Literature DB >> 6197070

A new feature of angiotensin-converting enzyme in the brain: hydrolysis of substance P.

H Yokosawa, S Endo, Y Ogura, S Ishii.   

Abstract

Highly purified rat brain angiotensin-converting enzyme hydrolyzes substance P which contains a C-terminal amino acid with an amidated carboxyl group. The hydrolysis of substance P verified by amino-group fluorometry and by high-performance liquid chromatography is inhibited by captopril, but not by phosphoramidon. The presence of sodium chloride is essential for the hydrolysis. The analyses of cleavage products indicate that the enzyme hydrolyzes substance P between Phe7-Phe8 and Phe8-Gly9 by an endopeptidase action, followed by successive release of dipeptides by a dipeptidyl carboxypeptidase action.

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Year:  1983        PMID： 6197070     DOI： 10.1016/0006-291x(83)90586-7

Source DB:  PubMed          Journal:  Biochem Biophys Res Commun        ISSN： 0006-291X            Impact factor:   3.575


  15 in total

1.  Investigation of the metabolism of substance P at the blood-brain barrier using LC-MS/MS.

Authors:  Arvind K Chappa; Joshua D Cooper; Kenneth L Audus; Susan M Lunte
Journal:  J Pharm Biomed Anal       Date:  2006-11-21       Impact factor: 3.935

2.  The metabolism of neuropeptides. Endopeptidase-24.11 in human synaptic membrane preparations hydrolyses substance P.

Authors:  R Matsas; M Rattray; A J Kenny; A J Turner
Journal:  Biochem J       Date:  1985-06-01       Impact factor: 3.857

3.  Immunohistochemistry of the guinea-pig trachea using an anti-idiotypic antibody recognizing substance P receptors.

Authors:  W Kummer; A Fischer; U Preissler; J Y Couraud; C Heym
Journal:  Histochemistry       Date:  1990

4.  An immunoradiometric assay for endopeptidase-24.11 shows it to be a widely distributed enzyme in pig tissues.

Authors:  N S Gee; M A Bowes; P Buck; A J Kenny
Journal:  Biochem J       Date:  1985-05-15       Impact factor: 3.857

5.  Novel activity of human angiotensin I converting enzyme: release of the NH2- and COOH-terminal tripeptides from the luteinizing hormone-releasing hormone.

Authors:  R A Skidgel; E G Erdös
Journal:  Proc Natl Acad Sci U S A       Date:  1985-02       Impact factor: 11.205

6.  The endopeptidase activity and the activation by Cl- of angiotensin-converting enzyme is evolutionarily conserved: purification and properties of an an angiotensin-converting enzyme from the housefly, Musca domestica.

Authors:  N S Lamango; M Sajid; R E Isaac
Journal:  Biochem J       Date:  1996-03-01       Impact factor: 3.857

7.  Novel activity of angiotensin-converting enzyme. Hydrolysis of cholecystokinin and gastrin analogues with release of the amidated C-terminal dipeptide.

Authors:  P Dubreuil; P Fulcrand; M Rodriguez; H Fulcrand; J Laur; J Martinez
Journal:  Biochem J       Date:  1989-08-15       Impact factor: 3.857

8.  A comparison of the zinc contents and substrate specificities of the endothelial and testicular forms of porcine angiotensin converting enzyme and the preparation of isoenzyme-specific antisera.

Authors:  T A Williams; K Barnes; A J Kenny; A J Turner; N M Hooper
Journal:  Biochem J       Date:  1992-12-15       Impact factor: 3.857

9.  The metabolism of neuropeptides. Neurokinin A (substance K) is a substrate for endopeptidase-24.11 but not for peptidyl dipeptidase A (angiotensin-converting enzyme).

Authors:  N M Hooper; A J Kenny; A J Turner
Journal:  Biochem J       Date:  1985-10-15       Impact factor: 3.857

10.  Metabolism of neuropeptides. Hydrolysis of the angiotensins, bradykinin, substance P and oxytocin by pig kidney microvillar membranes.

Authors:  S L Stephenson; A J Kenny
Journal:  Biochem J       Date:  1987-01-01       Impact factor: 3.857
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