ArticleBiophysical journal1997
Effects of dipalmitoylglycerol and fatty acids on membrane structure and protein kinase C activity.
Article in Biophysical journal, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 42 citations in OpenAlex.
- Insertion Depth Modulates Protein Kinase C-δ-C1b Domain Interactions with Membrane Cholesterol as Revealed by MD Simulations.International journal of molecular sciences · 2023Article
- A mouse model of gestational diabetes shows dysregulated lipid metabolism post-weaning, after return to euglycaemia.Nutrition & diabetes · 2022Article
- PKCβ: Expanding role in hepatic adaptation of cholesterol homeostasis to dietary fat/cholesterol.American journal of physiology. Gastrointestinal and liver physiology · 2017Review
- The Causative Gene in Chanarian Dorfman Syndrome Regulates Lipid Droplet Homeostasis in C. elegans.PLoS genetics · 2015Article
- Synthesis, biological, and biophysical studies of DAG-indololactones designed as selective activators of RasGRP.Bioorganic & medicinal chemistry · 2014Article
- LPIAT1 regulates arachidonic acid content in phosphatidylinositol and is required for cortical lamination in mice.Molecular biology of the cell · 2012Article
- Conformationally constrained analogues of diacylglycerol. 29. Cells sort diacylglycerol-lactone chemical zip codes to produce diverse and selective biological activities.Journal of medicinal chemistry · 2008Article
- Amplification of diacylglycerol activation of protein kinase C by cholesterol.Biophysical journal · 2008Article
- Docosahexaenoic acid inhibits protein kinase C translocation/activation and cardiac hypertrophy in rat cardiomyocytes.Journal of molecular and genetic medicine : an international journal of biomedical research · 2005Article
- Hepatitis C virus RNA replication is regulated by host geranylgeranylation and fatty acids.Proceedings of the National Academy of Sciences of the United States of America · 2005Article
- The effects of acyl chain length and saturation of diacylglycerols and phosphatidylcholines on membrane monolayer curvature.Biophysical journal · 2002Article
- Genetic dissection of polyunsaturated fatty acid synthesis in Caenorhabditis elegans.Proceedings of the National Academy of Sciences of the United States of America · 2002Article
- Ceramides modulate protein kinase C activity and perturb the structure of Phosphatidylcholine/Phosphatidylserine bilayers.Biophysical journal · 1999Article
- A comparative study of the activation of protein kinase C alpha by different diacylglycerol isomers.The Biochemical journal · 1999Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
The individual and combined effects of the saturated diacylglycerol (DAG) dipalmitin (DP) and saturated or polyunsaturated unesterified fatty acids (PUFAs) on both the structure of phosphatidylcholine/phosphatidylserine (PC/PS; 4:1 mol/mol) bilayers and on protein kinase C (PKC) activity were studied using 2H nuclear magnetic resonance (NMR) and enzyme activity assays. In the absence of DP, PUFAs only slightly activated PKC whereas palmitic acid had no effect. In the absence of fatty acids, DP induced lateral phase separation of the bilayer into liquid-crystalline and gel phases. Under these conditions virtually all DP was sequestered into the gel phase and no activation of PKC was observed. The addition of polyunsaturated arachidonic or docosahexaenoic acids to the DP-containing bilayers significantly increased the relative amounts of DP and other lipid components in the liquid-crystalline phase, correlating with a dramatic increase in PKC activity. Furthermore, the effect was greater with PS, resulting in an enrichment of PS in the liquid-crystalline domains. In the presence of DP, palmitic acid did not decrease the amount of gel phase lipid and had no effect on PKC activity. The results explain the observed lack of PKC-activating capacity of long-chain saturated DAGs as due to the sequestration of DAG into gel domains wherein it is complexed with phospholipids and thus not available for the required interaction with the enzyme.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.