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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
11
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pubmed:dateCreated |
1998-11-25
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pubmed:abstractText |
Angiotensin II regulates blood pressure and may affect adipogenesis and adipocyte metabolism. Angiotensin II is produced by cleavage of angiotensinogen by renin and angiotensin-converting enzyme in the circulation. In addition, angiotensin II may be produced in various tissues by enzymes of the renin-angiotensin system (RAS) or the nonrenin-angiotensin system (NRAS). We have analyzed the expression of angiotensinogen and enzymes required for its conversion to angiotensin II in human adipose tissue. Northern blot demonstrated angiotensinogen expression in adipose tissue from nine obese subjects. Western blot revealed a distinct band of expected size of the angiotensinogen protein (61 kDa) in isolated adipocytes. RT-PCR, followed by Southern blot, demonstrated renin expression in human adipose tissue. Angiotensin-converting enzyme messenger RNA was detected by RT-PCR, and the identity of the PCR products was verified by restriction enzyme cleavage. Transcripts for cathepsin D and cathepsin G, components of the NRAS, were detected by RT-PCR, verified by restriction enzyme cleavage. We conclude that human adipose tissue expresses angiotensinogen and enzymes of RAS and NRAS. This opens the possibility that angiotensinogen-derived peptides, produced in adipose tissue itself, may affect adipogenesis and play a role in the pathogenesis of obesity.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
AIM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Angiotensin II,
http://linkedlifedata.com/resource/pubmed/chemical/Angiotensinogen,
http://linkedlifedata.com/resource/pubmed/chemical/CTSG protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Cathepsin D,
http://linkedlifedata.com/resource/pubmed/chemical/Cathepsin G,
http://linkedlifedata.com/resource/pubmed/chemical/Cathepsins,
http://linkedlifedata.com/resource/pubmed/chemical/Peptidyl-Dipeptidase A,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger,
http://linkedlifedata.com/resource/pubmed/chemical/Renin,
http://linkedlifedata.com/resource/pubmed/chemical/Serine Endopeptidases
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
0021-972X
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
83
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
3925-9
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:9814470-Adipose Tissue,
pubmed-meshheading:9814470-Adult,
pubmed-meshheading:9814470-Angiotensin II,
pubmed-meshheading:9814470-Angiotensinogen,
pubmed-meshheading:9814470-Cathepsin D,
pubmed-meshheading:9814470-Cathepsin G,
pubmed-meshheading:9814470-Cathepsins,
pubmed-meshheading:9814470-Female,
pubmed-meshheading:9814470-Humans,
pubmed-meshheading:9814470-Middle Aged,
pubmed-meshheading:9814470-Peptidyl-Dipeptidase A,
pubmed-meshheading:9814470-RNA, Messenger,
pubmed-meshheading:9814470-Renin,
pubmed-meshheading:9814470-Renin-Angiotensin System,
pubmed-meshheading:9814470-Reverse Transcriptase Polymerase Chain Reaction,
pubmed-meshheading:9814470-Serine Endopeptidases
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pubmed:year |
1998
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pubmed:articleTitle |
Human adipose tissue expresses angiotensinogen and enzymes required for its conversion to angiotensin II.
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pubmed:affiliation |
Research Centre for Endocrinology and Metabolism, Department of Internal Medicine, Sahlgrenska University Hospital, Göteborg, Sweden.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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