Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0162871 (abdominal aortic aneurysm)
 8,664 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Prior experience with the rare combination of horseshoe kidney and significant atherosclerotic vascular disease suggests difficulty in intraoperative management, often requiring division of the renal isthmus or sacrifice of some renal tissue. Seven patients have been managed successfully over the past ten years at The Ohio State University Hospital. There were six men and one woman, ranging in age from 39 to 66 years. Of the five patients with abdominal aortic aneurysm, four had a pulsatile abdominal mass, three had abdominal pain, and one had back pain. The other two patients had progressively symptomatic aortoiliac disease. All seven patients had hypertension, easily controlled by medication. Critical diagnostic procedures are preoperative intravenous pyelogram (IVP) and abdominal aortic arteriogram. The IVP detected the previously unsuspected diagnosis in 100% of the cases. The arteriogram accurately located the aneurysm in relation to the renal vascular supply, and disclosed aberrant blood supply in three of four patients with aberrant vessels. All seven horseshoe kidneys were fused at the lower pole. The operative approach involves meticulous dissection of the aberrant blood supply to the kidneys, and mobilization of the isthmus for adequate retrorenal aortic exposure. In six of the seven patients, the grafts were placed posterior to the isthmus. There were no deaths, and there were no complications related to the presence of the horseshoe kidney. In three of the seven patients, hypertension improved. Patients with horseshoe kidney and aortic disease may be safely operated upon without damage to the kidney. IVP and selective angiography are essential to provide preoperative information.
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PMID:Abdominal aortic surgery in the presence of a horseshoe kidney. 66 80

pBR322 contains the amp gene encoding beta-lactamase. When Escherichia coli carrying this plasmid is exposed to heat shock, beta-lactamase synthesis is repressed transiently at the translational level. To identify the DNA element responsible for this translational repression, DNA segments containing the translation start region of the amp gene were excised from pAT153 and fused in frame with the lacZ reading frame in the open reading frame vector pORF1. These constructs were introduced into E. coli, and the effect of heat shock of the cells on the synthesis of beta-galactosidase starting from the amp start codon was examined. As is the case for pBR322-encoded synthesis of beta-lactamase, the synthesis of beta-galactosidase encoded by the fused genes also ceased transiently upon heat shock. It is concluded that the heat shock-induced repression of the amp gene occurs at the initiation step of translation. As far as the present study is concerned, the minimum DNA segment responsible for the repression is AT TGA AAA AGG AAG AGT ATG AG, which includes the Shine-Dalgarno sequence (AAGGA) and the initiation codon (ATG).
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PMID:The translation start signal region of TEM beta-lactamase mRNA is responsible for heat shock-induced repression of amp gene expression in Escherichia coli. 250 25

A case with crossed fused ectopy of the right kidney covering an abdominal aortic aneurysm and thus complicating its repair is described as a rarity.
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PMID:Crossed fused ectopy of the right kidney complicating the repair of abdominal aortic aneurysm. 274 41

We report the first case of an infrarenal abdominal aortic aneurysm associated with crossed-fused ectopia of the kidney. This is the second most common fusion defect of the kidney with an incidence in the general population of 1 in 1000. The different types of crossed renal ectopia with and without fusion are described. The renal artery anomalies associated with crossed renal ectopia are emphasized. Abdominal ultrasonography or CT scanning must be used to uncover renal anomalies before surgery so that a selective preoperative aortogram can be obtained to determine the location of the arterial supply to the kidneys.
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PMID:Abdominal aortic and multiple iliac aneurysms associated with crossed-fused ectopia of the kidney: a case report and review. 291 Nov 38

To examine normal and aberrant translation initiation in Saccharomyces cerevisiae mitochondria, we fused the synthetic mitochondrial reporter gene ARG8m to codon 91 of the COX2 coding sequence and inserted the chimeric gene into mitochondrial DNA (mtDNA). Translation of the cox2(1-91)::ARG8m mRNA yielded a fusion protein precursor that was processed to yield wild-type Arg8p. Thus mitochondrial translation could be monitored by the ability of mutant chimeric genes to complement a nuclear arg8 mutation. As expected, translation of the cox2(1-91)::ARG8m mRNA was dependent on the COX2 mRNA-specific activator PET111. We tested the ability of six triplets to function as initiation codons in both the cox2(1-91)::ARG8m reporter mRNA and the otherwise wild-type COX2 mRNA. Substitution of AUC, CCC or AAA for the initiation codon abolished detectable translation of both mRNAs, even when PET111 activity was increased. The failure of these mutant cox2(1-91)::ARG8m genes to yield Arg8p demonstrates that initiation at downstream AUG codons, such as COX2 codon 14, does not occur even when normal initiation is blocked. Three mutant triplets at the site of the initiation codon supported detectable translation, with efficiencies decreasing in the order GUG, AUU, AUA. Increased PET111 activity enhanced initiation at AUU and AUA codons. Comparisons of expression, at the level of accumulated product, of cox2(1-91)::ARG8m and COX2 carrying these mutant initiation codons revealed that very low-efficiency translation can provide enough Cox2p to sustain significant respiratory growth, presumably because Cox2p is efficiently assembled into stable cytochrome oxidase complexes.
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PMID:In vivo analysis of mutated initiation codons in the mitochondrial COX2 gene of Saccharomyces cerevisiae fused to the reporter gene ARG8m reveals lack of downstream reinitiation. 1066 64

