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PLC-gamma1 regulates fibronectin assembly and cell aggregation.

Cornelia E Crooke1, Ambra Pozzi, Graham F Carpenter

  • 1Department of Biochemistry, Vanderbilt University School of Medicine, 647 Light Hall, 21st Ave South @ Pierce, Nashville, TN 37232-2372, USA.

Experimental Cell Research
|April 22, 2009
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Phospholipase C-gamma1 (PLC-gamma1) negatively regulates cell aggregation by controlling fibronectin secretion. PLC-gamma1 deficiency increases fibronectin secretion and enhances cell-matrix adhesion and aggregation.

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Area of Science:

  • Cell Biology
  • Biochemistry
  • Molecular Biology

Background:

  • Phospholipase C-gamma1 (PLC-gamma1) is implicated in cell adhesion and migration.
  • The precise mechanism by which PLC-gamma1 influences these processes, particularly cell-matrix adhesion, remains largely undefined.

Purpose of the Study:

  • To investigate the role of PLC-gamma1 in cell-matrix adhesion and aggregation.
  • To elucidate the molecular mechanisms underlying PLC-gamma1's function in these cellular processes.

Main Methods:

  • Hanging drop assay for cell aggregation.
  • Analysis of fibronectin assembly and integrin-mediated interactions.
  • Comparison of Plcg1 Null (-/-) mouse embryonic fibroblasts with re-expressing cells (Null+).
  • Measurement of fibronectin mRNA, protein levels, and secretion.

Main Results:

  • Plcg1 Null cells formed larger, more dissociation-resistant aggregates compared to Null+ cells.
  • Fibronectin assembly, mediated by integrin alpha5beta1, was increased in Null cells.
  • While fibronectin mRNA and intracellular protein levels were equivalent, Null cells showed increased fibronectin secretion into conditioned medium.
  • Inhibition of fibronectin-integrin interaction disrupted aggregate formation.

Conclusions:

  • PLC-gamma1 negatively regulates cell aggregation.
  • PLC-gamma1 controls cell aggregation through the modulation of fibronectin secretion and assembly into extracellular matrix fibrils.