Identification of pancreatic type I secreted phospholipase A2 in human epidermis and its determination by tape stripping

Phospholipases A2 (PLA2) catalyse the release of fatty acids from the sn‐2 position of phospholipids and have been suggested to play a key part in permeability barrier homeostasis. Using a sensitive and versatile fluorometric method, significant PLA2 activity has been detected in both human skin hom...

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Published inBritish journal of dermatology (1951) Vol. 142; no. 3; pp. 424 - 431
Main Authors Mazereeuw-Hautier, J., Redoules, D., Tarroux, R., Charveron, M., Salles, J.P., Simon, M.F., Cerutti, I., Assalit, M.F., Gall, Y., Bonafe, J.L., Chap, H.
Format Journal Article
LanguageEnglish
Published Oxford, UK Blackwell Science Ltd 01.03.2000
Subjects
Adolescent
Adult
Biopsy - methods
Calcium - metabolism
Epidermis - enzymology
Female
human epidermis
Humans
Immunohistochemistry
Middle Aged
pancreatic type I secreted phospholipase A2
Phospholipases A - chemistry
Phospholipases A - isolation & purification
Phospholipases A2
tape stripping
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Abstract Phospholipases A2 (PLA2) catalyse the release of fatty acids from the sn‐2 position of phospholipids and have been suggested to play a key part in permeability barrier homeostasis. Using a sensitive and versatile fluorometric method, significant PLA2 activity has been detected in both human skin homogenates and tape strippings of stratum corneum. Based on various properties (resistance to heat and sulphuric acid treatment, neutral optimal pH, absolute requirement for millimolar calcium concentrations, inhibition by dithiothreitol and p‐bromophenacyl bromide, and resistance to a trifluoromethyl ketone derivative of arachidonic acid, AACOCF3, a specific inhibitor of cytosolic PLA2), this enzyme was characterized as a secretory PLA2 (sPLA2). Immunohistochemistry revealed strong labelling of type I pancreatic sPLA2 at the stratum corneum–stratum granulosum junction, type II sPLA2 being undetectable. An increase in PLA2 activity in tape‐stripped material from the deepest level of the stratum corneum was correlated with partial morphological disappearance of type I sPLA2 immunolabelling. Our data thus provide the first convincing evidence that pancreatic sPLA2 is significantly expressed in human epidermis, where it might participate in the accumulation of free fatty acids contributing to the permeability barrier. In addition, our method for determining PLA2 activity in easily available tape strippings should allow further clinical studies aimed to explore possible PLA2 abnormalities in various dermatoses.
AbstractList Abstract Phospholipases A2 (PLA2) catalyse the release of fatty acids from the sn-2 position of phospholipids and have been suggested to play a key part in permeability barrier homeostasis. Using a sensitive and versatile fluorometric method, significant PLA2 activity has been detected in both human skin homogenates and tape strippings of stratum corneum. Based on various properties (resistance to heat and sulphuric acid treatment, neutral optimal pH, absolute requirement for millimolar calcium concentrations, inhibition by dithiothreitol and p-bromophenacyl bromide, and resistance to a trifluoromethyl ketone derivative of arachidonic acid, AACOCF3, a specific inhibitor of cytosolic PLA2), this enzyme was characterized as a secretory PLA2 (sPLA2). Immunohistochemistry revealed strong labelling of type I pancreatic sPLA2 at the stratum corneum–stratum granulosum junction, type II sPLA2 being undetectable. An increase in PLA2 activity in tape-stripped material from the deepest level of the stratum corneum was correlated with partial morphological disappearance of type I sPLA2 immunolabelling. Our data thus provide the first convincing evidence that pancreatic sPLA2 is significantly expressed in human epidermis, where it might participate in the accumulation of free fatty acids contributing to the permeability barrier. In addition, our method for determining PLA2 activity in easily available tape strippings should allow further clinical studies aimed to explore possible PLA2 abnormalities in various dermatoses.
