ArticleThe Journal of cell biology1991
The participation of annexin II (calpactin I) in calcium-evoked exocytosis requires protein kinase C.
Article in The Journal of cell biology, 1991. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 67 papers.
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Who cites it
67 citing papers in PubMed, 194 citations in OpenAlex.
- The role of Annexin A2 in Alzheimer's disease: From cellular functions to therapeutic potential.The FEBS journal · 2026Review
- Revisiting the role of Annexins in membrane trafficking.Cellular and molecular life sciences : CMLS · 2025Review
- Review
- Annexins-a family of proteins with distinctive tastes for cell signaling and membrane dynamics.Nature communications · 2024Review
- Recent Advances in Molecular and Cellular Functions of S100A10.Biomolecules · 2023Review
- The association between Annexin A2 and epithelial cell adhesion molecule in breast cancer cells.Cancer reports (Hoboken, N.J.) · 2022Article
- Human colorectal cancer-associated carbohydrate antigen on annexin A2 protein.Journal of molecular medicine (Berlin, Germany) · 2021Article
- Advances in cancer treatment: a new therapeutic target, Annexin A2.Journal of Cancer · 2021Review
- Multiple Routes of Bluetongue Virus Egress.Microorganisms · 2020Review
- Annexin A2 Deficiency Exacerbates Neuroinflammation and Long-Term Neurological Deficits after Traumatic Brain Injury in Mice.International journal of molecular sciences · 2019Article
- Regulation of von-Willebrand Factor Secretion from Endothelial Cells by the Annexin A2-S100A10 Complex.International journal of molecular sciences · 2018Review
- Stromal Annexin A2 expression is predictive of decreased survival in pancreatic cancer.Oncotarget · 2017Article
- Annexins as Overlooked Regulators of Membrane Trafficking in Plant Cells.International journal of molecular sciences · 2017Review
- Atorvastatin protects endothelial colony‑forming cells against H2O2‑induced oxidative damage by regulating the expression of annexin A2.Molecular medicine reports · 2015Article
- Annexin A2 Acts as an Adhesion Molecule on the Endometrial Epithelium during Implantation in Mice.PloS one · 2015Article
- Annexin A3 Regulates Early Blood Vessel Formation.PloS one · 2015Article
- Annexin A2: its molecular regulation and cellular expression in cancer development.Disease markers · 2014Review
- Annexin A2 regulates β1 integrin internalization and intestinal epithelial cell migration.The Journal of biological chemistry · 2013Article
- Annexin A2 heterotetramer: structure and function.International journal of molecular sciences · 2013Article
- Myosin VI small insert isoform maintains exocytosis by tethering secretory granules to the cortical actin.The Journal of cell biology · 2013Article
7 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Permeabilized adrenal chromaffin cells secrete catecholamines by exocytosis in response to micromolar calcium concentrations. Recently, we have demonstrated that chromaffin cells permeabilized with digitonin progressively lose their capacity to secrete due to the release of certain cytosolic proteins essential for exocytosis (Sarafian T., D. Aunis, and M. F. Bader. 1987. J. Biol. Chem. 34:16671-16676). Here we show that one of the released proteins is calpactin I, a calcium-dependent phospholipid-binding protein known to promote in vitro aggregation of chromaffin granules at physiological micromolar calcium levels. The addition of calpactin I into digitonin- or streptolysin-O-permeabilized chromaffin cells with reduced secretory capacity as a result of the leakage of cytosolic proteins partially restores the calcium-dependent secretory activity. This effect is specific of calpactin I since other annexins (p32, p37, p67) do not stimulate secretion at similar or higher concentrations. Calpactin I requires the presence of Mg-ATP, suggesting that a phosphorylating step may regulate the activity of calpactin. Calpactin is unable to restore the secretory activity in cells which have completely lost their cytosolic protein kinase C or in cells having their protein kinase C inhibited by sphingosine or downregulated by long-term incubation with TPA. In contrast, calpactin I prephosphorylated in vitro by purified protein kinase C is able to reconstitute secretion in cells depleted of their protein kinase C activity. This stimulatory effect is also observed with thiophosphorylated calpactin I which is resistant to cellular phosphatases or with phosphorylated calpactin I introduced into cells in the presence of microcystin, a phosphatase inhibitor. These results suggest that calpactin I is involved in the exocytotic machinery by a mechanism which requires phosphorylation by protein kinase C.
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