The influence of Zn on signaling pathways and attachment of Mytilus galloprovincialis haemocytes to extracellular matrix proteins.
The present study investigates the cytotoxic mechanisms induced by zinc (Zn) in haemocytes of mussel Mytilus galloprovincialis. Haemocytes play a key role in the immune defence of mussels. Micromolar concentration of Zn (50 microM) play an important role in the elevation of pHi and increase in Na+ influx in haemocytes. The observed effects were inhibited by the Na+/H+ exchanger (NHE) inhibitor, ethyl-N-isopropyl-amiloride (EIPA). Furthermore, our results showed that Zn caused an increase in O(-)(2) production that was reversed after NHE inhibition. Phorbol ester (PMA) caused a significant rise both in pHi and Na+ influx as well as in O(-)(2) production. These effects were reversed by calphostin C. Our results indicated that Zn also enhanced haemocyte attachment to both BSA and laminin which was reversed by EIPA and calphostin C. The enhancement of haemocytes attachment to both BSA and laminin after Zn suggests that it is likely to play a signal role in cytoskeleton-dependent process of cell growth and migration in mussel M. galloprovincialis haemocytes. We conclude that Zn induces a signaling pathway with the involvement of NHE, PKC, O(-)(2) and alpha1- and beta-adrenergic receptors.
Kaloyianni
Martha
M
Laboratory of Animal Physiology, Zoology Department, School of Biology, Faculty of Science, Aristotle University of Thessaloniki, Thessaloniki, Greece. Kaloyian@bio.auth.gr
Ragia
Vaia
V
Tzeranaki
Irini
I
Dailianis
Stefanos
S
D000818:Animals; D002448:Cell Adhesion / Q000187:drug effects / Q000502:physiology; D002478:Cells, Cultured; D006434:Hemocytes / Q000187:drug effects* / Q000502:physiology; D006863:Hydrogen-Ion Concentration; D007797:Laminin / Q000378:metabolism; D049878:Mytilus / Q000187:drug effects* / Q000502:physiology; D011493:Protein Kinase C / Q000378:metabolism; D012710:Serum Albumin, Bovine / Q000378:metabolism; D015398:Signal Transduction / Q000187:drug effects; D012964:Sodium / Q000378:metabolism; D017923:Sodium-Hydrogen Exchangers / Q000378:metabolism; D013481:Superoxides / Q000378:metabolism; D015032:Zinc / Q000633:toxicity*
D007797:Laminin; D017923:Sodium-Hydrogen Exchangers; C121346:laminin 1; D013481:Superoxides; D012710:Serum Albumin, Bovine; D012964:Sodium; D011493:Protein Kinase C; D015032:Zinc