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Neutrophil specific 33 kDa protein: Its Ca 2+ ‐ and phospholipid‐dependent intracellular translocation
Author(s) -
Sato Eisuke F.,
Morimoto Yasuko M.,
Matsuno Tsuyoshi,
Miyahara Masanobu,
Utsumi Kozo
Publication year - 1987
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(87)80038-8
Subject(s) - polyclonal antibodies , phosphatidylserine , cytoplasm , transmembrane protein , phospholipid , chromosomal translocation , intracellular , biology , microbiology and biotechnology , membrane protein , monoclonal antibody , biochemistry , guinea pig , chemistry , antibody , membrane , receptor , immunology , gene , endocrinology
A 33 kDa protein from neutrophils has been shown to associate reversibly with phosphatidylserine containing liposomes in a Ca 2+ ‐dependent manner. The protein was purified from guinea pig neutrophils. Immunoblotting and cytochemical studies with polyclonal and monoclonal antibodies to the protein revealed that the protein is commonly distributed in neutrophil cytoplasm of different animal species. The protein was translocated to the plasma membrane by treatment with stimuli. Thus the 33 kDa protein is neutrophil specific and may be involved in transmembrane signaling.