Diseases associated with expression

Ei addition, clinical observations in EFN-a-treated hqiatitis C or melanoma patients have suggested a promoting effect of type I EFN in autoreactive skin disorders such as Lichen planus. This inflammatory skin disease was, however, not restricted to EFN-a treated patients but was found to be associated with expression by so far unknown mechanisms of the EFN-induced MxA... 

The adherence mechanisms involved in Salmonella infection have been studied in great deal. Disease associated with S. enterica serovars is initiated by attachment to and invasion of hosf cells, followed by subse-quenf inflammation of the lamina propria and lymph nodes (Darwin and Miller, 1999). Several genetically defined fimbrial or piliar adhesins con-tribufe fo fhe initial attachment and the overall infection process of Salmonella. Some of fhese include t)q)e 1 fimbriae (Fim), plasmid-encoded (PE) fimbriae, long polar (LP) fimbriae, and thin aggregative fimbriae (curli). However, many ofher putative fimbrial operons have been identified within various S. enterica serovar genomes, but the expression of fhese proteins is currently undefined. 

Many of the safety issues concerning naked pDNA are similar to those of conventional pharmaceutical agents, such as the inherent toxicity of the pDNA itself. However, the use of pDNA for the delivery of therapeutic proteins poses novel theoretical safety concerns. These concerns involve any toxicity associated with expression of the encoded protein, the potential for unexpected and untoward consequences as a result of the persistent expression of a therapeutic protein which could lead to autoimmune disease, the biodistribution of the pDNA, and the potential for a transformation event resulting from the integration of the pDNA into chromosomal DNA. The safety of naked pDNA has now been well documented in pre-clinical studies in animals, and more recently, in clinical trials in humans. 

EMBL Nucleotide Sequence Database. SWISS-PROT consists of core sequence data with minimal redundancy, citation and extensive annotations including protein function, post-translational modifications, domain sites, protein structural information, diseases associated with protein deficiencies and variants. SWISS-PROT and TrEMBL are available at EBI site, http //www.ebi.ac.uk/swissprot/, and ExPASy site, http //www.expasy.ch/sprot/. From the SWISS-PROT and TrEMBL page of ExPASy site, click Full text search (under Access to SWISS-PROT and TrEMBL) to open the search page (Figure 11.3). Enter the keyword string (use Boolean expression if required), check SWISS-PROT box, and click the Submit button. Select the desired entry from the returned list to view the annotated sequence data in Swiss-Prot format. An output in the fasta format can be requested. Links to BLAST, feature table, some ExPASy proteomic tools (e.g., Compute pI/Mw, ProtParam, ProfileScan, ProtScale, PeptideMass, ScanProsite), and structure (SWISS-MODEL) are provided on the page. 

Abstract The existence of neuronal nicotinic acetylcholine receptor (nAChRs) expression in the brain was discovered 30 years ago. Although the relevance of neuronal nAChRs at the time of their discovery was debated, it is now clear that nAChRs are expressed throughout the brain where they mainly serve a modulatory role. Neuronal nAChRs increasingly have become of interest due to the many observations that various nAChR subtypes exhibit abnormal expression or function in a wide assortment of neurological diseases. In this review, the putative role of nAChRs in brain disease is discussed in several broad categories (1) diseases associated with a loss of nAChRs, (2) diseases associated with innate differences in the expression of nAChRs, (3) diseases associated with genetic variability in genes that code for nAChR subunit proteins, and (4) diseases in which nAChRs are implicated based on the observation that nicotine has a therapeutic effect. 

Diseases Associated with Innate Differences in the Expression of nAChRs. 763... 

---