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Vol. 11, Issue 4, 1433-1443, April 2000
and
*Department of Life Science, Kwangju Institute of Science and
Technology, Kwangju 500-712, Korea; and The engagement of integrin Department of
Cell and Structural Biology, University of Illinois, Urbana, Illinois
61801
7 in E63 skeletal muscle
cells by laminin or anti-7 antibodies triggered transient elevations in the intracellular free Ca2+ concentration that resulted
from both inositol triphosphate-evoked Ca2+
release from intracellular stores and extracellular Ca2+
influx through voltage-gated, L-type Ca2+ channels. The
extracellular domain of integrin 7 was found to associate
with both ectocalreticulin and dihydropyridine receptor on the cell
surface. Calreticulin appears to also associate with cytoplasmic domain
of integrin 7 in a manner highly dependent on the cytosolic
Ca2+ concentration. It appeared that intracellular
Ca2+ release was a prerequisite for Ca2+ influx
and that calreticulin associated with the integrin cytoplasmic domain mediated the coupling of between the Ca2+ release
and Ca2+ influx. These findings suggest that calreticulin
serves as a cytosolic activator of integrin and a signal
transducer between integrins and Ca2+ channels on
the cell surface.
Corresponding author. E-mail address:
wksong{at}pia.kjist.ac.kr.
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