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Cell-specific expression of group X and group V secretory phospholipases A(2) in human lung airway epithelial cells
- Source :
- American journal of respiratory cell and molecular biology. 23(1)
- Publication Year :
- 2000
-
Abstract
- Secretory phospholipase A(2) (sPLA(2)) enzymes contribute to inflammatory injury in human lungs by several mechanisms, including eicosanoid production and hydrolytic damage to surfactant phospholipids. Several distinct sPLA(2) genes have been described in human tissue but little is known regarding their presence, localization, or function(s) within lungs. We hypothesized that sPLA(2)s would have cell-specific distributions within lung. We used reverse transcriptase/polymerase chain reaction to identify sPLA(2) messenger RNAs (mRNAs) in adult human lung tissue. Resulting complementary DNA (cDNA) sequences indicated that total lung extracts contained mRNA for Groups IB, IIA, V, and X sPLA(2). An epithelial cell line, BEAS cells, expressed only Groups IIA, V, and X. We used these cDNAs to clone these enzymes, especially the recently described Group X and Group V enzymes. Digoxigenin-labeled complementary RNA probes were used to determine localization of each sPLA(2) by in situ hybridization of human lung. Hybridization was strongly positive for Group X and Group V in airway epithelial cells, which failed to hybridize Group IB or IIA probes. Although four known mammalian sPLA(2) isotypes were expressed in lung, only Group X and Group V sPLA(2) mRNAs appear uniquely expressed in airway epithelium, suggesting they could provide a mechanism of pulmonary surfactant hydrolysis during lung injury.
- Subjects :
- Pulmonary and Respiratory Medicine
Clinical Biochemistry
Clone (cell biology)
Bronchi
In situ hybridization
Biology
Transfection
Group II Phospholipases A2
Phospholipases A
Cell Line
Substrate Specificity
Complementary DNA
medicine
Animals
Humans
RNA, Messenger
Cloning, Molecular
Molecular Biology
Gene
Lung
In Situ Hybridization
chemistry.chemical_classification
Messenger RNA
Histocytochemistry
Reverse Transcriptase Polymerase Chain Reaction
Hydrolysis
Epithelial Cells
Cell Biology
Molecular biology
Reverse transcriptase
Epithelium
Isoenzymes
Enzyme
medicine.anatomical_structure
chemistry
Organ Specificity
COS Cells
Subjects
Details
- ISSN :
- 10441549
- Volume :
- 23
- Issue :
- 1
- Database :
- OpenAIRE
- Journal :
- American journal of respiratory cell and molecular biology
- Accession number :
- edsair.doi.dedup.....469f3b45dc95694f0a45143ba557f586