Pex6p belongs to the AAA family of ATPases. Its CHO mutant, ZP92, lacks normal peroxisomes but contains peroxisomal membrane remnants, so called peroxisomal ghosts, which are detected with anti-70-kDa peroxisomal membrane protein (PMP70) antibody. No peroxisomal matrix proteins were detected inside the ghosts, but exogenously expressed green fluorescent protein (GFP) fused to peroxisome targeting signal-1 (PTS-1) accumulated in the areas adjacent to the ghosts. Electron microscopic examination revealed that PMP70-positive ghosts in ZP92 were complex membrane structures, rather than peroxisomes with reduced matrix protein import ability. In a typical case, a set of one central spherical body and two layers of double-membraned loops were observed, with endoplasmic reticulum present alongside the outer loop. In the early stage of complementation by PEX6 cDNA, catalase and acyl-CoA oxidase accumulated in the lumen of the double-membraned loops. Biochemical analysis revealed that almost all the peroxisomal ghosts were converted into peroxisomes upon complementation. Our results indicate that 1) Peroxisomal ghosts are complex membrane structures; and 2) The complex membrane structures become import competent and are converted into peroxisomes upon complementation with PEX6.
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PMID:Peroxisomes are formed from complex membrane structures in PEX6-deficient CHO cells upon genetic complementation. 1185 24

Pathogenic Yersinia spp. secrete Yop proteins via the type III pathway. yopQ codons 1 to 15 were identified as a signal necessary and sufficient for the secretion of a fused reporter protein. Frameshift mutations that alter codons 2 to 15 with little alteration of yopQ mRNA sequence do not abolish type III transport, suggesting a model in which yopQ mRNA may provide a signal for secretion (D. M. Anderson and O. Schneewind, Mol. Microbiol. 31:1139-1148, 2001). In a recent study, the yopE signal was truncated to codons 1 to 12. All frameshift mutations introduced within the first 12 codons of yopE abolished secretion. Also, multiple synonymous mutations that changed the mRNA sequence of yopE codons 1 to 12 without altering the amino acid sequence did not affect secretion. These results favor a model whereby an N-terminal signal peptide initiates YopE into the type III pathway (S. A. Lloyd et al., Mol. Microbiol. 39:520-531, 2001). It is reported here that codons 1 to 10 of yopQ act as a minimal secretion signal. Further truncation of yopQ, either at codon 10 or at codon 2, abolished secretion. Replacement of yopQ AUG with either of two other start codons, UUG or GUG, did not affect secretion. However, replacement of AUG with CUG or AAA and initiating translation at the fusion site with npt did not permit Npt secretion, suggesting that the translation of yopQ codons 1 to 15 is a prerequisite for secretion. Frameshift mutations of yopQ codons 1 to 10, 1 to 11, and 1 to 12 abolished secretion signaling, whereas frameshift mutations of yopQ codons 1 to 13, 1 to 14, and 1 to 15 did not. Codon changes at yopQ positions 2 and 10 affected secretion signaling when placed within the first 10 codons but had no effect when positioned in the larger fusion of yopQ codons 1 to 15. An mRNA mutant of yopQ codons 1 to 10, generated by a combination of nine synonymous mutations, was defective in secretion signaling, suggesting that the YopQ secretion signal is not proteinaceous. A model is discussed whereby the initiation of YopQ polypeptide into the type III pathway is controlled by properties of yopQ mRNA.
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PMID:Yersinia enterocolitica type III secretion: mutational analysis of the yopQ secretion signal. 1202 49

