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Title page for ETD etd-04012009-100228

Type of Document Dissertation
Author Crooke, Cornelia Elizabeth
URN etd-04012009-100228
Title Regulation of Fibronectin Assembly by PLC-gamma1
Degree PhD
Department Biochemistry
Advisory Committee
Advisor Name Title
Graham Carpenter Committee Chair
Ambra Pozzi Committee Member
Bruce Carter Committee Member
David Cortez Committee Member
Roy Zent Committee Member
  • integrins
  • extracellular matrix
  • phospholipase C gamma 1
Date of Defense 2009-02-23
Availability unrestricted
Phospholipase C-γ1 (PLC-γ1) mediates cell adhesion and migration through an undefined mechanism. Here, we examine the role of PLC-γ1 in cell-matrix adhesion in a hanging drop assay of cell aggregation. Plcg1 Null (-/-) mouse embryonic fibroblasts formed aggregates that were larger and significantly more resistant to dissociation than cells in which PLC-γ1 is re-expressed (Null + cells). Aggregate formation could be disrupted by inhibition of fibronectin interaction with integrins, indicating that fibronectin assembly may mediate aggregate formation. Fibronectin assembly was mediated by integrin α5β1 in both cell lines, while assays measuring fibronectin assembly revealed increased assembly in the Null cells. Null and Null + cells exhibited equivalent fibronectin mRNA levels and equivalent levels of fibronectin protein in pulse-labeling experiments. However, levels of secreted fibronectin in the conditioned medium were increased in Null cells. The data implicates a negative regulatory role for PLC-γ1 in cell aggregation by controlling the secretion of fibronectin into the media and its assembly into fibrils.
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