Updating Ohio\u27s Class Action Rules After More than Forty Years

In 1970, the Ohio Rules of Civil Procedure made their debut. The new set of rules included Civil Rule 23, governing procedure in class actions. Like most of the new Ohio civil rules, Rule 23 closely tracked its federal counterpart, Federal Rule of Civil Procedure 23, which itself was then relatively new, having been adopted in 1966. Since 1970, Ohio’s Rule 23 has sat untouched. In the meantime, the Ohio Supreme Court has amended other civil rules more than thirty times. During the more than forty years since Ohio Rule 23 was adopted, there have been significant changes in class-action practice and in the language of federal Rule 23. In 2003, the federal rule was substantially revised and improved to address a number of important issues not covered in the 1966 version of the rule. It is now time to update Ohio’s Rule 23 to better conform to the current federal rule and to address the realities of class actions today. Specifically, Ohio’s Rule 23 should be amended to incorporate the amendments to federal Rule 23 relating to the timing of the class certification decision, appointment of class counsel, notices to class members, and approval of proposed settlements. Those topics either are not treated at all in the current Ohio rule or are treated inadequately. Judges and litigants in Ohio courts deserve better guidance on the difficult procedural questions that can arise in class actions, and that guidance can come from sprucing up Ohio Rule 23 after more than forty years of benign neglect

Updating Ohio\u27s Class Action Rules After More than Forty Years

In 1970, the Ohio Rules of Civil Procedure made their debut. The new set of rules included Civil Rule 23, governing procedure in class actions. Like most of the new Ohio civil rules, Rule 23 closely tracked its federal counterpart, Federal Rule of Civil Procedure 23, which itself was then relatively new, having been adopted in 1966. Since 1970, Ohio’s Rule 23 has sat untouched. In the meantime, the Ohio Supreme Court has amended other civil rules more than thirty times. During the more than forty years since Ohio Rule 23 was adopted, there have been significant changes in class-action practice and in the language of federal Rule 23. In 2003, the federal rule was substantially revised and improved to address a number of important issues not covered in the 1966 version of the rule. It is now time to update Ohio’s Rule 23 to better conform to the current federal rule and to address the realities of class actions today. Specifically, Ohio’s Rule 23 should be amended to incorporate the amendments to federal Rule 23 relating to the timing of the class certification decision, appointment of class counsel, notices to class members, and approval of proposed settlements. Those topics either are not treated at all in the current Ohio rule or are treated inadequately. Judges and litigants in Ohio courts deserve better guidance on the difficult procedural questions that can arise in class actions, and that guidance can come from sprucing up Ohio Rule 23 after more than forty years of benign neglect

Scaling net ecosystem production and net biome production over a heterogeneous region in the western United States

Bottom-up scaling of net ecosystem production (NEP) and net biome production (NBP) was used to generate a carbon budget for a large heterogeneous region (the state of Oregon, 2.5×10<sup>5</sup> km<sup>2</sup>) in the western United States. Landsat resolution (30 m) remote sensing provided the basis for mapping land cover and disturbance history, thus allowing us to account for all major fire and logging events over the last 30 years. For NEP, a 23-year record (1980–2002) of distributed meteorology (1 km resolution) at the daily time step was used to drive a process-based carbon cycle model (Biome-BGC). For NBP, fire emissions were computed from remote sensing based estimates of area burned and our mapped biomass estimates. Our estimates for the contribution of logging and crop harvest removals to NBP were from the model simulations and were checked against public records of forest and crop harvesting. The predominately forested ecoregions within our study region had the highest NEP sinks, with ecoregion averages up to 197 gC m<sup>−2</sup> yr<sup>−1</sup>. Agricultural ecoregions were also NEP sinks, reflecting the imbalance of NPP and decomposition of crop residues. For the period 1996–2000, mean NEP for the study area was 17.0 TgC yr<sup>−1</sup>, with strong interannual variation (SD of 10.6). The sum of forest harvest removals, crop removals, and direct fire emissions amounted to 63% of NEP, leaving a mean NBP of 6.1 TgC yr<sup>−1</sup>. Carbon sequestration was predominantly on public forestland, where the harvest rate has fallen dramatically in the recent years. Comparison of simulation results with estimates of carbon stocks, and changes in carbon stocks, based on forest inventory data showed generally good agreement. The carbon sequestered as NBP, plus accumulation of forest products in slow turnover pools, offset 51% of the annual emissions of fossil fuel CO<sub>2</sub> for the state. State-level NBP dropped below zero in 2002 because of the combination of a dry climate year and a large (200 000 ha) fire. These results highlight the strong influence of land management and interannual variation in climate on the terrestrial carbon flux in the temperate zone

Epidermal growth factor induces HCCR expression via PI3K/Akt/mTOR signaling in PANC-1 pancreatic cancer cells

