Biology Reference
In-Depth Information
limited. The findings from our laboratory and other laboratories support a
critical role for the calcium-dependent protease calpain during migration and
in the regulation of integrin-containing adhesive contact sites. It is likely that
the effects of calpain on cell motility are to a large extent mediated by its
effects on the composition and organization of focal adhesions. However, how
the irreversible modification of substrates by calpain participates in
intracellular signalling and the dynamic regulation of cell motility remains a
challenge. The tight regulation of its activity with only localized activation is
likely to be critical for its participation in cell migration. Its activation is likely
to be required for cell motility and cell retraction, while at the same time
critical for mediating stop signals that inhibit the protrusion machinery and
cell movement. The different roles of calpain in the migration of fibroblasts
and neutrophils underlie the complexity of its regulation and participation
during cell migration. The coming years promise to be informative and
exciting as we gain understanding of how migration is regulated, both
temporally and spatially, and how mediators such as calpain participate in this
regulation.
References
Allen, W. E., Zicha, D., Ridley, A. J. and Jones, G. E., 1998. A role for Cdc42 in
macrophage chemotaxis. J. Cell Biol. 141: 1147-1157.
Arthur, J. S. and Crawford, C., 1996. Investigation of the interaction of m-calpain
with phospholipids: calpain-phospholipid interactions. Biochim. Biophys. Acta 1293:
201-206.
Arthur, J. S., Elce, J. S., Hegadorn, C., Williams, K. and Greer, P. A., 2000. Disruption of
the murine calpain small subunit gene, Capn4: calpain is essential for embryonic
development but not for cell growth and division. Mol. Cell Biol. 20: 4474-4481.
Beckerle, M. C., Burridge, K., DeMartino, G. N. and Croall, D. E., 1987. Colocalization of
calcium-dependent protease II and one of its substrates at sites of cell adhesion. Cell 51:
569-577.
Bhatt, A., Kaverina, I., Otey, C. and Huttenlocher, A., 2002. Calpain regulates adhesive
complex composition and disassembly. J. Cell Science 115: 3415-3425.
Bialkowska, K., Kulkarni, S., Du, X., Goll, D. E., Saido, T. C. and Fox, J. E., 2000.
Evidence that beta3 integrin-induced Rac activation involves the calpain-dependent
formation of integrin clusters that are distinct from the focal complexes and focal
adhesions that form as Rac and RhoA become active. J. Cell Biol. 151: 685-696.
Burridge, K., Fath, K., Kelly, T., Nuckolls, G. and Turner, C., 1988. Focal adhesions:
transmembrane junctions between the extracellular matrix and the cytoskeleton. Annu.
Rev. Cell Biol. 4: 487-525.
Carragher, N. O., Levkau, B., Ross, R. and Raines, E. W., 1999. Degraded collagen
fragments promote rapid disassembly of smooth muscle focal adhesions that correlates
with cleavage of pp125(FAK), paxillin, and talin. J. Cell Biol. 147: 619-630.
Carragher, N. O., Westhoff, M. A., Riley, D., Potter, D. A., et al., 2002. v-Src-induced
modulation of the calpain-calpastatin proteolytic system regulates transformation. Mol.
Cell Biol. 22: 257-269.
Search WWH ::




Custom Search