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S D DEODHAR

Publications and source records attributed to S D DEODHAR.

15 recordsLinked to original sources

VARICOSE VEINS.

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Humans↗

STUDIES ON THE MECHANISM OF EXPERIMENTAL PROTEINURIA INDUCED BY RENIN.

Renin-induced proteinuria in the rat was investigated, with special emphasis on the relationship between the enzymatic activity and the proteinuric effect of renin. The dependence of the proteinuric effect on the enzymatic activity was shown by using (a) renin preparations of widely varying purity and (b) chemically modified "active" and "inactive" renin derivatives. Angiotensin II, the pressor product of the enzymatic action of renin, also produced significant proteinuria. Adrenalectomy abolished the proteinuria induced by renin. Proteinuria, however, occurred as a result of pretreatment with DOCA, or aldosterone, or without treatment, 7 to 8 weeks after adrenalectomy. Electron microscopic studies of the kidney at the time of maximal proteinuria showed focal flattening and fusion of epithelial foot processes, as well as swelling and vesicle formation in endothelial and epithelial cells of the glomeruli. Studies with intravenously injected saccharated iron oxide showed increased permeability of the glomerular capillary basement membrane to these particles. These changes were transient and were not seen 24 hours after renin injection. Adrenalectomy prevented these changes. It is concluded that renin, acting through angiotensin, causes glomerular capillary damage with increased permeability of these structures to protein and resultant proteinuria. The adrenal glands participate in a permissive role in this phenomenon.

Adrenalectomy↗

PRODUCTION OF ANTIRENIN TO HOMOLOGOUS RENIN AND ITS EFFECT OF EXPERIMENTAL RENAL HYPERTENSION.

1. Procedures are described for the extraction and partial purification of dog renin, on a large scale, as well as for the acetylation of rat, rabbit, and dog renin. 2. Untreated homologous renin was not antigenic in rat, rabbit, or dog, but the acetylation of homologous renin made it antigenic. 3. Immunization of rats, rabbits, and dogs, with acetylated rat, rabbit, and dog renin, respectively, resulted in each case in the development of anti-renin to the homologous, untreated, as well as to the acetylated renin. 4. The progressive development of antirenin as a result of repeated, subcutaneous injections of acetylated dog renin, in a dog with experimental renal hypertension for more than 6 years, was accompanied by a correspondingly progressive fall of the mean arterial blood pressure to the prehypertensive level. This points up the important part played by the renin-angiotensin mechanism in the maintenance of the hypertension, even in the chronic phase of experimental renal hypertension.

Angiotensins↗

Immunologic production of antiangiotensin. I. Preparation of angiotensin-protein complex antigen.

Angiotensin II was coupled with bovine gamma-globulin (BGG) through the following series of reactions. See PDF for Structure By determinations of the aromatic amine and tyrosine contents of p-aminobenzoylangiotensin II, the number of p-aminobenzoyl residues introduced per molecule of angiotensin II was calculated. Absorption spectra (between 250 and 500 mmicro) of BGG complexes of p-aminobenzoylangiotensin II and six different para substituted aromatic amines were compared. Specific activities (dog units/millimicromole) of the different intermediate products were determined. Presence of a terminal, free amino group does not appear to be an absolute requirement for the biological activity of angiotensin II, since substitution of a p-aminobenzoyl radical in this group yields a product with 40 to 50 per cent of the activity of the parent compound. Angiotensin I, on the other hand, is completely inactivated under identical circumstances. Possible implication of this finding has been discussed.

Amines↗

Immunologic production of antiangiotensin. II. Production and detection of antiangiotensin.

The parenteral administration of benzoylangiotensin II-azo-BGG to rabbits produced an antiserum with antiangiotensin activity. Antiangiotensin inhibited the biological action of p-aminobenzoylangiotensin II, valine(5)-angiotensin II (free acid form), isoleucine(5)-angiotensin II and valine(5)-angiotensin II (amide form), but it was totally inert towards angiotensin 1. Antiangiotensin activity was distinguished from that of serum angiotensinase by the following observations: (a) an angiotensinase-free gamma-globulin fraction contained antiangiotensin, (b) angiotensinase inactivated angiotensin II (both the amide and free acid forms) and angiotensin I in contrast to the remarkable specificity for angiotensin II exhibited by antiangiotensin. Serological demonstration of antiangiotensin included: (a) a comparison of its precipitin reaction with the angiotensin BGG complex with the reaction with BGG alone, (b) the partial inhibition of the precipitin reaction with the angiotensin BGG complex by angiotensin II, (c) a precipitin reaction with a different angiotensin II protein complex (cat serum). Angiotensin II administered parenterally as the free polypeptide was not antigenic.

Angiotensin Amide↗