Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:2.7.11.13 (protein kinase C)
 49,245 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Macrophages exhibit high activities of a phospholipase A2 which preferentially cleaves arachidonic acid (I. Flesch, B. Schmidt, and E. Ferber, Z. Naturforsch. 40c, 356-363, 1985). In unstimulated cells more than 90% of the total activity of this enzyme is localized in the cytosol. Treatment of these cells with 100 microM 1-oleoyl-2-acetyl-glycerol (OAG) for 30 min induced a translocation of phospholipase A2 to cellular membranes. The amount of translocated phospholipase A2 was about 30% of the total activity and correlated with a similar translocation of protein kinase C to membranes. These data suggest that the translocation of phospholipase A2 to membranes is related to the activation process of this enzyme.
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PMID:Translocation of phospholipase A2 from cytosol to membranes induced by 1-oleoyl-2-acetyl-glycerol in serum-free cultured macrophages. 342 99

We have carried out an analysis of 833 bp of the chick myogenin gene 5' flanking sequence. A 131-bp segment of this upstream region, which contains a CANNTG promoter element (E box) and a myocyte-enhancer-binding-factor-2 (MEF-2) site, acts as a full promoter. It resembles the human and the mouse myogenin promoters in the structure and disposition of regulatory elements, including a TATA box and the transcription start site. Examination of eight myogenic factor/E protein combinations cotransfected with several myogenin promoter constructs into HeLa cells, reveals that the chick myogenin/E2-5 combination maximally activates the myogenin promoter. This activation is mediated through the E box motif; the MEF-2 site limits the factor combinations that can activate the myogenin promoter and enhances activation by myogenin/E2-5. We have found previously that activation of protein kinase C inactivates the transcription of the chick myogenin gene [Huang, C.-F., Neville, C. M. & Schmidt, J. (1993) Control of myogenic factor genes by the membrane depolarization/protein kinase C cascade in chick skeletal muscle, FEBS Lett. 319, 21-25]. In this study, we show that the activation of protein kinase C inhibits the factor bound to the E box, which thereupon negatively regulates the activity of the MEF-2 binding protein.
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PMID:The role of the CANNTG promoter element (E box) and the myocyte-enhancer-binding-factor-2 (MEF-2) site in the transcriptional regulation of the chick myogenin gene. 760 Nov 28