Biology Reference
In-Depth Information
14
Calpain Regulation
of Cell Migration
Anna Huttenlocher
Cell migration requires complex adhesive interactions between a cell and its
substrate. The integrin-mediated adhesions established during cell movement
are both highly regulated and dynamic. The calcium-dependent protease
calpain regulates both adhesive complex disassembly and rear retraction, and
protrusion events at the leading edge. Temporal and spatial regulation of
calpain activity is likely to be critical for effective directional migration. The
complex regulation of motility pathways by calpain is supported by the
differential effects of calpain inhibition on fibroblast and neutrophil motility.
Challenge for future investigation will be to identify critical effectors of
calpain during cell motility and to understand the mechanisms that regulate
calpain activity both temporally and spatially during cell migration.
Cell migration is a fundamental process involved in both normal and
pathological conditions such as wound healing, inflammation and tumour
invasion and metastasis. Integrin-mediated adhesion to extracellular matrix
proteins is a critical regulator of cell migration. Integrin receptors are a family
of heterodimeric cell surface adhesion receptors that link the extracellular
matrix to the actin cytoskeleton. Upon engagement, integrins cluster in the
membrane to form organized adhesive contact sites, such as focal adhesions
(Hynes, 1992; Schoenwaelder and Burridge, 1999). Adhesive contact sites are
highly dynamic structures that undergo regulated assembly, translocation and
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