Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0403608 (ureter)
 9,655 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The Electromechanical Impactor was conceived as a safe and effective device for intracorporeal stone fragmentation. It is a 3 French EHL electrode enclosed within a stainless steel sheath. The interior is irrigated with saline. Discharge of the system causes an EHL spark which vaporizes saline and produces a cavitation bubble and subsequent shock wave. The shock wave propels a conical titanium tip forward for a distance of 2.7 mm with an impact pressure of 900 bar. Bench and animal testing has proven its effectiveness for stone fragmentation and safety for use within the ureter. The mean lifetime of each probe is approximately 700 pulses. It is used under direct vision through the straight operating port of a rigid or semi-rigid 9.5 French ureteroscope. Clinical studies at the Massachusetts General Hospital (reported herein) and the Mayo Clinic demonstrate approximately 90% efficacy. It is especially effective on cystine, calcium oxalate dihydrate, struvite and mixed calcium oxalate monohydrate calculi. Shiny-smooth black calcium oxalate monohydrate calculi will fragment but are more resistant. There has been no evidence of ureteral wall injury. The EMI is currently 5 French and is used both safely and effectively under direct vision of fragment ureteral calculi. Larger sizes are designed for percutaneous use and for bladder stone fragmentation.
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PMID:The electromechanical impactor: a new device for intracorporeal stone fragmentation. 834 87

Kidney development has often served as a model for epithelial-mesenchymal cell interaction where the branching epithelium of the ureteric bud induces the metanephrogenic mesenchyme to form epithelial nephrons. In a screen for genes differentially expressed during kidney development, we have identified a novel gene that is dynamically expressed in the branching ureter and the developing nephrons. It was designated Emu1 since it shares an N-terminal cysteine-rich domain with Emilin1/2 and Multimerin. This highly conserved EMI domain is also found in another novel protein (Emu2) of similar protein structure: an N-terminal signal peptide followed by the EMI domain, an interrupted collagen stretch, and a conserved C-terminal domain of unknown function. We identified two further secreted EMI domain proteins, prompting us to compare their gene and protein structures, the EMI domain phylogeny, as well as the embryonic expression pattern of known (Emilin1/2, Multimerin) and novel (Emu1/2, Emilin3, Multimerin2) Emu gene family members. Emu1 and Emu2 not only show a similar structural organization, but furthermore a striking complementary expression in organs developing through epithelial-mesenchymal interactions. In these tissues, Emu1 is restricted to epithelial and Emu2 to mesenchymal cells. Preliminary biochemical analysis of Emu1/2 confirmed that they are secreted glycoproteins which are attached to the extracellular matrix and capable of forming homo- and heteromers via disulfide bonding. The widespread, but individually distinct expression patterns of all Emu gene family members suggest multiple functions during mouse embryogenesis. Their multidomain protein structure may indicate that Emu proteins interact with several different extracellular matrix components and serve to connect and integrate the function of multiple partner molecules.
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PMID:Developmental expression and biochemical characterization of Emu family members. 1222 Oct 2