Premium
Zinc causes tyrosine phosphorylation of hippocampal p60 c‐src
Author(s) -
Alexander V. Vener,
Jacques Loeb
Publication year - 1992
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(92)80534-n
Subject(s) - phosphorylation , immunoprecipitation , biochemistry , tyrosine phosphorylation , tyrosine , proto oncogene tyrosine protein kinase src , biology , protein phosphorylation , chemistry , microbiology and biotechnology , protein kinase a , gene
Zinc cations at concentrations of 0.2 mM and greater catalyzed specific phosphorylation, by ATP, of two membrane‐associated proteins from rat hippocampus. These proteins, corresponding to molecular weights or 60 and 49 kDa, were phosphorylated primarily at tyrosine residues. The 60‐kDa protein was identified as p60 c‐src by immunoprecipitation using two different p60 c‐src ‐specific monoclonal antibodies. The 49‐kDa protein co‐immunoprecipitated with p60 c‐src . Cyanogen bromide cleavage of p60 c‐src and the 49‐kDa protein phosphorylated in the presence of Zn 2+ gave different patterns or phosphopeptides. It is suggested that tyrosine phosphorylation of p60 c‐src and the p60 c‐src ‐associated 49‐kDa protein may be a way of zinc participation in hippocampal neurotransmission.