Antigen receptor-mediated activation of extracellular related kinase (ERK) in B lymphocytes of teleost fishes

MacDougal, Kent C.; Mericko, Patricia; Burnett, Karen G.

doi:10.1016/s0145-305x(99)00006-3

Cited by 23 publications

(13 citation statements)

References 22 publications

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“…Our observations are consistent with a study of peripheral blood lymphocytes from red drum, Sciaenops ocellatus L. and channel cat fish, Ictalurus punctatus R., demonstrating the presence of PMA-sensitive ERK proteins of 43 and 46·kDa (MacDougal et al, 1999). Furthermore, p38ERK is probably …”

Section: P44erk Activity During Anoxia/recoverysupporting

confidence: 92%

“…After 5·min, p38ERK was phosphorylated sevenfold, with respect to serum starved cells. This was followed by a decreasing level of phosphorylation, reaching a minimum after 15·min before peaking again at 20·min.Our observations are consistent with a study of peripheral blood lymphocytes from red drum, Sciaenops ocellatus L. and channel cat fish, Ictalurus punctatus R., demonstrating the presence of PMA-sensitive ERK proteins of 43 and 46·kDa (MacDougal et al, 1999). Furthermore, p38ERK is probably …”

supporting

confidence: 92%

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Regulation of the mitogen-activated protein kinase p44 ERK activity during anoxia/recovery in rainbow trout hypodermal fibroblasts

Ossum

Wulff

Hoffmann

2006

Journal of Experimental Biology

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THE JOURNAL OF EXPERIMENTAL BIOLOGY1766 signalling has been the subject for a number of studies. However, most studies have focussed on specialised mammalian tissues, such as cardiovascular cell types, specialised epithelial cells and neurons. In the whole rat heart, ERK2 is inactivated in response to ischemia, followed by translocation of the inactive kinase to the nuclear compartment . Interestingly, ERK2 was activated in response to reperfusion, suggesting an interface capable of ERK activation in the nuclear membrane. Using the rat myocyte cell line H9c2, which has been shown to display ERK activities similar to those seen in whole organs during oxidative and metabolic stress (Abas et al., 2000), it was demonstrated that the ischemic nuclear translocation of ERK2 was dependent on both phosphatidyl inositol 3-kinase (PI 3-kinase) and the atypical protein kinase C (PKC) isoform PKC Mizukami et al., 2000). Hypoxia also stimulates ERK1/2 phosphorylation in vascular smooth muscle cells (Blaschke et al., 2002). To our knowledge, there are no studies on the effect of anoxia on ERK signalling in fish cells.Previously, we demonstrated a rapid, but transient activation of p38MAPK during chemical anoxia in rainbow trout hypodermal fibroblasts (RTHDF) (Ossum et al., 2004). Such an activation of p38 MAPK by anoxic insults have previously been reported in perfused hearts (Bogoyevitch et al., 1996;Nakano et al., 2000), ventricular myocytes (Saurin et al., 2000), H9c2 cells (Jung et al., 2004) and in neuronal tissues (Conrad et al., 1999;Harper and LoGrasso, 2001;Zhu et al., 2002). These studies demonstrate multiple functions of p38 MAPK . In PC12 cells, activation of p38 MAPK inhibits expression of cyclin D1 (Conrad et al., 1999) and in primary neurons, p38MAPK stabilises p53 and inhibits transformed mouse 3T3 cell double minute 2 (Mdm2) . Studies of vascular tissue demonstrate activation of mitogen-activated protein kinaseactivated protein kinase 2 (MAPKAP K-2) downstream of p38 MAPK (Bogoyevitch et al., 1996;Nakano et al., 2000). In primary rat astrocytes, p38 MAPK signalling has been implicated in induction of Hsp70 (Uehara et al., 1999). Together, these studies demonstrate roles for p38 MAPK in both cell death and protection. There are several observations showing cross-talk between p38MAPK and ERK (e.g. Singh et al., 1999). Thus it is probable that the observed activation of p38 MAPK could be followed by an inhibition of ERK.The present study was initiated to determine the effects of chemical anoxia, as well as nitrogen-induced anoxia and recovery on p44ERK activity in RTHDF (Ossum et al., 2004), originating from the rainbow trout Oncorhynchus mykiss L. Here, we report that both chemical anoxia induced by sodium azide, as well as true anoxia (P O 2<0.1%) result in inhibition of p44ERK during azide treatment and that p44ERK is dramatically activated in response to recovery. In the chemical anoxia model we find that inhibition of p44ERK activity during anoxia is dependent on p38 MAPK activity, whereas its activation ...

