ArticleThe Biochemical journal1993
Isolation, characterization and localization of annexin V from chicken liver.
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 7 papers.
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Who cites it
7 citing papers in PubMed, 33 citations in OpenAlex.
- Characterization of platelet aminophospholipid externalization reveals fatty acids as molecular determinants that regulate coagulation.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Dual acylation accounts for the localization of {alpha}19-giardin in the ventral flagellum pair of Giardia lamblia.Eukaryotic cell · 2009Article
- Key role of the N-terminus of chicken annexin A5 in vesicle aggregation.Protein science : a publication of the Protein Society · 2009Article
- Relocation of annexin V to platelet membranes is a phosphorylation-dependent process.The Biochemical journal · 1997Article
- Phosphatidylserine-mediated adhesion of T-cells to endothelial cells.The Biochemical journal · 1996Article
- Ca2+ concentration during binding determines the manner in which annexin V binds to membranes.The Biochemical journal · 1995Article
- The sub-cellular localization of annexin V in cultured chick-embryo fibroblasts.The Biochemical journal · 1993Article
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Authors and funding
3 authors at 1 institution in 1 country.
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Abstract
Annexin V has been purified from chicken liver; 40 mg of annexin V was obtained per kg of tissue. In contrast with mammalian liver, very little annexin VI was obtained. Surprisingly, chicken liver annexin V resembles mammalian annexin IV in its M(r) (32,500) and its isoelectric point (5.6), but amino-acid-sequence analysis demonstrates identity with chicken annexin V (anchorin CII). It binds to phospholipids in a Ca(2+)-dependent manner with free-Ca2+ concentrations for half-maximal binding to phosphatidylserine and phosphatidic acid of 10 microM; phosphatidylethanolamine of 32 microM and phosphatidylinositol of 90 microM. No binding to phosphatidylcholine was observed at Ca2+ concentrations up to 300 microM. In isolated liver membranes a significant proportion of annexin V was not extractable with EGTA but could only be extracted with Triton X-100, suggesting the existence of a tightly membrane-associated form of annexin V. A specific antiserum to chicken annexin V was used to localize the protein in adult and embryonic chicken liver. In the adult, annexin V was highly concentrated in epithelial cells lining the bile ducts, and along the bile canaliculi. In embryonic liver, strong staining of the bile-duct epithelial cells was again evident, and in addition, endothelial cells were strongly immunoreactive.
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