SiRNAdb: a database of siRNA sequences
NUCLEIC ACIDS RESEARCH
Authors: Chalk, AM; Warfinge, RE; Georgii-Hemming, P; Sonnhammer, ELL
Abstract
Short interfering RNAs(siRNAs) area popular method for gene-knockdown, acting by degrading the target mRNA. Before performing experiments it is invaluable to locate and evaluate previous knockdown experiments for the gene of interest. The siRNA database provides a gene-centric view of siRNA experimental data, including siRNAs of known efficacy and siRNAs predicted to be of high efficacy by a combination of methods. Linked to these sequences is information such as siRNA thermodynamic properties and the potential for sequence-specific off-target effects. The database enables the user to evaluate an siRNA's potential for inhibition and non-specific effects. The database is available at http:// siRNA.cgb.ki.se.
Large dense-core secretory granule biogenesis is under the control of chromogranin A in neuroendocrine cells
CHROMAFFIN CELL: TRANSMITTER BIOSYNTHESIS, STORAGE, RELEASE, ACTIONS, AND INFORMATICS
Authors: Kim, T; Tao-Cheng, JH; Eiden, LE; Loh, YP
Abstract
The large dense-core secretory granule is an organelle in neuroendocrine/endocrine cells, where prohormones and proneuropeptides are stored, processed, and secreted in a regulated manner. Here we present evidence that chromogranin A (CgA), one of the most abundant acidic glycoproteins ubiquitously present in neuroendocrine/endocrine cells, regulates dense-core secretory granule biogenesis. Specific depletion of CgA expression by antisense RNAs in PC12 cells led to a profound loss of secretory granule formation. An exogenously expressed prohormone, pro-opiomelanocortin, was neither stored nor secreted in a regulated manner in CgA-deficient PC12 cells. Overexpression of bovine CgA into CgA-deficient PC12 cells rescued regulated secretion. Other secretory granule proteins, such as chromogranin B (CgB), carboxypeptidase E, and synaptotagmin, were rapidly degraded, whereas nongranule proteins were not affected in CgA-deficient PC12 cells. Unlike CgA, another granin protein CgB could not substitute for the role of CgA in secretory granule biogenesis. Thus, we conclude that CgA is a master "on/off" switch regulating the formation of the dense-core secretory granule in neuroendocrine cells.