Induction of aromatase activity in human adipose tissue stromal cells by extracellular nucleotides--evidence for P2-purinoceptors in adipose tissue.
Schmidt M., Löffler G.
Laboratory Study, published in Eur J Biochem (1998) — summary generated from the PubMed abstract.
Evidence from laboratory and animal studies provides groundwork for understanding mechanisms and potential before human studies continue.
- Level A · Stronger Clinical Evidence
- Level B · Emerging clinical evidence with positive signals
- Level C · Early human research exploring benefits
- Level D · Scientific groundwork from lab and animal studies
- Emerging · Emerging topic under active research
This page is generated from the PubMed record. The Thai description is an automated summary of bibliographic fields and the abstract, not a full translation, and is not medical advice.
- Study type
- Laboratory Study
- Journal
- Eur J Biochem (1998)
- Country
- England
- Reported sample size
- —
- Source database
- PubMed
- PMID
- 9523724
- DOI
- 10.1046/j.1432-1327.1998.2520147.x
Abstract (original English)
Here we describe properties of the P2-purinoceptor, which is involved in the regulation of the key enzyme of estrogen biosynthesis, aromatase cytochrome P-450, in stromal cells from human adipose tissue. Aromatase activity induced by cortisol and platelet-derived growth factor BB (PDGF-BB) is further increased by addition of ATP, ADP, AMP and, albeit with reduced potency, adenosine, GTP and adenosine(5')tetraphospho(5') adenosine. Stable P1-purinoceptor agonists are inactive, whereas P2X-purinoceptor agonists mimic the effects of purine(s) (nucleotides). Prior incubation of cells with a P2-purinoceptor antagonist, but not P1-purinoceptor antagonists, blocks augmentation of aromatase activity by all ligands. Nucleotides, but not adenosine, retain their ability to augment aromatase activity in the presence of adenosine deaminase, indicating that they do not act via their metabolite adenosine. These results lead to the conclusion, that at least one member of the P2-subclass of purinoceptors exists in adipose tissue and is involved in modulation of aromatase activity in vitro. The pharmacological profile of the P2-site differs from those reported for cloned P2-purinoceptors, but is similar to that of the P2X-subclass. Therefore, a combined response of different members of the P2X-purinoceptor subclass or of members of different P2-purinoceptor subclasses cannot be discounted. Purin
What this study does not prove
- • This study does not prove SVF is an approved treatment or a replacement for standard care.
- • This is preclinical work; animal or laboratory results cannot be applied to humans.
Evidence level
Evidence from laboratory and animal studies provides groundwork for understanding mechanisms and potential before human studies continue.
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