ArticleThe Biochemical journal1993
Protein kinase C-dependent phosphorylation of annexins I and II in mesangial cells.
Article in The Biochemical journal, 1993. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 31 citations in OpenAlex.
- Effects of triethylene glycol dimethacrylate and bisphenol A-glycidyl methacrylate on annexin A proteins in human mesangial cells.European journal of oral sciences · 2026Article
- Post-translational modifications of Annexin A2 are linked to its association with perinuclear nonpolysomal mRNP complexes.FEBS open bio · 2017Article
- Annexin A1 translocates to nucleus and promotes the expression of pro-inflammatory cytokines in a PKC-dependent manner after OGD/R.Scientific reports · 2016Article
- Annexin A2 regulates β1 integrin internalization and intestinal epithelial cell migration.The Journal of biological chemistry · 2013Article
- Differential expression of annexin I in human mammary ductal epithelial cells in normal and benign and malignant breast tissues.Clinical & experimental metastasis · 1997Article
- Molecular biology of angiotensin receptors and their role in human cardiovascular disease.Journal of molecular medicine (Berlin, Germany) · 1996Review
- Translocation of lipocortin (annexin) 1 to the membrane of U937 cells induced by phorbol ester, but not by dexamethasone.British journal of pharmacology · 1996Article
- In vivo and in vitro phosphorylation of annexin II in T cells: potential regulation by annexin V.The Biochemical journal · 1995Article
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Authors and funding
4 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In this study we describe the phosphorylation of annexins from cultured rat mesangial cells by protein kinase C (PKC) both in vitro and in vivo. Annexins I and II were detected either by Western-blot analysis or by immunoprecipitation using specific antibodies. In the presence of [gamma-32P]ATP, cytosolic annexin I and annexin II were phosphorylated in vitro only when Ca2+ and phospholipids were added, but not in the presence of phospholipids alone. Annexin I was shown to be a better substrate than annexin II. In experiments in vivo performed on 32P-labelled mesangial cells, the addition of two well-known activators of PKC, namely angiotensin II (AII) and phorbol myristate acetate (PMA), increased preferentially the phosphorylation of annexin I. Annexin II was phosphorylated to a much lesser extent after AII treatment. Phosphoamino acid analysis of annexins, either by two-dimensional chromatography or by using a specific antiphosphotyrosine antibody, revealed only phosphoserine in these experiments in vivo. The addition of AII to mesangial cells increased serine phosphorylation of annexin I and annexin II, whereas PMA only increased serine phosphorylation of annexin I. V8-protease phosphopeptide mapping of annexin I that was phosphorylated both in vitro and in vivo by PKC from mesangial cells shows similar phosphopeptides.
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