Manganese overload affects p38 MAPK phosphorylation and metalloproteinase activity during sea urchin embryonic development
In the marine environment, manganese represents a potential emerging contaminant, resulting from an increased production of manganese-containing compounds. In earlier reports we found that the exposure of Paracentrotus lividus sea urchin embryos to manganese produced phenotypes with no skeleton. In...
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Published in | Marine environmental research Vol. 93; pp. 64 - 69 |
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Main Authors | , , |
Format | Journal Article Conference Proceeding |
Language | English |
Published |
Oxford
Elsevier Ltd
01.02.2014
Elsevier |
Subjects | |
Online Access | Get full text |
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Summary: | In the marine environment, manganese represents a potential emerging contaminant, resulting from an increased production of manganese-containing compounds. In earlier reports we found that the exposure of Paracentrotus lividus sea urchin embryos to manganese produced phenotypes with no skeleton. In addition, manganese interfered with calcium uptake, perturbed extracellular signal-regulated kinase (ERK) signaling, affected the expression of skeletogenic genes, and caused an increase of the hsc70 and hsc60 protein levels. Here, we extended our studies focusing on the temporal activation of the p38 mitogen-activated protein kinase (p38 MAPK) and the proteolytic activity of metalloproteinases (MMPs). We found that manganese affects the stage-dependent dynamics of p38 MAPK activation and inhibits the total gelatin-auto-cleaving activity of MMPs, with the exclusion of the 90–85 kDa and 68–58 kDa MMPs, whose levels remain high all throughout development. Our findings correlate, for the first time to our knowledge, an altered activation pattern of the p38 MAPK with an aberrant MMP proteolytic activity in the sea urchin embryo.
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•Mn represents a potential emerging contaminant in the environment.•Mn blocks the modulation of p38 MAPK phosphorylation occurring during normal sea urchin embryonic development.•Mn overload inhibits the total gelatin-auto-cleaving activity of metalloproteinases from gastrula to pluteus stage.•Mn causes a strong activity of specific subsets of MMPs having apparent molecular weights of 90–85 kDa and 68–58 kDa. |
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ISSN: | 0141-1136 1879-0291 |
DOI: | 10.1016/j.marenvres.2013.08.004 |