RGD Reference Report - Secretory Phospholipase A2-Mediated Depletion of Phosphatidylglycerol in Early Acute Respiratory Distress Syndrome. - Rat Genome Database

Send us a Message



Submit Data |  Help |  Video Tutorials |  News |  Publications |  Download |  REST API |  Citing RGD |  Contact   

Secretory Phospholipase A2-Mediated Depletion of Phosphatidylglycerol in Early Acute Respiratory Distress Syndrome.

Authors: Seeds, MC  Grier, BL  Suckling, BN  Safta, AM  Long, DL  Waite, BM  Morris, PE  Hite, RD 
Citation: Seeds MC, etal., Am J Med Sci. 2011 Dec 14.
RGD ID: 6482717
Pubmed: PMID:22173044   (View Abstract at PubMed)
PMCID: PMC3307942   (View Article at PubMed Central)
DOI: DOI:10.1097/MAJ.0b013e318239c96c   (Journal Full-text)

INTRODUCTION: Secretory phospholipases A2 (sPLA2) hydrolyze phospholipids in cell membranes and extracellular structures such as pulmonary surfactant. This study tests the hypothesis that sPLA2 are elevated in human lungs during acute respiratory distress syndrome (ARDS) and that sPLA2 levels are associated with surfactant injury by hydrolysis of surfactant phospholipids. METHODS: Bronchoalveolar lavage (BAL) fluid was obtained from 18 patients with early ARDS (<72 hours) and compared with samples from 10 healthy volunteers. Secreted phospholipase A2 levels were measured (enzyme activity and enzyme immunoassay) in conjunction with ARDS subjects' surfactant abnormalities including surfactant phospholipid composition, large and small aggregates distribution and surface tension function. RESULTS: BAL sPLA2 enzyme activity was markedly elevated in ARDS samples relative to healthy subjects when measured by ex vivo hydrolysis of both phosphatidylglycerol (PG) and phosphatidylcholine (PC). Enzyme immunoassay identified increased PLA2G2A protein in the ARDS BAL fluid, which was strongly correlated with the sPLA2 enzyme activity against PG. Of particular interest, the authors demonstrated an average depletion of 69% of the PG in the ARDS sample large aggregates relative to the normal controls. Furthermore, the sPLA2 enzyme activity against PG and PC ex vivo correlated with the BAL recovery of in vivo PG and PC, respectively, and also correlated with the altered distribution of the large and small surfactant aggregates. CONCLUSIONS: These results support the hypothesis that sPLA2-mediated hydrolysis of surfactant phospholipid, especially PG by PLA2G2A, contributes to surfactant injury during early ARDS.



RGD Manual Disease Annotations    Click to see Annotation Detail View
Object SymbolSpeciesTermQualifierEvidenceWithNotesSourceOriginal Reference(s)
PLA2G2AHumanadult respiratory distress syndrome  IEP protein:increased expression:respiratory system fluid/secretionRGD 
Pla2g2aRatadult respiratory distress syndrome  ISOPLA2G2A (Homo sapiens)protein:increased expression:respiratory system fluid/secretionRGD 
Pla2g2aMouseadult respiratory distress syndrome  ISOPLA2G2A (Homo sapiens)protein:increased expression:respiratory system fluid/secretionRGD 

Objects Annotated

Genes (Rattus norvegicus)
Pla2g2a  (phospholipase A2 group IIA)

Genes (Mus musculus)
Pla2g2a  (phospholipase A2, group IIA (platelets, synovial fluid))

Genes (Homo sapiens)
PLA2G2A  (phospholipase A2 group IIA)


Additional Information