Cold acclimation-induced up-regulation of the ribosomal protein L7 gene in the freeze tolerant wood frog, Rana sylvatica

Wu, Shaobo; Croos, J.N. Amritha De; Storey, Kenneth B.

doi:10.1016/j.gene.2008.07.023

Cited by 35 publications

(26 citation statements)

References 38 publications

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“…Previous studies have shown that brain IP 3 levels rose significantly after 4 h of freezing (Holden & Storey, 1996), and so this is one frog tissue in which the overall increases in PKC phosphorylation state correlate with this rise in IP 3 . Numerous other adaptive “activations” occur in frog brains in response to freezing, including: (1) moderately-increased expression of fr10 (Cai & Storey, 1997) and li16 (Sullivan & Storey, 2012), novel genes with putative roles in freezing protection; (2) increased levels of c-Fos (Greenway & Storey, 2000), and; (3) up-regulation of genes for ribosomal proteins, including the acidic ribosomal phosphoprotein P0 (Wu & Storey, 2005) and the ribosomal large subunit protein 7 (Wu, De Croos & Storey, 2008). At present, however, we cannot conclusively identify any of the proteins listed here as being substrates of PKC, nor can we confirm that any of the upregulated-genes are facilitated by transcription factors downstream of PKC.…”

Section: Resultsmentioning

confidence: 99%

Protein kinase C in the wood frog,Rana sylvatica: reassessing the tissue-specific regulation of PKC isozymes during freezing

Dieni

Storey

2014

PeerJ

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The wood frog, Rana sylvatica, survives whole-body freezing and thawing each winter. The extensive adaptations required at the biochemical level are facilitated by alterations to signaling pathways, including the insulin/Akt and AMPK pathways. Past studies investigating changing tissue-specific patterns of the second messenger IP3 in adapted frogs have suggested important roles for protein kinase C (PKC) in response to stress. In addition to their dependence on second messengers, phosphorylation of three PKC sites by upstream kinases (most notably PDK1) is needed for full PKC activation, according to widely-accepted models. The present study uses phospho-specific immunoblotting to investigate phosphorylation states of PKC—as they relate to distinct tissues, PKC isozymes, and phosphorylation sites—in control and frozen frogs. In contrast to past studies where second messengers of PKC increased during the freezing process, phosphorylation of PKC tended to generally decline in most tissues of frozen frogs. All PKC isozymes and specific phosphorylation sites detected by immunoblotting decreased in phosphorylation levels in hind leg skeletal muscle and hearts of frozen frogs. Most PKC isozymes and specific phosphorylation sites detected in livers and kidneys also declined; the only exceptions were the levels of isozymes/phosphorylation sites detected by the phospho-PKCα/βII (Thr638/641) antibody, which remained unchanged from control to frozen frogs. Changes in brains of frozen frogs were unique; no decreases were observed in the phosphorylation levels of any of the PKC isozymes and/or specific phosphorylation sites detected by immunoblotting. Rather, increases were observed for the levels of isozymes/phosphorylation sites detected by the phospho-PKCα/βII (Thr638/641), phospho-PKCδ (Thr505), and phospho-PKCθ (Thr538) antibodies; all other isozymes/phosphorylation sites detected in brain remained unchanged from control to frozen frogs. The results of this study indicate a potential important role for PKC in cerebral protection during wood frog freezing. Our findings also call for a reassessment of the previously-inferred importance of PKC in other tissues, particularly in liver; a more thorough investigation is required to determine whether PKC activity in this physiological situation is indeed dependent on phosphorylation, or whether it deviates from the generally-accepted model and can be “overridden” by exceedingly high levels of second messengers, as has been demonstrated with certain PKC isozymes (e.g., PKCδ).

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Section: Resultsmentioning

confidence: 99%

Protein kinase C in the wood frog,Rana sylvatica: reassessing the tissue-specific regulation of PKC isozymes during freezing

Dieni

Storey

2014

PeerJ

Self Cite

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“…Diminished protein synthesis is reflected in the lowered abundance of regulatory proteins, including mRNA transport regulator and elongation factor 1-α (EF1-α), a central component of the active translation and elongation machinery. R. sylvatica up-regulates translation of the ribosomal protein L7 gene, whose product is thought to inhibit translation, during cold acclimation [6]. …”

Section: Resultsmentioning

confidence: 99%

Seasonal Variation in the Hepatoproteome of the Dehydration- and Freeze-Tolerant Wood Frog, Rana sylvatica

Kiss

Muir

Lee

et al. 2011

IJMS

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Winter’s advent invokes physiological adjustments that permit temperate ectotherms to cope with stresses such as food shortage, water deprivation, hypoxia, and hypothermia. We used liquid chromatography (LC) in combination with tandem mass spectrometry (MS/MS) quantitative isobaric (iTRAQ™) peptide mapping to assess variation in the abundance of hepatic proteins in summer- and winter-acclimatized wood frogs (Rana sylvatica), a northerly-distributed species that tolerates extreme dehydration and tissue freezing during hibernation. Thirty-three unique proteins exhibited strong seasonal lability. Livers of winter frogs had relatively high levels of proteins involved in cytoprotection, including heat-shock proteins and an antioxidant, and a reduced abundance of proteins involved in cell proliferation, protein synthesis, and mitochondrial function. They also exhibited altered levels of certain metabolic enzymes that participate in the biochemical reorganization associated with aphagia and reliance on energy reserves, as well as the freezing mobilization and post-thaw recovery of glucose, an important cryoprotective solute in freezing adaptation.

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“…In the context of sexual differentiation of zebra finch song system, Tang et al showed that genes encoding ribosomal proteins L17 and L37 were specifically upregulated in the song control nuclei of the forebrain of developing males [67]. To determine the genes involved in freeze tolerance of wood frog, which can survive after freezing in winter, Wu et al analyzed the gene expression profiles of cold-and warm-acclimated frogs and observed that expression of the gene encoding ribosomal large subunit protein 7 (RPL7) was specifically upregulated in the skin of cold-acclimated frogs [68].…”

Section: Specific Functions Of Ribosomal Proteinsmentioning

confidence: 99%

Emerging roles of nucleolar and ribosomal proteins in cancer, development, and aging

Takada

Kurisaki

2015

Cell. Mol. Life Sci.

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Changes in nucleolar morphology and function are tightly associated with cellular activity, such as growth, proliferation, and cell cycle progression. Historically, these relationships have been extensively examined in cancer cells, which frequently exhibit large nucleoli and increased ribosome biogenesis. Recent findings indicate that alteration of nucleolar activity is a key regulator of development and aging. In this review, we have provided evidences that the nucleolus is not just a housekeeping factor but is actively involved in the regulation of cell proliferation, differentiation, and senescence both in vitro and in vivo. In addition, we have discussed how alteration of nucleolar function and nucleolar proteins induces specific physiological effects rather than widespread effects.

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Cold acclimation-induced up-regulation of the ribosomal protein L7 gene in the freeze tolerant wood frog, Rana sylvatica

Cited by 35 publications

References 38 publications

Protein kinase C in the wood frog,Rana sylvatica: reassessing the tissue-specific regulation of PKC isozymes during freezing

Protein kinase C in the wood frog,Rana sylvatica: reassessing the tissue-specific regulation of PKC isozymes during freezing

Seasonal Variation in the Hepatoproteome of the Dehydration- and Freeze-Tolerant Wood Frog, Rana sylvatica

Emerging roles of nucleolar and ribosomal proteins in cancer, development, and aging

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