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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
7
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pubmed:dateCreated |
1991-10-17
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pubmed:abstractText |
In order to understand angiotensin metabolism in the canine brain, we determined the molecular forms of angiotensin peptides present in the hypothalamus of the dog and carried out measurements of the metabolism of 125I-angiotensin I in homogenates of that tissue. Angiotensin peptides were extracted from canine hypothalamic tissue and quantified by specific radioimmunoassays combined with high-performance liquid chromatography. The major angiotensin peptides detected were angiotensin-(2-7) (391.2 +/- 16.8 pg/g tissue) and angiotensin-(3-7) (864.8 +/- 128.1 pg/g). Angiotensin II immunoreactivity was mainly composed of angiotensin-(3-8) (117.5 +/- 64 pg/g) and trace amounts of angiotensin II and angiotensin III. Angiotensin I immunoreactivity was composed of angiotensin I (52.3 +/- 5.8 pg/g). In separate experiments, addition of 125I-angiotensin I into supernatants (18,000 g for 2 min) of canine hypothalamic homogenates resulted in the accumulation of 125I-angiotensin-(1-7) as the major peptide product (14% of the total 125I-radioactivity) at 2 min. Incubation of the homogenate supernatants with enalaprilat (1 mumol/l), phosphoramidon (10 mumol/l), or ethylenediamine tetraacetic acid (1 mmol/l) did not inhibit the production of 125I-angiotensin-(1-7). In contrast, addition of Z-Pro-Prolinal (1 mumol/l), a specific inhibitor of prolyl endopeptidase, prevented the generation of 125I-angiotensin-(1-7) from 125I-angiotensin I by 47.0 +/- 8.0% (n = 6).(ABSTRACT TRUNCATED AT 250 WORDS)
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Angiotensin I,
http://linkedlifedata.com/resource/pubmed/chemical/Angiotensin II,
http://linkedlifedata.com/resource/pubmed/chemical/Endopeptidases,
http://linkedlifedata.com/resource/pubmed/chemical/Iodine Radioisotopes,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Fragments,
http://linkedlifedata.com/resource/pubmed/chemical/Serine Endopeptidases,
http://linkedlifedata.com/resource/pubmed/chemical/angiotensin II (1-7),
http://linkedlifedata.com/resource/pubmed/chemical/prolyl oligopeptidase
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
0263-6352
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
9
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
631-8
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:1653799-Angiotensin I,
pubmed-meshheading:1653799-Angiotensin II,
pubmed-meshheading:1653799-Animals,
pubmed-meshheading:1653799-Chromatography, High Pressure Liquid,
pubmed-meshheading:1653799-Dogs,
pubmed-meshheading:1653799-Endopeptidases,
pubmed-meshheading:1653799-Hypothalamus,
pubmed-meshheading:1653799-Iodine Radioisotopes,
pubmed-meshheading:1653799-Male,
pubmed-meshheading:1653799-Peptide Fragments,
pubmed-meshheading:1653799-Radioimmunoassay,
pubmed-meshheading:1653799-Renin-Angiotensin System,
pubmed-meshheading:1653799-Serine Endopeptidases
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pubmed:year |
1991
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pubmed:articleTitle |
Evidence that prolyl endopeptidase participates in the processing of brain angiotensin.
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pubmed:affiliation |
Department of Brain and Vascular Research, Cleveland Clinic Foundation, Ohio.
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pubmed:publicationType |
Journal Article,
In Vitro,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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