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Biomedical subjects

C Haas

Publications and source records attributed to C Haas.

At least 127 records · Page 7Linked to original sources
PubMed1989

[Bronchial manifestation of drug-induced complications].

Bronchial side effects of drugs are varied and numerous. The most frequent are the hypersensitivity type 1 and 3 reactions of asthma. Asthma is primarily caused by anti-infectious agents but also by protein drugs (and many others). At the present time, attention is being focused on excipients and solvents: cremophore, anti-oxidative sulfites (E 220 to E 227), found in over 700 drugs and responsible for severe side effects. Other bronchospasms are due to direct or indirect potentiation of parasympathetic bronchomotor tonus, chiefly with alpha-agonists, and perhaps with beta-agonists but this remains to be proven. Asthmatic reactions caused by interference in mediator synthesis are another current topic of study; some are well known, such as histamine release and interference in arachidonic acid metabolism (non-steroidal antiinflammatory drugs). Other side effects are the result of local irritation, obstruction or bronchial stenosis. A drug-induced cough could be a consequence of local irritation or of the action of converting enzyme inhibitors on bradykinin catabolism.

Adrenergic alpha-Antagonists↗
PubMed1989

[Drug-induced pleural pathology (excluding antineoplastic chemotherapy)].

Drug-induced pleural side effects are rare and not usually identified. They may be a fibrous thickening of the pleura or an effusion, generally associated with an interstitial pneumopathy. Sometimes the pleural fluid is clear, sometimes hemorrhagic, and of varied cytological composition. The effusion can be uni- or bilateral. In the majority of cases, the pleural involvement stops when the causative agent is withdrawn. The pathology is usually attributed to a hypersensitivity mechanism when the following drugs have been given: nitrofurantoin, salazopyrine, erythromycin, ampicillin, gold salts, phenytoin, methysergide, ergotamine and bromocriptine. Some pleural lesions resemble lupus (induced by beta-blockers, hydralazine or procainamide). Amiodarone can cause fibroses or effusions via a toxic or hypersensitivity mechanism. In some instances, the mechanism remains unknown (1 case with imipramine, 1 case of fibrosis with perhexiline, 1 case of effusion with ibuprofen, 4 cases of effusion induced by dandrolene).

Drug-Related Side Effects and Adverse Reactions↗
PubMed1988

Treatment of metastatic breast cancer with AZQ: a phase II trial.

Seventeen patients with metastatic breast cancer who had failed prior chemotherapy were treated with intravenous AZQ at a dose of 15-20 mg/m2 weekly for four consecutive weeks followed by a two-week rest period. No responses were observed. Myelosuppression was the dose-limiting toxicity. One patient experienced massive liver infarction possibly related to AZQ. Our data suggest that this agent at the schedule and dosage used is of no benefit in pretreated breast cancer patients.

Antineoplastic Agents↗
PubMed1988

[Not Available].

Explore the source record for details and available documents.

Academies and Institutes↗
PubMed1987

The influence of anions and inhibitors on the catalytic metal ion in Co(II)-substituted horse liver alcohol dehydrogenase.

1H-NMR and electronic spectroscopic data are reported for the interaction of the effector molecule imidazole and the inhibitor molecule pyrazole with horse liver alcohol dehydrogenase whose catalytic zinc ions were replaced by Co(II). In addition 13C-NMR and optical data are given for the binding of acetate to this enzyme species. For the binary complex with imidazole an assignment of the protons of the metal-coordinated imidazole has been made and it was found that the rate of exchange of the effector molecule is slow on the NMR time scale. In the presence of NADH which is bound to the open conformation of the binary complex, the most pronounced change is a shift of the beta-CH2 protons of the metal-coordinated cysteine residues which is attributed to hydrogen bonding interactions between the carboxamide group of the nicotinamide moiety with cysteine 46. The 1H-NMR spectra of the binary complex of Co(II)-HLADH with pyrazole show resonances assigned to the protons in the 3- and 4-positions of the bound inhibitor, the NH proton resonance is not detectable. In the ternary complex with pyrazole and NAD+ only the resonances of the beta-CH2 protons (beyond 150 ppm) are changed whereas the protons of histidine 67 and the bound inhibitor are unchanged. The data demonstrate that the coordination environment of the catalytic metal ion is changed very little when the protein changes from the open to the closed conformation.(ABSTRACT TRUNCATED AT 250 WORDS)

Acetates↗
PubMed1986

The effect of citrate/cis-aconitate on oxidative metabolism during transformation of Trypanosoma brucei.

Monomorphic bloodstream forms of Trypanosoma brucei, grown in the mammal, are deficient in aconitase and 2-oxoglutarate dehydrogenase and they do not respire in the presence of the substrates citrate, cis-aconitate, succinate, proline or 2-oxoglutarate. When grown in vitro low levels of aconitase, succinate oxidase and proline oxidase are detected. Addition of citrate/cis-aconitate at 37 degrees C to bloodstream forms leads to the formation of aconitase and proline oxidase. Most cells undergo an 'abortive' transformation to non-dividing procyclic-like cells while some cells adapt to the presence of the citric acid cycle intermediates and continue to multiply as bloodstream forms. At 27 degrees C and in the presence of citrate/cis-aconitate bloodstream forms transform synchronously to dividing procyclic cells. Within 72 h the rate of respiration with proline, succinate and 2-oxoglutarate becomes similar to that in established procyclic cells while the rate of glucose oxidation decreases. The possible role of citric acid cycle intermediates in determining whether a trypanosome will retain the properties of a bloodstream trypomastigote or differentiate to a procyclic trypomastigote is discussed.

Aconitic Acid↗