Evidence for selective regulation of the phosphorylation of myocyte proteins by isoproterenol and prostaglandin E1
β Scribed by HAYES, J; BOWLING, N; KING, K; BODER, G
- Book ID
- 125440375
- Publisher
- Elsevier Science
- Year
- 1982
- Tongue
- English
- Weight
- 536 KB
- Volume
- 714
- Category
- Article
- ISSN
- 0304-4165
No coin nor oath required. For personal study only.
π SIMILAR VOLUMES
The 130 kDa atrial natriuretic factor receptor (ANF-R1) purified from bovine adrenal zona glomerulosa is phosphorylated in vitro by serine/threonine protein kinases such as cAMP-, cGMP-dependent and protein kinase C. This phosphorylation is independent of the presence of ANF (99-126) and there is no
## Abstract Prostaglandin E~2~ (PGE~2~) is among the most important mediators involved in neuroinflammatory processes. The final step of its synthesis is regulated by enzymes termed prostaglandin E~2~ synthases (PGES). Three PGES are known, cytosolic (c)PGES, membraneβassociated (m)PGESβ1 and mPGES