<p>Abstract</p> <p>Background</p> <p>Human cervical cancer oncoprotein 1 (HCCR-1), reported as a negative regulator of p53, is over-expressed in a variety of human cancers. However, it is yet unknown whether HCCR-1 plays any role in pancreatic cancer development. The aim of this study was to investigate the effect of epidermal growth factor on the expression of HCCR in pancreatic cancer cells, and to explore if PI3K/Akt/mTOR signaling pathway mediated this expression.</p> <p>Methods</p> <p>A polyclonal antibody against HCCR protein was raised by immunizing Balb/c mice with the purified recombinant protein pMBPc-HCCR. Tissue samples were constructed on a tissue chip, and the expression of HCCR was investigated by immunohistochemistry assay and Western blotting. Pancreatic cell line, PANC-1 cells were stably transfected with plasmids containing sense-HCCR-1 fragment and HCCR siRNA fragment. MTT and transwell assay were used to investigate the proliferation and invasion of stable tansfectants. The specific inhibitor of PI3K and mTOR was used to see if PI3K/mTOR signal transduction was involved in the induction of HCCR gene expression. A Luciferase assay was used to see if Akt can enhance the HCCR promoter activity.</p> <p>Results</p> <p>HCCR was up-regulated in pancreatic tumor tissues (mean Allred score 4.51 ± 1.549 <it>vs</it>. 2.87 ± 2.193, P < 0.01), especially with high expression in poorly differentiated pancreatic cancer. The growth of cells decreased in HCCR-1 siRNA transfected cells compared with vector transfectants. The number of invasion cells was significantly lower in HCCR-1 siRNA transfected cells (24.4 ± 9.9) than that in vector transfectants (49.1 ± 15.4). Treatment of PANC-1 cells with epidermal growth factor increased HCCR protein level in a dose- and time-dependent manner. However, application of LY294002 and rapamycin caused a dramatic reduction of epidermal growth factor-induced HCCR expression. Over-expression of exogenous constitutively active Akt increased the HCCR promoter activity; in contrast, dominant negative Akt decreased the promoter activity.</p> <p>Conclusions</p> <p>EGF-induced HCCR-1 over-expression is mediated by PI3K/AKT/mTOR signaling which plays a pivotal role in pancreatic tumor progression, suggesting that HCCR-1 could be a potential target for cancer therapeutics.</p

Metabolites of Purine Nucleoside Phosphorylase (NP) in Serum Have the Potential to Delineate Pancreatic Adenocarcinoma

Pancreatic Adenocarcinoma (PDAC), the fourth highest cause of cancer related deaths in the United States, has the most aggressive presentation resulting in a very short median survival time for the affected patients. Early detection of PDAC is confounded by lack of specific markers that has motivated the use of high throughput molecular approaches to delineate potential biomarkers. To pursue identification of a distinct marker, this study profiled the secretory proteome in 16 PDAC, 2 carcinoma in situ (CIS) and 7 benign patients using label-free mass spectrometry coupled to 1D-SDS-PAGE and Strong Cation-Exchange Chromatography (SCX). A total of 431 proteins were detected of which 56 were found to be significantly elevated in PDAC. Included in this differential set were Parkinson disease autosomal recessive, early onset 7 (PARK 7) and Alpha Synuclein (aSyn), both of which are known to be pathognomonic to Parkinson's disease as well as metabolic enzymes like Purine Nucleoside Phosphorylase (NP) which has been exploited as therapeutic target in cancers. Tissue Microarray analysis confirmed higher expression of aSyn and NP in ductal epithelia of pancreatic tumors compared to benign ducts. Furthermore, extent of both aSyn and NP staining positively correlated with tumor stage and perineural invasion while their intensity of staining correlated with the existence of metastatic lesions in the PDAC tissues. From the biomarker perspective, NP protein levels were higher in PDAC sera and furthermore serum levels of its downstream metabolites guanosine and adenosine were able to distinguish PDAC from benign in an unsupervised hierarchical classification model. Overall, this study for the first time describes elevated levels of aSyn in PDAC as well as highlights the potential of evaluating NP protein expression and levels of its downstream metabolites to develop a multiplex panel for non-invasive detection of PDAC

Molecular and pathological signatures of epithelial–mesenchymal transitions at the cancer invasion front

Reduction of epithelial cell–cell adhesion via the transcriptional repression of cadherins in combination with the acquisition of mesenchymal properties are key determinants of epithelial–mesenchymal transition (EMT). EMT is associated with early stages of carcinogenesis, cancer invasion and recurrence. Furthermore, the tumor stroma dictates EMT through intensive bidirectional communication. The pathological analysis of EMT signatures is critically, especially to determine the presence of cancer cells at the resection margins of a tumor. When diffusion barriers disappear, EMT markers may be detected in sera from cancer patients. The detection of EMT signatures is not only important for diagnosis but can also be exploited to enhance classical chemotherapy treatments. In conclusion, further detailed understanding of the contextual cues and molecular mediators that control EMT will be required in order to develop diagnostic tools and small molecule inhibitors with potential clinical implications