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Molecular Cloning and Characterization of Annexin V‐Binding Proteins with Highly Hydrophilic Peptide Structure
Author(s) -
Ohsawa Keiko,
Imai Yoshinori,
Ito Daisuke,
Kohsaka Shinichi
Publication year - 1996
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1046/j.1471-4159.1996.67010089.x
Subject(s) - peptide , cloning (programming) , chemistry , molecular cloning , annexin , peptide sequence , characterization (materials science) , annexin a2 , peptide mapping , microbiology and biotechnology , biochemistry , computational biology , biology , nanotechnology , gene , materials science , in vitro , computer science , programming language
We previously reported that annexin V promoted the survival of cultured rat neocortical neurons. In an effort to elucidate the mechanism underlying this neurotrophic activity of annexin V, we have attempted to identify the target or binding proteins of annexin V in neuronal cells. Herein, we screened an embryonic day 17 rat brain cDNA library by western blot using glutathione S ‐transferase‐annexin V fusion protein as a probe and then isolated four clones showing binding to annexin V in a Ca 2+ ‐ and phospholipid‐dependent manner. Although these cDNAs encoded different polypeptides, all four polypeptides shared the unique feature of containing highly hydrophilic stretches with high Lys, Glu, and Ser contents. Deduced amino acid sequences of two clones showed high homology with human X‐linked Helicase2 (XH2) and DNA (cytosine‐5) methyltransferase (DMTase) sequences, whereas the other two were not related to any known peptide sequence. These results suggest that XH2 and DMTase are candidates for annexin V‐binding proteins and thus may mediate the biological activity of annexin V.