The "foamy" esophagus: a radiographic sign of Candida esophagitis.

OBJECTIVE: The purpose of this study was to describe the radiographic features of the "foamy" esophagus, a new sign of Candida esophagitis seen on double-contrast esophagography, in six patients. CONCLUSION: The foamy esophagus was characterized by innumerable tiny (1-3 mm), round lucencies (bubbles) that intermingled with the barium suspension along the top of the barium column, producing a layer of foam. Candida esophagitis should be strongly suspected when a foamy esophagus is detected on double-contrast esophagography, particularly in patients with underlying esophageal involvement by scleroderma.

The right inferior supraazygous recess: a cause of upper esophageal pseudomass on double-contrast esophagography.

OBJECTIVE: Our purpose was to characterize the radiographic features of a pseudomass impression on the upper thoracic esophagus, to determine the frequency of such a pseudomass both on double-contrast esophagography and on CT, and to elucidate the anatomic basis for this finding. MATERIALS AND METHODS: Our study group consisted of 135 patients whose double-contrast esophagograms were reviewed retrospectively for the presence or absence of an extrinsic indentation on the right posterolateral wall of the upper thoracic esophagus. In another patient group, 50 CT scans of the chest were also reviewed for the presence or absence of a prominent right inferior supraazygous recess and an associated indentation on the upper thoracic esophagus. RESULTS: Thirteen (9.6%) of the 135 barium studies revealed a smooth, gently sloping indentation on the right posterolateral wall of the upper thoracic esophagus. The indentations ranged from 5 to 10 cm in length and extended inferiorly from the thoracic inlet to or just below the aortic arch. Twenty-four (48%) of the 50 CT scans revealed a prominent right inferior supraazygous recess projecting behind the esophagus. In five cases (10%), this recess also caused a smooth indentation on the upper thoracic esophagus. CONCLUSION: A pseudomass impression was seen on double-contrast radiography as a smooth, gently sloping indentation on the right posterolateral wall of the upper thoracic esophagus in approximately 10% of patients. The indentation probably represents a normal anatomic variant (i.e., an unusually prominent right inferior supraazygous recess) that should not be mistaken for adenopathy or other masses in the mediastinum impinging on the esophagus.

Sequence-specific changes in the metal site of ferric bleomycin induced by the binding of DNA.

The binding of the iron complex of the antineoplastic glycopeptide bleomycin A2 (Fe-BLM) to calf thymus DNA and the self-complementary oligonucleotides d(CGCGCG) and d(ATATAT) has been studied using optical, EPR, and resonance Raman spectroscopies. An increase in the intensity of the bands at 365 and 384 nm is observed in the optical spectrum of Fe(III)-BLM when the drug binds to either oligonucleotide. However, in the presence of phosphate, this increase is observed only with d(CGCGCG) and not with d(ATATAT). In addition, the gmax feature in the EPR spectrum of low spin Fe(III)-BLM is narrowed in a way suggesting a reduction of possible conformers that the drug can achieve when it is bound to d(CGCGCG) or to calf thymus DNA but not when bound to d(ATATAT). When Fe(III)-BLM is bound to d(CGCGCG), changes in the resonance Raman spectrum of the metal drug complex suggest conformational changes in three of the ligands to iron: the beta-hydroxyhistidyl amide, the pyrimidine, and the axial hydroxide. In addition, the Fe-OH band undergoes narrowing, again consistent, with the reduction of conformers of the drug. No such resonance Raman changes are observed upon binding to d(ATATAT). The changes in the pyrimidine modes upon binding d(CGCGCG) to the drug are consistent with a recently proposed model (Wu, W., Vanderwall, D. E., Turner, C. J., Kozarich, J. W., and Stubbe, J. (1996) J. Am. Chem. Soc. 118, 1281-1294) of DNA recognition by activated bleomycin, HOO-Fe(III)-BLM, in which the pyrimidine moiety of the drug is important for the preferential cleavage of 5'-GpPy-3' sequences.

EPR spectroscopic investigation of the lability of oxygen in activated bleomycin: implications for the mechanism of bleomycin-mediated DNA degradation.

Bleomycin (BLM), an antitumor antibiotic, is capable of degrading DNA through the formation of activated BLM, an activated iron-oxygen complex of the drug with a unique EPR spectrum. A recent study [Rabow, L. E., McGall, G. H., Stubbe, J., & Kozarich, J. W. (1990) J. Am. Chem. Soc. 112, 3203-3208] has cast doubt onto the "hydroxyl-radical-rebound" mechanism, commonly accepted for cytochrome P-450 [McMurray, T.J., & Groves, J.T. (1985) in Cytochrome P-450: Structure, Mechanism, and Biochemistry (Ortiz de Montellano, P., Ed.) pp 1-28, Plenum, New York] and proposed for the anaerobic nucleic base release reaction of BLM, by demonstrating that the source of oxygen in the products of this reaction is solvent molecules and not molecular oxygen. A central issue in this debate is whether the oxygen of activated BLM is available for exchange with that of solvent. The lability of oxygen in activated BLM has been investigated through the use of EPR spectroscopy to measure the exchange of 17O (I = 5/2) between activated BLM and solvent. Evidence for the lack of oxygen exchange between activated BLM and solvent is presented, and the implications of this result for the mechanism of BLM-mediated DNA degradation are discussed.