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Thrombin regulates PDGF expression in bovine glomerular endothelial cells
G Grandaliano1, G G Choudhury, E Poptic
1Department of Medicine, University of Texas Health Science Center at San Antonio, Texas 78284-7882, USA.
Journal of the American Society of Nephrology : JASN
|April 29, 1998
Summary
Thrombin stimulates platelet-derived growth factor (PDGF) production and DNA synthesis in glomerular endothelial cells. This suggests PDGF released by these cells may influence kidney cell functions via paracrine signaling.
Area of Science:
- Nephrology
- Vascular Biology
- Cellular Signaling
Background:
- Thrombin, a coagulation enzyme, is implicated in glomerular diseases.
- Intraglomerular fibrin deposition and thrombosis are hallmarks of kidney pathologies.
- Platelet-derived growth factor (PDGF) plays a role in cellular processes.
Purpose of the Study:
- To investigate the effect of thrombin on PDGF production and DNA synthesis in bovine glomerular endothelial cells (G/endo).
- To analyze PDGF mRNA expression in response to thrombin stimulation.
- To determine the responsiveness of G/endo to different PDGF isoforms.
Main Methods:
- DNA synthesis measured by [3H]thymidine incorporation.
- PDGF levels assessed by Western blotting and radioreceptor assay.
- PDGF mRNA expression analyzed using solution hybridization with cDNA probes.
Main Results:
- Bovine G/endo constitutively secrete PDGF.
- Thrombin significantly stimulates PDGF production and B-chain mRNA expression in G/endo.
- Thrombin also enhances DNA synthesis in G/endo, peaking at 24 hours.
- G/endo do not respond to PDGF isoforms BB, AB, or AA.
Conclusions:
- Bovine glomerular endothelial cells produce PDGF.
- Thrombin induces de novo synthesis of PDGF in these cells.
- PDGF released by G/endo likely acts on mesangial cells via paracrine mechanisms, influencing their proliferation and matrix production.