Document Detail


Hydrolysis of surfactant-associated phosphatidylcholine by mammalian secretory phospholipases A2.
MedLine Citation:
PMID:  9755106     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Hydrolysis of surfactant-associated phospholipids by secretory phospholipases A2 is an important potential mechanism for surfactant dysfunction in inflammatory lung diseases. In these conditions, airway secretory phospholipase A2 (sPLA2) activity is increased, but the type of sPLA2 and its impact on surfactant function are not well understood. We examined in vitro the effect of multiple secretory phospholipases A2 on surfactant, including their ability to 1) release free fatty acids, 2) release lysophospholipids, and 3) increase the minimum surface tension (gammamin) on a pulsating bubble surfactometer. Natural porcine surfactant and Survanta were exposed to mammalian group I (recombinant porcine pancreatic) and group II (recombinant human) secretory phospholipases A2. Our results demonstrate that mammalian group I sPLA2 hydrolyzes phosphatidylcholine (PC), producing free fatty acids and lysophosphatidylcholine, and increases gammamin. In contrast, mammalian group II sPLA2 demonstrates limited hydrolysis of PC and does not increase gammamin. Group I and group II secretory phospholipases A2 from snake venom hydrolyze PC and inhibit surfactant function. In summary, mammalian secretory phospholipases A2 from groups I and II differ significantly from each other and from snake venom in their ability to hydrolyze surfactant-associated PC.
Authors:
R D Hite; M C Seeds; R B Jacinto; R Balasubramanian; M Waite; D Bass
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Publication Detail:
Type:  Journal Article; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  The American journal of physiology     Volume:  275     ISSN:  0002-9513     ISO Abbreviation:  Am. J. Physiol.     Publication Date:  1998 Oct 
Date Detail:
Created Date:  1998-11-23     Completed Date:  1998-11-23     Revised Date:  2007-11-15    
Medline Journal Info:
Nlm Unique ID:  0370511     Medline TA:  Am J Physiol     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  L740-7     Citation Subset:  IM    
Affiliation:
Section on Pulmonary and Critical Care, Department of Internal Medicine, Wake Forest University School of Medicine, Winston-Salem, North Carolina 27157, USA.
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MeSH Terms
Descriptor/Qualifier:
Animals
Biological Products*
COS Cells
Fatty Acids, Nonesterified / metabolism
Group II Phospholipases A2
Humans
Hydrolysis
Lung / enzymology
Lysophospholipids / metabolism
Mammals
Pancreas / enzymology
Phosphatidylcholines / metabolism*
Phospholipases A / metabolism*
Phospholipases A2
Pulmonary Surfactants / chemistry*,  metabolism*
Recombinant Proteins / metabolism
Snake Venoms
Substrate Specificity
Surface Tension
Swine
Transfection
Grant Support
ID/Acronym/Agency:
CA-12107/CA/NCI NIH HHS; P01-HL-50395/HL/NHLBI NIH HHS
Chemical
Reg. No./Substance:
0/Biological Products; 0/Fatty Acids, Nonesterified; 0/Lysophospholipids; 0/Phosphatidylcholines; 0/Pulmonary Surfactants; 0/Recombinant Proteins; 0/Snake Venoms; 108778-82-1/beractant; EC 3.1.1.-/Phospholipases A; EC 3.1.1.4/Group II Phospholipases A2; EC 3.1.1.4/Phospholipases A2

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