“…Both bead adhesion and calcium signaling are specific to RGD and are decreased by antibodies that inhibit the function of av133 and avP35 integrins (Sjaastad et al, 1994 We examined the dependence of (Paulmichl et al, 1990). Ca2+ release occurs because of activation of phospholipase C and generation of IP3 via a phorbol ester and pertussis toxin-sensitive mechanism (Paulmichl et al, 1990 , 1993), tyrosine phosphorylation-dependent activation of phospholipase C (Kanner et al, 1993;Blake et al, 1994;Somogyi et al, 1994), and production of IP3 (Sultan et al, 1991;Somogyi et al, 1994 (Hill et al, 1987;Ghosh et al, 1988;Harootunian et al, 1991). MDCK cells were preloaded by electroporation in the presence of low-molecularweight heparin or unlabeled CS as a control (Boitano et al, 1992) (Figure 6c), whereas identical concentrations of CS had little or no effect (Figure 6d (Thastrup et al, 1990) Ca2" channels have been described (Fasolato et al, 1994) and that MDCK cells contain at least two known Ca2" entry pathways (Dietl and Volkl, 1994;Delles et al, 1995 (Figure 8b (Sjaastad et al, 1994 potent regulator of integrin-mediated adhesion to RGD than is Ca21 store release.…”