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