tailieunhanh - Báo cáo khoa học: Long-term extracellular signal-related kinase activation following cadmium intoxication is negatively regulated by a protein kinase C-dependent pathway affecting cadmium transport

Extracellular signal-related kinase (ERK) is a well-known kinase taking part in a signal transduction cascade in response to extracellular stimuli. ERK is generally viewed as a kinase that is rapidly and transiently phos-phorylated following mitogenic stimulation. | ỊFEBS Journal Long-term extracellular signal-related kinase activation following cadmium intoxication is negatively regulated by a protein kinase C-dependent pathway affecting cadmium transport Patrick Martin Kim E. Boulukos Marie C. Poggi and Philippe Pognonec CNRS FRE3094 Université de Nice Sophia Antipolis France Keywords cadmium extracellular signal-related kinase ERK protein kinase C PKC sustained activation ZIP8 Correspondence P. Pognonec TranscriptionalRegulation and Differentiation CNRS FRE3094 Universite de Nice Parc Valrose 06108 Nice cedex 2 France Fax Tel 33 492 07 64 13 E-mail pognonec@ Received 16 September 2008 revised 12 December 2008 accepted 12 January 2009 doi Extracellular signal-related kinase ERK is a well-known kinase taking part in a signal transduction cascade in response to extracellular stimuli. ERK is generally viewed as a kinase that is rapidly and transiently phosphorylated following mitogenic stimulation. This activation results in ERK phosphorylating further downstream targets thus transmitting and amplifying the original stimulus and ultimately resulting in the onset of cellular proliferation and or protection against apoptosis. More recently several groups have identified a strikingly new type of ERK activation that results in cell death. This activation is very different from conventional ERK activation as it occurs several hours after the original stimulation and results in the sustained phosphorylation of ERK which can be observed for up to several days. One way of inducing this delayed ERK activation is by low-dose cadmium treatment. We show here that sustained ERK activation induced by cadmium in human kidney-derived cells is inhibited following protein kinase C PKC activation even when this activation occurs hours before intoxication. Furthermore PKC inhibition results in an enhanced ERK activation in response to cadmium even when inhibition is induced hours before intoxication. PKCe .

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