Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0042961 (volvulus)
 4,305 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The Onchocerca volvulus superoxide dismutase was expressed in Escherichia coli, using a protocol designed to produce the native enzyme rather than a fusion protein. The recombinant O. volvulus superoxide dismutase (rOVSOD) was found in the cytosol of the disrupted bacteria and represented > 10% of the total bacterial protein. The enzyme was purified to homogeneity using DEAE-Sepharose chromatography, followed by phenyl-Sepharose chromatography. The rOVSOD was enzymatically active which was demonstrated by its reactivity with O2.- produced either by the xanthine-xanthine oxidase system or by stimulated eosinophils. The specific activity was determined to be 4668 U mg-1. This activity could be blocked by rabbit antiserum raised against the rOVSOD. The maximal activity was obtained upon supplementation of the bacterial growth media and enzyme buffer with copper and zinc ions. Activity characteristics in the presence of inhibitors was also characteristic of a Cu/Zn superoxide dismutase. The rOVSOD has an apparent subunit molecular mass of 16,000 in SDS-PAGE. The active enzyme behaves as a dimer of 32 kDa as determined by gel filtration.
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PMID:Characterization of enzymatically active Onchocerca volvulus Cu/Zn superoxide dismutase expressed in Escherichia coli. 783 82

A case of large bowel perforation at sigmoides level, secondary to application of a "medicated" intrauterine contraceptive device (IUD), Copper-7, is presented. This variety of IUD translocated to peritoneal cavity may provoke peritoneal or omental adhesions, volvulus, uterocutaneous fistula and bowel perforation, which involves a significant morbidity. The diagnosis is often delayed and difficult to establish, but, once knowing the exact location of ectopic IUD, it is justified the immediate removal from the peritoneal cavity by either laparoscopy or laparotomy with the utilization of prophylactic antimicrobials for colon preparation before elective surgery.
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PMID:[Perforation of the large intestine caused by a type 7 medicated copper IUD]. 835 6

This is a report of a 54-year-old schizophrenic patient with a 15-year history of ingesting metal objects (pica). He presented with severe anemia (hemoglobin of 3 g/dl and hematocrit of 8.3%) and leukopenia (white blood count of 1,300/mm3). Work-up revealed copper deficiency (copper level of <0.05 microg/ml) and elevated zinc levels (280 microg/ml). The zinc toxicity was produced by the zinc content in the coins ingested by the patient over a period of many years. He was initially treated with -acetylcysteine and sodium bicarbonate followed by intravenous copper sulfate. He was also placed on Adolph's meat tenderizer and pancreatin thrice a day orally to loosen the massive amount of metallic objects including coins in his bowel and allow them to pass out in his feces. He was also continued on oral copper sulfate. His copper levels began to rise and reached a maximum of 0.72 microg/ml, and his zinc level fell to 153 microg/ml. However, as he refused surgery to remove the metal objects from his bowel and continued to ingest more coins, there was continued absorption of zinc, which later overcame the efforts to reduce the zinc level and increase copper levels in his blood. He finally succumbed to sepsis and multiorgan failure. Autopsy revealed a coin mass in the stomach weighing 1,870 grams in addition to a sigmoid volvulus caused by another coin bezoar in the colon.
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PMID:Case report of sideroblastic anemia caused by ingestion of coins. 1142 Dec 92

Copper/zinc (Cu/Zn) superoxide dismutase (SOD) activity was identified for the first time in both crude somatic extracts (CE) and excretory/secretory (E/S) products of Trichinella pseudospiralis. It was the dominant SOD in infective-stage larvae. Native polyacrylamide gel electrophoresis of CE and E/S products yielded a prominent band, which was cyanide-sensitive and was partly inhibited by hydrogen peroxide in SOD assay. Cytosolic Cu/Zn SOD was cloned. The 471-bp full-length cDNA sequence contained an open reading frame of 157 amino acids. The gene contained three introns. Quantitative reverse transcription-polymerase chain reaction indicated that the expression of cytosolic Cu/Zn SOD was substantially higher in infective-stage larvae than in adult worms. Cluster analysis showed that the sequence of the Cu/Zn SOD of T. pseudospiralis, an adenophorean nematode, is related to those of Brugia pahangi, Acanthocheilonema viteae, Onchocerca volvulus, and Haemonchus contortus (all belonging to the sercenentean group).
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PMID:Cloning and characterization of the Cu/Zn superoxide dismutase of Trichinella pseudospiralis. 1634 81

The functions of the members of the S100 family of EF-hand proteins are modulated by calcium and, in a number of cases, by zinc or copper. One such protein is S100A12, which is implicated in inflammation and host-parasite responses. Previously, we reported the structures of human S100A12 in both low (dimeric) and high (hexameric) calcium forms and, in addition, that of a complex with copper and calcium. Here we report the crystal structures of the metal-free apo form of human S100A12 at 1.77 A resolution and of the zinc complex in two crystal forms (P2(1)2(1)2(1) and F222) to 1.88 A and 1.73 A resolution, respectively. These are the first structures of a zinc-only complex of an S100 protein to be determined. The zinc complex structure shows significant differences from those of both calcium-loaded and apo-S100A12 structures, and comparisons suggest an explanation for the zinc-induced 1500-fold increase in calcium affinity. In addition, the new structures provide insight into the role of zinc-calcium interplay in the transition of S100A12 from a dimer through a tetramer to a hexamer. The role of both zinc and calcium in target binding by S100A12 during host-parasite responses is confirmed by experiments with paramyosin from the tropical parasites Onchocerca volvulus and Brugia malayi.
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PMID:The crystal structures of human S100A12 in apo form and in complex with zinc: new insights into S100A12 oligomerisation. 1950 94