Enhancement of Calcium Sensitivity of Lipocortin I in Phospholipid Binding Induced by Limited Proteolysis and Phosphorylation at the Amino Terminus as Analyzed by Phospholipid Affinity Column Chromatography-Reference-Cited by-同舟云学术

Enhancement of Calcium Sensitivity of Lipocortin I in Phospholipid Binding Induced by Limited Proteolysis and Phosphorylation at the Amino Terminus as Analyzed by Phospholipid Affinity Column Chromatography

Published:1989-04 Issue:12 Volume:264 Page:6948-6955
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Ando Y,Imamura S,Hong Y M,Owada M K,Kakunaga T,Kannagi R

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference48 articles.

1. The regulation of lipomodulin, a phospholipase inhibitory protein, in rabbit neutrophils by phosphorylation.

2. Lipocortin inhibition of extracellular and intracellular phospholipases A2is substrate concentration dependent

3. Inhibition of phospholipase A2 by "lipocortins" and calpactins. An effect of binding to substrate phospholipids.

4. Characterization of lipocortin I and an immunologically unrelated 33-kDa protein as epidermal growth factor receptor/kinase substrates and phospholipase A2 inhibitors.

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