Anti-PCNA Anticorps (A28083)

The metabolic activity in cancer cells primarily rely on aerobic glycolysis. Besides glycolysis, some tumor cells also exhibit excessive addition to glutamine, which constitutes an advantage for tumor growth. M2-type pyruvate kinase (PKM2) plays a pivotal role in sustaining aerobic glycolysis, pentose phosphate pathway and serine synthesis pathway. However, the participation of PKM2 in glutaminolysis is little to be known. Here we demonstrated that PKM2 depletion could provoke glutamine metabolism by enhancing the β-catenin signaling pathway and consequently promoting its downstream c-Myc-mediated glutamine metabolism in colon cancer cells. Treatment with 2-deoxy-d-glucose (2-DG), a glycolytic inhibitor, got consistent results with the above. In addition, the dimeric form of PKM2, which lacks the pyruvate kinase activities, plays a critical role in regulating β-catenin. Moreover, we found that overexpression of PKM2 negatively regulated β-catenin through miR-200a. These insights supply evidence that glutaminolysis plays a compensatory role for cell survival upon glucose metabolism impaired.

Healthy SD rats were randomly divided into 3 groups as sham operation (group A), ICH (group B), and HBO2 (group C). The behavioral change and angiogenesis in brain tissue of rats in each group were observed. The protein expression of PCNA, vWF, HIF1-α, and VEGF in rat brain was measured by immunohistochemistry, while the mRNA expression level of HIF1-α and VEGF was determined using quantitative real-time PCR. This study has investigated the effect of HBO2 on intracephalic angiogenesis in rats with intracerebral hemorrhage (ICH). There were significant differences in behavior score between HBO2 and ICH groups at 14, 21, and 28 days. A large number of vessel-like structures and microvessels were observed in perihematomal brain tissues in HBO2 group. There were significant differences in HIF1-α and VEGF protein and HIF1-α mRNA level between HBO2 and ICH groups at 14, 21, and 28 days; at 7, 14, 21, and 28 days, the differences in PCNA and vWF protein expression between the 2 groups were statistically significant. At 21 and 28 days, the expression levels of VEGF mRNA in the 2 groups differed significantly from each other. Our results indicate that HBO2 can significantly promote the expression of HIF1-α and VEGF at both mRNA and protein levels in rats with ICH, increase the protein expression of both PCNA and vWF, promote the formation of new blood vessels, and promote the recovery of behavioral ability, hence resulting in a rapid rehabilitation.

The epidermal growth factor receptor (EGFR) is an important receptor tyrosine kinase member in animals, which plays versatile functions in development, growth, tissue regeneration etc. Current knowledge on EGFR is poor in bivalve mollusks. In this study, we cloned and analyzed an EGFR gene from the Pacific oyster Crassostrea gigas (cgegfr). A 5,731 bp full-length cDNA of cgegfr was obtained, encoding a peptide with 1,494 amino acids which exhibited a typical EGFR structure, including an extracellular region, a single transmembrane region and an intracellular region. A conserved tyrosine kinase domain was predicted in the intracellular region, while the extracellular region responsible for ligand binding showed comparatively poor conservation. Expression analysis revealed that cgefgr was expressed widely in C. gigas tissues and a highest expression level was observed in adductor tissue. Expression of cgegfr was revealed to be up-regulated during wound healing of mantle, indicating that EGFR might function in the cell proliferation and migration during wound healing. Further functional analysis of cgegfr was conducted in mouse myoblast cell line C2C12, in which different parts of cgegfr were expressed and their effects were measured. The results revealed that cgegfr was able to accelerate cell proliferation of C2C12 cells and the transmembrane region was necessary for self-activation of truncated cgegfr. Our results would provide supports for further studies on the roles of cgegfr in development and growth in C. gigas.