ArticleThe Biochemical journal1998
Annexin V inhibits protein kinase C activity via a mechanism of phospholipid sequestration.
Article in The Biochemical journal, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed, 88 citations in OpenAlex.
- The chordoid gliomaScience signaling · 2025Article
- Biologically Active Benzimidazole Hybrids as Cancer Therapeutics: Recent Advances.Pharmaceuticals (Basel, Switzerland) · 2025Review
- Integrated machine learning survival framework develops a prognostic model based on inter-crosstalk definition of mitochondrial function and cell death patterns in a large multicenter cohort for lower-grade glioma.Journal of translational medicine · 2023Article
- TheProceedings of the National Academy of Sciences of the United States of America · 2023Article
- A Temporal Comparative RNA Transcriptome Profile of the Annexin Gene Family in the Salivary versus Lacrimal Glands of the Sjögren's Syndrome-Susceptible C57BL/6.NOD-International journal of molecular sciences · 2022Article
- The phagocytic cyst cells inScience advances · 2022Article
- Phosphatidylserine externalized on the colonic capillaries as a novel pharmacological target for IBD therapy.Signal transduction and targeted therapy · 2021Article
- Annexin Animal Models-From Fundamental Principles to Translational Research.International journal of molecular sciences · 2021Review
- Annexin A5 regulates surface αvβ5 integrin for retinal clearance phagocytosis.Journal of cell science · 2019Article
- Annexins in Adipose Tissue: Novel Players in Obesity.International journal of molecular sciences · 2019Review
- Impact of ANXA5 polymorphisms on glioma risk and patient prognosis.Journal of neuro-oncology · 2019Article
- 3,5-Diiodo-L-Thyronine Exerts Metabolically Favorable Effects on Visceral Adipose Tissue of Rats Receiving a High-Fat Diet.Nutrients · 2019Article
- Phosphatidylserine Externalization Results from and Causes Neurite Degeneration in Drosophila.Cell reports · 2018Article
- Annexin A5 suppresses cyclooxygenase-2 expression by downregulating the protein kinase C-ζ-nuclear factor-κB signaling pathway in prostate cancer cells.Oncotarget · 2017Article
- Annexin-phospholipid interactions. Functional implications.International journal of molecular sciences · 2013Article
- CED-1, CED-7, and TTR-52 regulate surface phosphatidylserine expression on apoptotic and phagocytic cells.Current biology : CB · 2012Article
- The annexins: spatial and temporal coordination of signaling events during cellular stress.Cellular and molecular life sciences : CMLS · 2009Review
- Farnesol, a fungal quorum-sensing molecule triggers apoptosis in human oral squamous carcinoma cells.Neoplasia (New York, N.Y.) · 2008Article
- Annexins: putative linkers in dynamic membrane-cytoskeleton interactions in plant cells.Protoplasma · 2007Review
- Identification of differential gene expression in in vitro FSH treated pig granulosa cells using suppression subtractive hybridization.Reproductive biology and endocrinology : RB&E · 2006Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In this study, we assessed the role of annexin V, a Ca2+-dependent phospholipid-binding protein, as a regulator of protein kinase C (PKC) and characterized its mechanism of inhibition. Several mutants obtained by oligonucleotide site-directed mutagenesis were tested in vitro on PKC activity in cytosolic fractions from Jurkat cells and on purified PKCalpha. Annexin V inhibited phosphorylation of annexin II by endogenous PKC and phosphorylation of myelin basic protein by PKCalpha. In both systems, the use of single Ca2+-binding-site mutants of annexin V led to a partial reversal of inhibition, and the Ca2+-binding site located in the first domain of annexin V was found to have the most important role. An increase in the number of mutated Ca2+-binding sites led to a greater loss of inhibition. These results corroborated those showing the progressive loss of binding of these mutants to phospholipid liposomes. In conclusion, we show that PKC inhibition by annexin V is the consequence of a mechanism involving phospholipid sequestration by annexin V, and that the Ca2+-binding site located in domain 1 of annexin V plays a predominant role in this process. In addition, we show that the R122AIK site, which may act analogously to a PKC-inhibitory pseudosubstrate site, is not involved in PKC inhibition, and that a peptide corresponding to the C-terminal tail of annexin V inhibits PKC activity but to a lesser extent than annexin V itself.
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