BIOMAT Database Logo BIOMAT Database Logo

Handling of angiotensin II and oxytocin by renal tubular segments perfused in vitro. 1977

D R Peterson, and S Oparil, and G Flouret, and F A Carone

In order to study renal tubular handling of two small peptide hormones, [14c]angiotensin II ([14C]AII) and [3H]oxytocin ([3H]OT) were microperfused through rabbit kidney tubule segments in vitro. The reabsorption and tubular sequestration of radioactive label were determined, and the collection fluid was electrophoretically analyzed. The data suggest that [14C]AII is extensively hydrolyzed in the pars recta of the nephron and is rapidly reabsorbed across the tubular epithelium. Under similar experimental conditions, hydrolysis of [3H]OT was not observed in either the proximal straight or cortical collecting tubule segment, and the rate of reabsorption was low. Thus, tubular handling of OT appears to differ from that of AII, probably because of differences in molecular structure.

UI MeSH Term Description Entries
D007444 Inulin A starch found in the tubers and roots of many plants. Since it is hydrolyzable to FRUCTOSE, it is classified as a fructosan. It has been used in physiologic investigation for determination of the rate of glomerular function.
D007684 Kidney Tubules Long convoluted tubules in the nephrons. They collect filtrate from blood passing through the KIDNEY GLOMERULUS and process this filtrate into URINE. Each renal tubule consists of a BOWMAN CAPSULE; PROXIMAL KIDNEY TUBULE; LOOP OF HENLE; DISTAL KIDNEY TUBULE; and KIDNEY COLLECTING DUCT leading to the central cavity of the kidney (KIDNEY PELVIS) that connects to the URETER. Kidney Tubule,Tubule, Kidney,Tubules, Kidney
D010121 Oxytocin A nonapeptide hormone released from the neurohypophysis (PITUITARY GLAND, POSTERIOR). It differs from VASOPRESSIN by two amino acids at residues 3 and 8. Oxytocin acts on SMOOTH MUSCLE CELLS, such as causing UTERINE CONTRACTIONS and MILK EJECTION. Ocytocin,Pitocin,Syntocinon
D010446 Peptide Fragments Partial proteins formed by partial hydrolysis of complete proteins or generated through PROTEIN ENGINEERING techniques. Peptide Fragment,Fragment, Peptide,Fragments, Peptide
D011817 Rabbits A burrowing plant-eating mammal with hind limbs that are longer than its fore limbs. It belongs to the family Leporidae of the order Lagomorpha, and in contrast to hares, possesses 22 instead of 24 pairs of chromosomes. Belgian Hare,New Zealand Rabbit,New Zealand Rabbits,New Zealand White Rabbit,Rabbit,Rabbit, Domestic,Chinchilla Rabbits,NZW Rabbits,New Zealand White Rabbits,Oryctolagus cuniculus,Chinchilla Rabbit,Domestic Rabbit,Domestic Rabbits,Hare, Belgian,NZW Rabbit,Rabbit, Chinchilla,Rabbit, NZW,Rabbit, New Zealand,Rabbits, Chinchilla,Rabbits, Domestic,Rabbits, NZW,Rabbits, New Zealand,Zealand Rabbit, New,Zealand Rabbits, New,cuniculus, Oryctolagus
D000804 Angiotensin II An octapeptide that is a potent but labile vasoconstrictor. It is produced from angiotensin I after the removal of two amino acids at the C-terminal by ANGIOTENSIN CONVERTING ENZYME. The amino acid in position 5 varies in different species. To block VASOCONSTRICTION and HYPERTENSION effect of angiotensin II, patients are often treated with ACE INHIBITORS or with ANGIOTENSIN II TYPE 1 RECEPTOR BLOCKERS. Angiotensin II, Ile(5)-,Angiotensin II, Val(5)-,5-L-Isoleucine Angiotensin II,ANG-(1-8)Octapeptide,Angiotensin II, Isoleucine(5)-,Angiotensin II, Valine(5)-,Angiotensin-(1-8) Octapeptide,Isoleucine(5)-Angiotensin,Isoleucyl(5)-Angiotensin II,Valyl(5)-Angiotensin II,5 L Isoleucine Angiotensin II,Angiotensin II, 5-L-Isoleucine
D000818 Animals Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA. Animal,Metazoa,Animalia
D001692 Biological Transport The movement of materials (including biochemical substances and drugs) through a biological system at the cellular level. The transport can be across cell membranes and epithelial layers. It also can occur within intracellular compartments and extracellular compartments. Transport, Biological,Biologic Transport,Transport, Biologic

Related Publications

D R Peterson, and S Oparil, and G Flouret, and F A Carone
Handling of luteinizing hormone-releasing hormone by renal proximal tubular segments in vitro.
August 1981, The American journal of physiology,
D R Peterson, and S Oparil, and G Flouret, and F A Carone
Renal tubular hypertrophy induced by angiotensin II.
September 1997, Seminars in nephrology,
D R Peterson, and S Oparil, and G Flouret, and F A Carone
Measurement of Renal Tubular Angiotensin II.
January 2001, Methods in molecular medicine,
D R Peterson, and S Oparil, and G Flouret, and F A Carone
Angiotensin II and renal tubular ion transport.
August 2005, TheScientificWorldJournal,
D R Peterson, and S Oparil, and G Flouret, and F A Carone
Angiotensin II facilitates autoregulation in the perfused mouse kidney: An optimized in vitro model for assessment of renal vascular and tubular function.
October 2004, Nephrology (Carlton, Vic.),
D R Peterson, and S Oparil, and G Flouret, and F A Carone
Effects of constituent amino acids on tubular handling of microinfused angiotensin II.
April 1978, The American journal of physiology,
D R Peterson, and S Oparil, and G Flouret, and F A Carone
Mechanism of renal handling of angiotensin II in the dog.
November 1973, Circulation research,
D R Peterson, and S Oparil, and G Flouret, and F A Carone
Angiotensin II induces apoptosis in renal proximal tubular cells.
May 2003, American journal of physiology. Renal physiology,
D R Peterson, and S Oparil, and G Flouret, and F A Carone
Renal tubular handling of drugs.
April 1977, The American journal of medicine,
D R Peterson, and S Oparil, and G Flouret, and F A Carone
Increases in renal angiotensin II content and tubular angiotensin II receptors in prehypertensive spontaneously hypertensive rats.
October 1988, Journal of hypertension,
Copied contents to your clipboard!