Regulation of motility of cells from marine sponges by calcium ions.
Sponges are known not to contain muscle and nerve cells. Since sponge cells are characterized by high motility we determined the effect of intracellular calcium ion concentration ([Ca2+]i) on their motility. Addition of the Ca2+ ionophore ionomycin to dissociated cells from the marine sponge Suberites domuncula caused in Ca(2+)-containing artificial seawater (ASW) an increase in motility from 0.2 micron/min (absence of the ionophore) to 3.7 microns/min (presence of ionomycin). When the experiments were performed in Ca(2+)-free medium, no effect of ionomycin could be observed. In parallel experiments the changes of [Ca2+]i using the dye Fura-2 were measured. The experiments revealed that ionomycin causes an influx of Ca2+ into the cytosol of cells suspended in Ca(2+)-containing artificial seawater. In contrast, if cells were suspended in Ca(2+)-free artificial seawater, no increase of [Ca2+]i occurred. Incubation of cells in the presence of inhibitors, specific for endoplasmatic Ca(2+)-ATPase in mammals such as thapsigargin, cyclopiazonic acid, or 2,5 di-t-butylhydrochinone, did not influence the [Ca2+]i if cells were suspended in Ca(2+)-free artificial seawater. From these data we conclude that the [Ca2+]i is primarily regulated through channels in the plasma membrane. In addition we summarize experimental evidence indicating that the [Ca2+]i is involved in the control of cell motility. From the marine sponge Geodia cydonium a partial sequence of the myosin cDNA has been cloned. The deduced amino acid sequence comprises highest homology to nonmuscle myosin type II found in higher invertebrates and vertebrates. Taken together, these data show that the [Ca2+]i level in sponge cells can be modulated by incubation with ionomycin. An increase of the Ca2+ level parallels with higher motility of cells, suggesting an activation of Ca(2+)-dependent protein kinases of myosin type II. Investigations on the ionomycin-activated influx of Ca2+ into the cytosol revealed that predominantly the Ca2+ channels in plasma membrane control the level of [Ca2+]i.
Lorenz
B
B
Institut, für Biochemie, Universität, Magdeburg, Germany.
Bohnensack
R
R
Gamulin
V
V
Steffen
R
R
Müller
W E
WE
D000595:Amino Acid Sequence; D000818:Animals; D002118:Calcium / Q000502:physiology*; D002465:Cell Movement / Q000502:physiology*; D005456:Fluorescent Dyes; D016257:Fura-2; D006801:Humans; D015759:Ionomycin / Q000494:pharmacology; D007476:Ionophores / Q000494:pharmacology; D007477:Ions; D008969:Molecular Sequence Data; D009218:Myosins / Q000737:chemistry; D011161:Porifera / Q000166:cytology / Q000502:physiology*; D012623:Seawater; D017386:Sequence Homology, Amino Acid
D005456:Fluorescent Dyes; D007476:Ionophores; D007477:Ions; D015759:Ionomycin; D009218:Myosins; D002118:Calcium; D016257:Fura-2