Phospholipases A2 (PLA2) catalyse the release of fatty acids from the sn‐2 position of phospholipids and have been suggested to play a key part in permeability barrier homeostasis. Using a sensitive and versatile fluorometric method, significant PLA2 activity has been detected in both human skin homogenates and tape strippings of stratum corneum. Based on various properties (resistance to heat and sulphuric acid treatment, neutral optimal pH, absolute requirement for millimolar calcium concentrations, inhibition by dithiothreitol and p‐bromophenacyl bromide, and resistance to a trifluoromethyl ketone derivative of arachidonic acid, AACOCF3, a specific inhibitor of cytosolic PLA2), this enzyme was characterized as a secretory PLA2 (sPLA2). Immunohistochemistry revealed strong labelling of type I pancreatic sPLA2 at the stratum corneum–stratum granulosum junction, type II sPLA2 being undetectable. An increase in PLA2 activity in tape‐stripped material from the deepest level of the stratum corneum was correlated with partial morphological disappearance of type I sPLA2 immunolabelling. Our data thus provide the first convincing evidence that pancreatic sPLA2 is significantly expressed in human epidermis, where it might participate in the accumulation of free fatty acids contributing to the permeability barrier. In addition, our method for determining PLA2 activity in easily available tape strippings should allow further clinical studies aimed to explore possible PLA2 abnormalities in various dermatoses.
Author Mazereeuw-Hautier, J.
Gall, Y.
Bonafe, J.L.
Cerutti, I.
Chap, H.
Charveron, M.
Simon, M.F.
Salles, J.P.
Redoules, D.
Tarroux, R.
Assalit, M.F.
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1990; 95
1986; 876
1993; 8
1991; 295
1997; 22
1997; 272
1995; 36
1989; 1007
1995; 34
1989; 177
1993; 1170
1985; 85
1988; 263
1975; 55
1988; 90
1988; 91
1996; 288
1996; 97
1988; 106
1996; 106
1998; 273
1994; 102
1993; 13
1998; 39
1993; 17
1994; 269
1991; 24
1986; 86
1980; 74
1991; 183
1968; 159
1995; 1257
1993; 32
1986; 5
1971; 58
1985; 112
1999; 34
1995; 104
1982
1994; 18
1997; 390
1985; 150
1983; 108
1977; 252
1990; 94
Metz (2023012714364784700_b47) 1991; 295
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Bergers (2023012714364784700_b11) 1988; 90
Tischfield (2023012714364784700_b14) 1997; 272
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Li-Stiles (2023012714364784700_b30) 1998; 39
Street (2023012714364784700_b34) 1993; 32
Chaminade (2023012714364784700_b12) 1999; 34
Seilhamer (2023012714364784700_b42) 1986; 5
Radvanyi (2023012714364784700_b31) 1989; 177
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Schürer (2023012714364784700_b1) 1991; 183
Dennis (2023012714364784700_b13) 1997; 22
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Elias (2023012714364784700_b2) 1991; 24
Bonventre (2023012714364784700_b22) 1997; 390
Mao-Qiang (2023012714364784700_b29) 1996; 106
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Grass (2023012714364784700_b27) 1996; 97
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Snippet Phospholipases A2 (PLA2) catalyse the release of fatty acids from the sn‐2 position of phospholipids and have been suggested to play a key part in permeability...
Phospholipases A2 (PLA2) catalyse the release of fatty acids from the sn-2 position of phospholipids and have been suggested to play a key part in permeability...
Abstract Phospholipases A2 (PLA2) catalyse the release of fatty acids from the sn-2 position of phospholipids and have been suggested to play a key part in...
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SubjectTerms Adolescent
Adult
Biopsy - methods
Calcium - metabolism
Epidermis - enzymology
Female
human epidermis
Humans
Immunohistochemistry
Middle Aged
pancreatic type I secreted phospholipase A2
Phospholipases A - chemistry
Phospholipases A - isolation & purification
Phospholipases A2
tape stripping
Title Identification of pancreatic type I secreted phospholipase A2 in human epidermis and its determination by tape stripping
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https://onlinelibrary.wiley.com/doi/abs/10.1046%2Fj.1365-2133.2000.03351.x
https://www.ncbi.nlm.nih.gov/pubmed/10735945
https://search.proquest.com/docview/70992523
Volume 142
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