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Transglutaminase activity is involved in polyamine-induced programmed cell death
F Facchiano1, D D'Arcangelo, A Riccomi
1Laboratorio di Patologia Vascolare, Istituto Dermopatico dell'Immacolata, Rome, Italy. f.facchiano@idi.it
Experimental Cell Research
|November 8, 2001
Summary
Polyamines like spermidine and spermine can cause cell death in aortic cells and melanoma cells, particularly in the presence of fetal calf serum. This cell death is linked to apoptosis and involves increased transglutaminase activity.
Area of Science:
- Cell Biology
- Biochemistry
- Molecular Biology
Background:
- Polyamines (putrescine, spermidine, spermine) are vital for cell growth and development.
- Their role in cell viability under specific conditions requires further investigation.
Purpose of the Study:
- To investigate the impact of polyamines on the viability of bovine aortic endothelial cells (BAECs), rat aortic smooth muscle cells (RASMCs), and a human melanoma cell line.
- To elucidate the mechanism underlying polyamine-induced cell death.
Main Methods:
- Cell culture of BAECs, RASMCs, and melanoma cells.
- Assessment of cell viability and apoptosis using FACS analysis, nucleosome ELISA, Hoechst staining, and Annexin V-FITC.
- Measurement of intracellular transglutaminase (TGase) activity.
- Evaluation of apoptosis inhibition using TGase or polyamine oxidation inhibitors.
Main Results:
- Spermidine and spermine induced dose-dependent apoptosis in the presence of fetal calf serum (FCS), while putrescine was ineffective.
- Rat aortic smooth muscle cells (RASMCs) exhibited higher sensitivity to polyamine-induced cell death.
- Apoptosis was associated with a significant increase in intracellular transglutaminase (TGase) activity.
- Inhibition of TGase activity or polyamine oxidation prevented apoptosis.
- Overexpression of tissue TGase enhanced sensitivity to polyamines.
Conclusions:
- Polyamines, specifically spermidine and spermine, can induce apoptosis in vascular and melanoma cells under FCS conditions.
- Transglutaminase (TGase) activity plays a crucial role in mediating polyamine-induced apoptosis.
- This study reveals a novel TGase-dependent mechanism by which polyamines modulate cell viability.