PubMed Health⌕ Search

Biomedical subjects

U Dreher

Publications and source records attributed to U Dreher.

2 recordsLinked to original sources
PubMed2001

[Ulcerative ileocolitis induced by NSAID therapy].

HISTORY AND PHYSICAL EXAMINATION: A 67-year-old woman was admitted to our hospital for spasmodic abdominal pain, diarrhea, and general weakness. She had lost 5 kg of weight over the past few weeks. The patient had a 20-year history of chronic analgetic abuse, mainly consuming over-the-counter nonsteroidal anti-inflammatory drugs (NSAID). EXAMINATION: Laboratory examination was remarkable for a low serum albumin (2.3 g/dl), an increased erythrocyte sedimentation rate of 70 mm/h, and a profound anemia of 8.5 g/dl. Ultrasound of the abdomen showed thickening of the colonic wall and distended colon loops filled with fluid. On colonoscopy several ulcerations from the sigmoid to the ileum were seen. Histologic examination showed a nonspecific ileocolitis. DIAGNOSIS, THERAPY AND CLINICAL COURSE: After cessation of NSAID intake diarrhea stopped within a few days. Abdominal pain resolved, anemia improved and the patient gained weight. A second colonoscopy revealed healing of the colonic ulcerations. Additional examinations regarding differential diagnoses showed no pathological results. Clinical course and subsequent clinical and endoscopic controls revealing further improvement confirmed the diagnosis of an NSAID-induced ileocolitis. CONCLUSION: This patient is a typical example for NSAID-induced colonic ulcerations. It should be recognized that NSAID induce ulcers not only in the upper gastrointestinal tract. A careful drug history may provide the clue for the cause of lower gastrointestinal tract ulcerations.

Abdominal Pain↗
PubMed1998

Mutagenesis of histidine 26 demonstrates the importance of loop-loop and loop-protein interactions for the function of iso-1-cytochrome c.

In yeast iso-1-cytochrome c, the side chain of histidine 26 (His26) attaches omega loop A to the main body of the protein by forming a hydrogen bond to the backbone atom carbonyl of glutamic acid 44. The His26 side chain also forms a stabilizing intra-loop interaction through a hydrogen bond to the backbone amide of asparagine 31. To investigate the importance of loop-protein attachment and intra-loop interactions to the structure and function of this protein, a series of site-directed and random-directed mutations were produced at His26. Yeast strains expressing these variant proteins were analyzed for their ability to grow on non-fermentable carbon sources and for their intracellular production of cytochrome c. While the data show that mutations at His26 lead to slightly decreased intracellular amounts of cytochrome c, the level of cytochrome c function is decreased more. The data suggest that cytochrome c reductase binding is affected more than cytochrome c oxidase or lactate dehydrogenase binding. We propose that mutations at this residue increase loop mobility, which, in turn, decreases the protein's ability to bind redox partners.

Amino Acid Sequence↗