Document Detail


Identification of pancreatic type I secreted phospholipase A2 in human epidermis and its determination by tape stripping.
MedLine Citation:
PMID:  10735945     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
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.
Authors:
J Mazereeuw-Hautier; D Redoules; R Tarroux; M Charveron; J P Salles; M F Simon; I Cerutti; M F Assalit; Y Gall; J L Bonafe; H Chap
Related Documents :
6301875 - Phosphatidic acid mimics the muscarinic action of acetylcholine in cultured bovine chro...
16814865 - Properties of the group iv phospholipase a2 family.
1834475 - Phospholipid molecular species from isolated bovine rod outer segments incorporate exog...
2752015 - Studies on the incorporation and transacylation of various fatty acids in choline and e...
24689485 - A brief review of krill oil history, research, and the commercial market.
18961015 - Removal of graphite by oxidation with perchloric acid plus periodic acid inapplicabilit...
Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  The British journal of dermatology     Volume:  142     ISSN:  0007-0963     ISO Abbreviation:  Br. J. Dermatol.     Publication Date:  2000 Mar 
Date Detail:
Created Date:  2000-04-19     Completed Date:  2000-04-19     Revised Date:  2007-11-15    
Medline Journal Info:
Nlm Unique ID:  0004041     Medline TA:  Br J Dermatol     Country:  ENGLAND    
Other Details:
Languages:  eng     Pagination:  424-31     Citation Subset:  IM    
Affiliation:
Service de Dermatologie, Hôpital de Rangueil, 1 avenue J Poulhès, 31403 Toulouse Cedex 4, France.
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Descriptor/Qualifier:
Adolescent
Adult
Biopsy / methods
Calcium / metabolism
Epidermis / enzymology*
Female
Humans
Immunohistochemistry
Middle Aged
Phospholipases A / chemistry*,  isolation & purification
Phospholipases A2
Chemical
Reg. No./Substance:
7440-70-2/Calcium; EC 3.1.1.-/Phospholipases A; EC 3.1.1.4/Phospholipases A2

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


Previous Document:  Laser resurfacing of the skin for the improvement of facial acne scarring: a systematic review of th...
Next Document:  Expression of the inducible isoform of nitric oxide synthase in pigment cell lesions of the skin.