We established an AQP4-Ab ELISA, which could be a potential monitoring tool of disease activity.

There has been considerable interest in virulence genes in the plasticity region of Helicobacter pylori, but little is known about many of these genes. JHP940, one of the virulence factors encoded by the plasticity region of H. pylori strain J99, is a proinflammatory protein that induces tumor necrosis factor-alpha and interleukin-8 secretion as well as enhanced translocation of NF-κB in cultured macrophages. Here we have characterized the structure and function of JHP940 to provide the framework for better understanding its role in inflammation by H. pylori. Our work demonstrates that JHP940 is the first example of a eukaryotic-type Ser/Thr kinase from H. pylori. We show that JHP940 is catalytically active as a protein kinase and translocates into cultured human cells. Furthermore, the kinase activity is indispensable for indirectly up-regulating phosphorylation of NF-κB p65 at Ser276. Our results, taken together, contribute significantly to understanding the molecular basis of the role of JHP940 in inflammation and subsequent pathogenesis caused by H. pylori. We propose to rename the jhp940 gene as ctkA (cell translocating kinase A).

Background: Up-regulated in various cancers, API5 prevents apoptosis under growth factor deprivation. Results: We have determined the crystal structure of API5 with the HEAT and ARM repeat and show that Lys-251 acetylation is important for its function. Conclusion: API5 likely serves as a scaffold for multiprotein complex with its cellular function regulated by lysine acetylation. Significance: Structural basis of API5 function is important in targeting anti-apoptosis.

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