ArticleNeuroscience bulletin2009
Pro-protein convertase-2/carboxypeptidase-E mediated neuropeptide processing of RGC-5 cell after in vitro ischemia.
Article in Neuroscience bulletin, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. It has been retracted, and should not be counted. Cited by 5 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
5 citing papers in PubMed, 5 citations in OpenAlex.
- Differential proteomics of tobacco seedling roots at high and low potassium concentrations.Scientific reports · 2021Article
- Differential processing of neuropeptide proprotein in human breast adenocarcinoma.Journal of endocrinological investigation · 2013Article
- New roles of carboxypeptidase E in endocrine and neural function and cancer.Endocrine reviews · 2012Review
- Sensitivity of staurosporine-induced differentiated RGC-5 cells to homocysteine.Current eye research · 2010Article
- PC2/CPE-mediated pro-protein processing in tumor cells and its differentiated cells or tissues.Molecular and cellular endocrinology · 2009Article
Corrections and comments
- Retraction · 2009-05-19Copyright Claims ·
- Retracted
Authors and funding
5 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
objectiveTo observe the change of the neuropeptide pro-protein processing system in the ischemic retina ganglion cell-5 (RGC-5) cells, pro-protein convertase-2 (PC2), carboxypeptidase-E (CPE) and preproneuropeptide Y (preproNPY) protein levels in the ischemic RGC-5 cells and conditioned medium were analyzed.
methodsThe RGC-5 cell was differentiated in 0.1 mumol/L staurosporine for 24 h and then stressed by different doses of oxygen and glucose deprivation (OGD). The acute or chronic OGD-induced cell death rates were obtained by using PI or TUNEL staining. The protein expression levels were determined by using the Western blot method and PC2 activity analysis.
resultsThe ischemia caused substantial cell death in an OGD dose-dependent manner. In the cells, proPC2 and preproNPY protein levels gradually increased whereas proCPE gradually decreased. After OGD, PC2 activity was decreased. In the conditioned medium, proPC2 and PC2 proteins gradually decreased whereas proCPE, CPE, and preproNPY proteins gradually increased.
conclusionThese results demonstrated that OGD inhibited the neuropeptide pro-protein processing system by reducing PC2 activity and the maturation of proPC2. The aggregation of the pro-proteins and the increase of the active CPE excision adversely exacerbated the cell injury. The pro-protein processing system might play a critical role in the ischemic stress of RGC-5 cells.
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