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J. Biochem, 1990, Vol. 107, No. 5 666-670
© 1990 Japanese Biochemical Society

research-article

Calcium-Dependent Binding of Phosphorylated Human Pre Interleukin 1{alpha} to Phospholipids1

Yoshiro Kobayashi2,3, Joost J. Oppenheim and Kouji Matsushima

Laboratory of Molecular Immunoregulation, Biological Response Modifiers Program, Division of Cancer Treatment, National Cancer Institute, Frederick Cancer Research Facility Frederick, MD 21701, U.S.A.

2 To whom correspondence should be addressed.

The effect of phosphorylation of pre interleukin la (IL la) on its association with various phospholipids was investigated. We prepared genetically engineered truncated human pre IL la (residues 64 to 271) and phosphorylated this pre IL la in vitro by using the catalytic subunit of cAMP-dependent protein kinase. Phosphorylated truncated pre IL la selectively binds to acidic phospholipids including phosphatidic acid, phosphatidylserine, and phosphatidylinositol, but not to other phospholipids (phosphatidylcholine and phos-phatidylethanolamine). This binding required divalent cations: Ca2+ or Mn2+, but not Mg2+. In order to obtain half-maximal binding of pre IL la to phosphatidic acid or phosphatidylserine, Ca2+ between 5 and 100 m{circumflex}M was required. Unphosphorylated pre IL la did not bind to phosphatidylserine, indicating that phosphorylation is required for this binding. Phosphorylated pre IL 1 {alpha} did not bind to intact peripheral blood mononuclear cells irrespective of lipopolysaccharide stimulation, but did bind to membrane vesicles prepared from these cells in the presence of calcium. Furthermore, phosphorylated pre IL la bound only to inside-out ghosts, but not right-side-out ghosts, prepared from human red blood cells. Taken together, these data suggest that phosphorylated pre IL la binds to the inner surface of plasma membrane in a Ca2+ and phospholipid-dependent manner.

1 This project has been supported in part with federal funds from the Department of Health and Human Services under contract number NO1-CO-74102 with Program Resources, Inc. The content of this publication does not necessarily reflect the views or policies of the Department of Health and Human Services, nor does mention of trade names, commercial products, or organizations imply endorsement by the U.S. Government.

3 Present address: Department of Biomolecular Science, Faculty of Science, Toho University, 2-2-1, Miyama, Funabashi, Chiba 274.


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