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Section: P44erk Activity During Anoxia/recoverysupporting

confidence: 92%

supporting

confidence: 92%

Regulation of the mitogen-activated protein kinase p44 ERK activity during anoxia/recovery in rainbow trout hypodermal fibroblasts

Ossum

Wulff

Hoffmann

2006

Journal of Experimental Biology

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“…It has also been previously reported that PMA stimulation of fish lymphocytes also uses ERK1/2 signaling [31]. Our current supposition is that early exposure to activate this pathway may lead to a lack of response to subsequent signals.…”

Section: Tablesupporting

confidence: 61%

Effects of low concentration of endosulfan on proliferation, ERK1/2 pathway, apoptosis and senescence in Nile tilapia (Oreochromis niloticus) splenocytes

Téllez‐Bañuelos

Ortiz‐Lazareno

Santerre

et al. 2011

Fish & Shellfish Immunology

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“…Likewise, in the present work, molecular responses to acute temperature and CO 2 stress were assessed by examining three interrelated cellular pathways intimately involved in the cellular stress response (stress signaling, energy metabolism and redox balance) using well-established indicators. Representative traits of the stress signaling pathway are HSPs (heat shock proteins) which are often used as proxies for the cellular stress responses of marine organisms (Hofmann 2005;Iwama et al 1998;Iwama 1999;Tomanek 2010;Tomanek et al 2011;Yamashita et al 2010) and members of the MAPK (mitogen-activated protein kinases) family, [p38 MAPK, ERK1/2 (p44/42 MAPK) and JNKs (cJun-N-terminal kinases)] which all have been identified in fish Feidantsis et al 2009;Fujii et al 2000;Hashimoto et al 1997Hashimoto et al , 1998Kültz and Avila 2001;MacDougal et al 1984). Moreover, ubiquitylation is a potential indicator for damaged proteins and their removal by the proteasome (Ciechanover 1998).…”

Section: Introductionmentioning

confidence: 99%

Synergistic effects of acute warming and low pH on cellular stress responses of the gilthead seabream Sparus aurata

et al. 2014

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The present study assesses the resilience of the Mediterranean gilthead seabream (Sparus aurata) to acute warming and water acidification, using cellular indicators of systemic to molecular responses to various temperatures and CO2 concentrations. Tissue metabolic capacity derived from enzyme measurements, citrate synthase, 3-hydroxyacyl CoA dehydrogenase (HOAD), as well as lactate dehydrogenase. Cellular stress and signaling responses were identified from expression patterns of Hsp70 and Hsp90, the phosphorylation of p38 MAPK, JNKs and ERKs, from protein ubiquitylation and finally from the levels of transcription factor Hif-1α as an indicator of systemic hypoxemia. Exposure to elevated CO2 levels at temperatures higher than 24 °C generally caused an increase in fish mortality above the rate caused by warming alone, indicating effects of the two factors and a failure of acclimation and thus the limits of phenotypic plasticity to be reached. As a potential reason, tissue-dependent induction and stabilization of Hif-1α indicate hypoxemic conditions. Their exacerbation by enhanced CO2 levels is linked to the persistent expression of Hsp70 and Hsp90, oxidative stress and activation of MAPK and ubiquitin pathways. Antioxidant defence is enhanced by expression of catalase and glutathione reductase, however, leaving superoxide dismutase suppressed by elevated CO2 levels. On longer timescales in specimens surviving warming and CO2 exposures, various metabolic adjustments initiate a preference to oxidize lipid via HOAD for energy supply. These processes indicate significant acclimation up to a limit and a time-limited capacity to survive extreme conditions passively by exploiting mechanisms of cellular resilience.

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Antigen receptor-mediated activation of extracellular related kinase (ERK) in B lymphocytes of teleost fishes

Cited by 23 publications

References 22 publications

Regulation of the mitogen-activated protein kinase p44 ERK activity during anoxia/recovery in rainbow trout hypodermal fibroblasts

Regulation of the mitogen-activated protein kinase p44 ERK activity during anoxia/recovery in rainbow trout hypodermal fibroblasts

Effects of low concentration of endosulfan on proliferation, ERK1/2 pathway, apoptosis and senescence in Nile tilapia (Oreochromis niloticus) splenocytes

Synergistic effects of acute warming and low pH on cellular stress responses of the gilthead seabream Sparus aurata

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