Furthermore, the testretest reliability and responsiveness of the questionnaire were not evaluated in this study.\n\nOur study addresses the urgent need for a valid and reliable instrument to measure the HRQoL of female patients with endometriosis in mainland China.\n\nThis work was supported by grants to J. Leng from the Key Project for Clinical Faculty Foundation, Ministry of Health, China (2010). None of the authors has any conflict of interest to declare.”
“In this communication
our aim was to study the JK cell growth inhibitory and apoptosis-inducing effects of ginsenoside Rg6 (GRg6) from steamed notoginseng on human lymphocytoma. The CCK-8 method was used to observe the anti-proliferative effect of GRg6 Curaxin 137 HCl on human lymphocytoma JK cells. RG7440 Flow cytometry was performed to analyze the influence of
GRg6 on cell cycle. The Annexin-V FITC/PI double-staining method was used to detect the ratio of apoptotic cells. JC-1 staining was undertaken to observe the influence of GRg6 on intracellular mitochondrial membrane potential. Finally, western blots were conducted to detect the expression level of apoptosis-related Bax and the Bcl-2 proteins. The results suggested that GRg6 can inhibit the proliferation of human lymphocytoma JK cells. GRg6 blocks an S arrest in the cell cycle. With the increase in GRg6 concentration, the potential in the cell decreased in a dose dependent manner, and Bax protein expression gradually increased, whereas Bcl-2 protein expression gradually decreased. In conclusion, GRg6 can inhibit JK cell proliferation in human lymphocytoma and induce its apoptosis. The mechanism of action may be related to mitochondrial dysfunction and an increase of Bax expression and decrease of Bcl-2 expression Selleck GSK1120212 caused by GRg6.”
“Ubiquitination, the covalent attachment of ubiquitin to target proteins, has emerged as a ubiquitous post-translational modification (PTM) whose function extends far beyond its original role as a tag for
protein degradation identified three decades ago. Although sharing parallel properties with phosphorylation, ubiquitination distinguishes itself in important ways. Nevertheless, the interplay and crosstalk between ubiquitination and phosphorylation events have become a recurrent theme in cell signalling regulation. Understanding how these two major PTMs intersect to regulate signal transduction is an important research question. In this review, we first discuss the involvement of ubiquitination in the regulation of the EGF-mediated ERK signalling pathway via the EGF receptor, highlighting the interplay between ubiquitination and phosphorylation in this cancer-implicated system and addressing open questions. The roles of ubiquitination in pathways crosstalking to EGFR/MAPK signalling will then be discussed.