Angiotensinase activity in rat and dog brain

Goldstein, Daniel J.; Díaz, Alcira Ofélia; Finkielman, Samuel; Nahmod, Víctor E.; Fischer-Ferraro, C

doi:10.1111/j.1471-4159.1972.tb01299.x

Cited by 25 publications

(7 citation statements)

References 12 publications

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“…This possibility is supported by the presence of a carboxypeptidase (cathepsin A) in rat brain lysosomes, capable of releasing phenylalanine from angiotensin 11 [30]. Moreover, following the isolation procedure for kidney lysosomal angiotensinase C [31], Goldstein et al [32] isolated from rat brain a carboxypeptidase-like activity that abolished the bioactivity of angiotensin I1 at pH 5.8. Recently, brain 'post-proline cleaving enzyme' has been proposed to be involved in angiotensin I1 inactivation [33].…”

Section: Discussionmentioning

confidence: 83%

Proteolytic Conversion of Angiotensins in Rat Brain Tissue

Tonnaer¹,

Engels²,

Wiegant³

et al. 1983

Eur J Biochem

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The proteolytic conversion of angiotensins in rat brain preparations was studied. Angiotensin 1 was converted into angiotensin I1 by enzymes which were associated with a synaptic membrane preparation, while angiotensin I1 was relatively resistant to proteolysis by these enzymes. Angiotensin I1 was rapidly metabolized at both pH 7.4 and pH 5.4 by enzymes in the soluble fraction of a synaptosomal preparation. One of the fragments formed at pH 7.4 was characterized as angiotensin 111. At pH 5.4 only one fragment was generated which was characterized as angiotensin-(1-7)-heptapeptide. Enzymatically generated angiotensin 11 and 111 displayed pronounced biological activity in the brain, whereas angiotensin-(l-7)-heptapeptide was inactive. These data indicate a route for the generation, and the inactivation of biologically active angiotensins in the brain.Angiotensin I1 (see Fig. 1) is an octapeptide which elicits apparent biological activity when injected into the brain or into the cerebral ventricular system (see [I] for review). Angiotensin I1 and the components necessary for the enzymatic generation of the octapeptide as well as for the expression of its biological activity have been found in brain tissue (see [2, 31 for reviews). Thus in addition to angiotensin 11, brain tissue contains angiotensinogen, renin-like enzymes, angiotensin I, angiotensin-I-converting enzyme, angiotensin 11 receptors and angiotensinases. The activity of the brain renin-angiotensin system in vivo may be inferred from the effects ofpharmacological blockade of this peptidergic system at the level of renin-like enzymes [4 -61, angiotensin-I-converting enzyme [4] or angiotensin I1 receptors [4, 71. Despite many studies on the activity in vivo of the reninangiotensin system in the brain, little is known about the subcellular localization of the various constituents of this system and their co-operation as a functional unit. The very short latencies to the biological effects upon intracerebroventricular injection of angiotensin TI and angiotensin I1 fragments [4,8] suggest a localization of the angiotensin I1 receptors in the plasma membrane of central nervous cells. Indeed, high affinity binding of angiotcnsin I1 to purified synaptosomes has been demonstrated [9]. Thus, angiotensin I1 might exert its effects in the central nervous system by modulation of neurones at the synaptic level.

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Section: Discussionmentioning

confidence: 83%

Proteolytic Conversion of Angiotensins in Rat Brain Tissue

Tonnaer¹,

Engels²,

Wiegant³

et al. 1983

Eur J Biochem

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“…All other components of the iso-RAS such as angiotensin I converting enzyme and angiotensinases are present in extrarenal tissue (Yang et al, 1972;Goldstein et al, 1972;Ganten et al, 197Sa).…”

Section: Possible P H Y S I O L O G I C a L R O L E O F T H E T I S Smentioning

confidence: 99%

The Iso-Renin Angiotensin Systems in Extrarenal Tissue

Ganten¹,

Hutchinson²,

Schelling³

et al. 1976

Clin Exp Pharmacol Physiol

141

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“…Further evidence to support the concept of a role for vasopressin secretion in blood pressure regulation is that clonidine, an anti-hypertensive agent, apparently suppresses vasopressin secretion (Humphreys, Reid & Ya, 1975). The additional data of Goldstein, Finkielman, Diaz, Fischer-Ferraro & Nahmod (1972), demonstrating a significant correlation between an angiotensin-like peptide in human cerebrospinal fluid and blood pressure of essential hypertensive patients, leads to interesting speculation about a vasopressinogenic hypertension.…”

Section: Discussionmentioning

confidence: 91%

“…Previously, evidence has been presented to suggest that the intrinsic angiotensin-forming system in the brain plays a role in blood pressure regulation Correspondence: Dr J. S. Hutchinson, Baker Medical Research Institute, Commercial Road, Prahran 3181, Victoria, Australia. (Finkielman, Fischer-Ferraro, Diaz, Goldstein & Nahmod, 1972; Ganten, Hutchinson & Schelling, 1975). Keil, Summy-Long & Severs (1975) have shown that intraventricular injection of angiotensin I1 in rats increases immunoreactive vasopressin levels in plasma in a dose-dependent manner.…”

Section: Introductionmentioning

confidence: 97%

Effect of Intraventricular Perfusion of Angiotensin II in Conscious Normal Rats and in Rats with Hereditary Hypothalamic Diabetes Insipidus

et al. 1976

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1.Artificial cerebrospinal fluid was perfused through the cerebral ventricles of conscious rats. A basal secretion rate of 16 ? 3 x 10-I mol of immunoreactive angiotensin II/min was calculated for intact rats.2. Most of the immunoreactive angiotensin I1 consisted probably of the heptapeptide or pentapeptide angiotensin I1 fragments.3. The pressor responses to intraventricular perfusions of angiotensin I1 were normal in Long-Evans rats, virtually absent in rats homozygous for hereditary hypothalamic diabetes insipidus, irrespective of whether they were injected with vasopressin tannate or not, and intermediate in rats heterozygous for hypothalamic diabetes insipidus.4. The results suggest that the pressor response to intraventricular angiotensin I1 is related to the release of vasopressin.

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Angiotensinase activity in rat and dog brain

Cited by 25 publications

References 12 publications

Proteolytic Conversion of Angiotensins in Rat Brain Tissue

Proteolytic Conversion of Angiotensins in Rat Brain Tissue

The Iso-Renin Angiotensin Systems in Extrarenal Tissue

Effect of Intraventricular Perfusion of Angiotensin II in Conscious Normal Rats and in Rats with Hereditary Hypothalamic Diabetes Insipidus

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