Pressor responses to amastatin, bestatin and Plummer's inhibitors are suppressed by pretreatment with the angiotensin receptor antagonist sarthran. 1988

C M Batt, and E W Klein, and J W Harding, and J W Wright
Department of Psychology, Washington State University, Pullman 99164-4830.

The aminopeptidase inhibitors, amastatin (AM) and bestatin (BE), and carboxypeptidase inhibitor Plummer's (PL) were applied intracerebroventricularly (ICV) in rats following pretreatment with the angiotensin receptor antagonist sarthran (Sar1,Thr8-AII) or artificial cerebrospinal fluid. Angiotensin II (AII) was also included as a comparison vasoactive peptide. Pressor responses were recorded at 30 min intervals for 90 min to ascertain the duration of the antagonistic effect of sarthran on subsequent injections of AM, BE, PL and AII. Sarthran was effective in suppressing pressor activity to AII- and PL-induced pressor activity until 60 min following pretreatment, and AM- and BE-induced pressor responses until 90 min following pretreatment. These data suggest that AM, BE and PL are having their pressor effects via the central angiotensinergic system and that the patterns of AM, BE, PL and AII recovery from the influence of a specific angiotensin receptor antagonist are similar. The results are consistent with the concept that these inhibitors may increase endogenously synthesized angiotensins which are associated with pressor responses.

UI MeSH Term Description Entries
D007276 Injections, Intraventricular Injections into the cerebral ventricles. Intraventricular Injections,Injection, Intraventricular,Intraventricular Injection
D007930 Leucine An essential branched-chain amino acid important for hemoglobin formation. L-Leucine,Leucine, L-Isomer,L-Isomer Leucine,Leucine, L Isomer
D008297 Male Males
D009842 Oligopeptides Peptides composed of between two and twelve amino acids. Oligopeptide
D010455 Peptides Members of the class of compounds composed of AMINO ACIDS joined together by peptide bonds between adjacent amino acids into linear, branched or cyclical structures. OLIGOPEPTIDES are composed of approximately 2-12 amino acids. Polypeptides are composed of approximately 13 or more amino acids. PROTEINS are considered to be larger versions of peptides that can form into complex structures such as ENZYMES and RECEPTORS. Peptide,Polypeptide,Polypeptides
D011919 Rats, Inbred Strains Genetically identical individuals developed from brother and sister matings which have been carried out for twenty or more generations or by parent x offspring matings carried out with certain restrictions. This also includes animals with a long history of closed colony breeding. August Rats,Inbred Rat Strains,Inbred Strain of Rat,Inbred Strain of Rats,Inbred Strains of Rats,Rat, Inbred Strain,August Rat,Inbred Rat Strain,Inbred Strain Rat,Inbred Strain Rats,Inbred Strains Rat,Inbred Strains Rats,Rat Inbred Strain,Rat Inbred Strains,Rat Strain, Inbred,Rat Strains, Inbred,Rat, August,Rat, Inbred Strains,Rats Inbred Strain,Rats Inbred Strains,Rats, August,Rats, Inbred Strain,Strain Rat, Inbred,Strain Rats, Inbred,Strain, Inbred Rat,Strains, Inbred Rat
D011945 Receptors, Angiotensin Cell surface proteins that bind ANGIOTENSINS and trigger intracellular changes influencing the behavior of cells. Angiotensin Receptor,Angiotensin Receptors,Angiotensin II Receptor,Angiotensin III Receptor,Receptor, Angiotensin II,Receptor, Angiotensin III,Receptor, Angiotensin
D001794 Blood Pressure PRESSURE of the BLOOD on the ARTERIES and other BLOOD VESSELS. Systolic Pressure,Diastolic Pressure,Pulse Pressure,Pressure, Blood,Pressure, Diastolic,Pressure, Pulse,Pressure, Systolic,Pressures, Systolic
D001921 Brain The part of CENTRAL NERVOUS SYSTEM that is contained within the skull (CRANIUM). Arising from the NEURAL TUBE, the embryonic brain is comprised of three major parts including PROSENCEPHALON (the forebrain); MESENCEPHALON (the midbrain); and RHOMBENCEPHALON (the hindbrain). The developed brain consists of CEREBRUM; CEREBELLUM; and other structures in the BRAIN STEM. Encephalon
D002268 Carboxypeptidases Enzymes that act at a free C-terminus of a polypeptide to liberate a single amino acid residue. Carboxypeptidase

Related Publications

C M Batt, and E W Klein, and J W Harding, and J W Wright
October 1987, Brain research,
C M Batt, and E W Klein, and J W Harding, and J W Wright
September 1987, The Journal of pharmacology and experimental therapeutics,
C M Batt, and E W Klein, and J W Harding, and J W Wright
October 1985, The Journal of biological chemistry,
C M Batt, and E W Klein, and J W Harding, and J W Wright
March 2010, Journal of hypertension,
C M Batt, and E W Klein, and J W Harding, and J W Wright
July 1987, Brain research bulletin,
C M Batt, and E W Klein, and J W Harding, and J W Wright
May 1992, Canadian journal of physiology and pharmacology,
C M Batt, and E W Klein, and J W Harding, and J W Wright
April 1970, Proceedings of the Society for Experimental Biology and Medicine. Society for Experimental Biology and Medicine (New York, N.Y.),
C M Batt, and E W Klein, and J W Harding, and J W Wright
July 1988, Brain research,
C M Batt, and E W Klein, and J W Harding, and J W Wright
February 1994, The American journal of physiology,
Copied contents to your clipboard!