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Association of tyrosine protein kinase activity with mitochondria in human fibroblasts
Author(s) -
Piedimonte Giuseppe,
Silvotti Lucia,
Borghetti Angelo F.,
Chamaret Solange,
Montagnier Luc
Publication year - 1986
Publication title -
journal of cellular biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.028
H-Index - 165
eISSN - 1097-4644
pISSN - 0730-2312
DOI - 10.1002/jcb.240320204
Subject(s) - tyrosine kinase , microbiology and biotechnology , tyrosine , mitochondrion , protein kinase a , chemistry , platelet derived growth factor receptor , kinase , biochemistry , biology , signal transduction , growth factor , receptor
Abstract A tyrosine protein kinase activity has been detected in the mitochondrial fraction purified from human fibroblasts. By enzymatic and sedimentation analysis this activity appeared to be localized in the mitochondrial outer membrane. Mitochondrial tyrosine phosphorylation was strictly dependent on the presence of Mn 2+ ions. An inverse relationship between cell proliferation and mitochondrial protein phosphorylation on tyrosine residues has been found: a marked increase in the mitochondrial tyrosine kinase activity occurred when a significant reduction in the growth rate followed serum step‐down. In mitochondria purified from resting cells, a protein band with apparent molecular weight of 50 kd appeared to be phosphorylated on tyrosine.