This study compared the adaptation of a conventional and an electroformed porcelain-fused-to-metal crown. A master model was selected from an ITI implant with a solid abutment (height: 4 mm). Conventional cast metal frameworks of 0.7 mm thickness were prepared with a high noble metal alloy (Degudent U, Degussa) for porcelain fusing (n = 5). Electroformed frameworks of 0.2 mm thickness were determined using pure gold deposition on the abutment using the Auro-Galva-Crown system (AGC, Wieland) (n = 5). Subsequently, a porcelain (Super Porcelain AAA, Noritake) was fused to each framework. Internal gaps between the framework and its abutment were determined using the thickness of a silicone fit checking material. The gaps were measured both before and after porcelain fusing. The thicknesses of the silicone layer of the electroformed and the conventional porcelain-fused-to-metal crown were 34.6 and 38.5 microns at the margin, 33.2 and 39.6 microns at the internal slope, 22.0 and 33.0 microns at the axial, 58.6 and 65.1 microns at the occlusal, respectively. Three-way analysis of variance revealed that the mean gaps in the electroformed porcelain-fused-to-metal crown were significantly thinner than those in the conventional porcelain-fused-to-metal crown (p < 0.05). The electroformed porcelain-fused-to-metal crown showed better adaptability than the conventional porcelain-fused-to-metal crown regardless of porcelain fusing.
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PMID:[Fit of electroformed porcelain-fused-to-metal crown on implant abutment]. 1457 40

Epstein-Barr virus (EBV) nuclear antigen 3C (EBNA3C) is critical for EBV immortalization of infected B lymphocytes and can coactivate the EBV LMP1 promoter with EBNA2. EBNA3C amino acids 365 to 545 are necessary and sufficient for coactivation and are required for SUMO-1 and SUMO-3 interaction. We found that EBNA3C but not EBNA3CDelta343-545 colocalized with SUMO-1 in nuclear bodies and was modified by SUMO-2, SUMO-3, and SUMO-1. EBNA3C amino acids 545 to 628 and amino acids 30 to 365 were also required for EBNA3C sumolation and nuclear body localization but were dispensable for coactivation, indicating that EBNA3C sumolation is not required for coactivation. Furthermore, EBNA3C amino acids 476 to 992 potently coactivated with EBNA2 but EBNA3C amino acids 516 to 922 lacked activity, indicating that amino acids 476 to 515 are critical for coactivation. EBNA3C amino acids 476 to 515 include DDDVIEV(507-513), which are similar to SUMO-1 EEDVIEV(84-90). EBNA3C m1 and m2 point mutations, DDD(507-509) mutated to AAA and DVIEVID(509-513) mutated to AVIAVIA, respectively, diminished SUMO-1 and SUMO-3 interaction in directed yeast two-hybrid and glutathione S-transferase pulldown assays. Furthermore, EBNA3C m1 and m2 did not coactivate the LMP1 promoter with EBNA2. Overexpression of wild-type SUMO-1, SUMO-3, and the SUMO-conjugating enzyme UBC9 coactivated the LMP1 promoter with EBNA2. Since EBNA2 activation is dependent on p300/CBP, the possible effect of EBNA3C on p300-mediated transcription was assayed. EBNA3C potentiated transcription of p300 fused to a heterologous DNA binding domain, whereas EBNA3C m1 and m2 did not. All of these data are consistent with a model in which EBNA3C upregulates EBNA2-mediated gene activation by binding to a sumolated repressor and inhibiting repressive effects on p300/CBP and other transcription factor(s) at EBNA2-regulated promoters.
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PMID:EBNA3C coactivation with EBNA2 requires a SUMO homology domain. 1467 Nov 18

A class of inherited neurodegenerative diseases including Huntington's disease is caused by polyglutamine (polyQ) expansion in the responsible proteins. Pathology is typically associated with polyQ expansions of greater than 40 residues, and the longer the length of the expansion, the earlier the onset of disease. It has been reported that p97/VCP/Cdc48p, a member of AAA family of proteins, can bind to longer polyQ tracts. In Caenorhabditis elegans, two p97/VCP/Cdc48p homologues, C41C4.8 and C06A1.1, have been identified. Our results indicate that these p97/VCP/Cdc48p homologues have essential but redundant functions in C. elegans. To provide a model system for investigating the molecular basis of pathogenesis, we have expressed polyQ expansions fused to green fluorescent protein in the body wall muscle cells of C. elegans. When the repeats are longer than 40, discrete cytoplasmic aggregates are formed and these appear at an early stage of embryogenesis. The formation of aggregates was partially suppressed by co-expression of either C41C4.8 or C06A1.1. These results suggest that these p97/VCP/Cdc48p homologues, AAA chaperones, may play a protective role in polyQ aggregation.
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PMID:Analysis of the two p97/VCP/Cdc48p proteins of Caenorhabditis elegans and their suppression of polyglutamine-induced protein aggregation. 1503 55


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