Search PubMed⌕ Search

Biomedical subjects

P Bataille

Publications and source records attributed to P Bataille.

41 records · Page 3Linked to original sources

[Intravenous pyelography with visualization of renal arteries and pyelogram wash-out, as the method of choice for the diagnosis of renovascular hypertension (author's transl)].

The authors review the various techniques of intravenous arteriography before an excretory urogram and discuss their role in the etiological diagnosis of hypertension. Detection of renovascular disease classically implied Seldinger arteriography, with its limited indications, because of side effects and cost. This classical approach should now be systematically replaced by the visualization of renal arteries during the intravenous pyelography procedure which appears to be a method more effective, as well as less expensive and hazardous. The pyelogram wash-out should still be performed when the visualization of the renal arteries is poor because of its value in the screening for renovascular hypertension. Furthermore, when a renal artery stenosis is clearly defined, the wash-out of the pyelogram should also be performed because of its prognostic value. As the classical approach for the etiological diagnosis of hypertension, this technique has limited indications. It is indicated in severe hypertension in the young, when medical treatment does not control blood pressure satisfactorily or when renal failure progresses rapidly. Furthermore, this technique allows a non traumatic follow up of operated or dilated stenoses.

Cost-Benefit Analysis↗

Interactions of adrenocorticotropic hormone with its adrenal receptors. Degradation of ACTH-1-24 and ACTH-11-24.

Crude membranes (20,000 times g pellet) prepared from human, rat, and ovine adrenals bind 125-I-corticotropin-(1-24)-tetracosapeptide (125-I-ACTH-1-24) and degrade unbound hormone. The degradation is dependent on temperature and the concentration of membrane proteins. The degradation of 125-I-[9-tryptophan(o-nitrophenylsulfenyl)]-corticotropin-(1-24)-tetracosapeptide (125-I-NPS-ACTH-1-24) is similar to 125-I-ACTH-1-24, but that of 125-I-corticotropin-(11-24)-tetradecapeptide (125-I-ACTH-1-24 is inhibited by ACTH-1-24 and corticotropin-(1-10)-decapeptide (ACTH-1-10), but ACTH-11-24 at the same molar concentration has no effect. On the other hand, the degradation of 125-I-ACTH-11-24 is protected by ACTH-11-24 and ACTH-1-24, but not by ACTH-1-10. This suggests two systems of degradation, one will have the NH-2-terminal sequence of ACTH-1-24 as substrate, and the other the 11-24 COOH-terminal sequence. The main label product from the degradation of the 125-I-ACTH-1-24 and 125-I-ACTH-11-24 behaves as [125-I]monoiodotyrosine on Sephadex G-50 and paper chromatography. The independence of ACTH binding to its receptor and degradation is demonstrated by the following facts. (a) Calcium and pancreatic trypsin inhibitor completely inhibit the binding at concentrations when the degradation is not altered; (b) the sequences of peptides of ACTH which inhibit the binding and degradation of 125-I-ACTH-1-24 are different.

Adenylyl Cyclases↗