Purification, identification and phosphorylation of annexin I from rat liver mitochondria.
Annexin was purified from rat liver mitochondria to an apparent homogeneity with a molecular weight of 35 kDa as determined by sodium dodecyl sulfate polyacrylamide gel electrophoresis. The purified mitochondrial annexin (AXmito) was identified as annexin I by an immunoblot analysis using anti-annexin I antibody. The inhibitory effect of AXmito I on porcine pancreatic phospholipase A2 activity was as potent as that of bovine lung annexin I. The presence of annexin I in mitochondria was confirmed by an electron-microscopic study. AXmito I was shown to be phosphorylated by intrinsic protein tyrosine kinases on its tyrosine residues. This annexin was also phosphorylated by protein kinase C.
Yoshii
K
K
Department of Physiology, Faculty of Medicine, Kagawa Medical University, Japan.
Sugimoto
K
K
Tai
Y
Y
Konishi
R
R
Tokuda
M
M
D000818:Animals; D017305:Annexin A1 / Q000302:isolation & purification* / Q000378:metabolism / Q000494:pharmacology; D004591:Electrophoresis, Polyacrylamide Gel; D016253:Microscopy, Immunoelectron; D008930:Mitochondria, Liver / Q000737:chemistry* / Q000378:metabolism / Q000648:ultrastructure; D010179:Pancreas / Q000187:drug effects / Q000201:enzymology; D010741:Phospholipases A / Q000378:metabolism; D054467:Phospholipases A2; D010766:Phosphorylation; D011493:Protein Kinase C / Q000378:metabolism; D011505:Protein-Tyrosine Kinases / Q000378:metabolism*; D051381:Rats
D017305:Annexin A1; D011505:Protein-Tyrosine Kinases; D011493:Protein Kinase C; D010741:Phospholipases A; D054467:Phospholipases A2