Abstract:
:A170 is an oxidative stress-inducible protein having a Zinc finger domain, two PEST sequences, and many potential phosphorylation sites for serine/threonine kinases. These structural features suggest that the phosphorylation of A170 affects its function and degradation. We have found that A170 is phosphorylated in cultured murine peritoneal macrophages. In addition, using recombinant A170 proteins, we found two proteins of 40 and 44 kDa with kinase activity in cell extracts using an in-gel kinase assay. We compared the properties of the intrinsic A170 kinases with those of mitogen-activated protein kinase (ERK 2), protein kinase A (PKA), casein kinase II (CK II), and protein kinase C, since their catalytic subunits have molecular masses similar to A170 kinases. ERK 2, CK II, and PKA phosphorylated recombinant A170 as a substrate. The 40 and 44 kDa kinases present in the macrophage extract were similar to alpha and alpha' subunits of CK II in respect to substrate specificity, pharmacological properties, immuno-reactivities, and ubiquitous expression in tissues.
journal_name
Biochem Biophys Res Communjournal_title
Biochemical and biophysical research communicationsauthors
Yanagawa T,Yuki K,Yoshida H,Bannai S,Ishii Tdoi
10.1006/bbrc.1997.7783subject
Has Abstractpub_date
1997-12-08 00:00:00pages
157-63issue
1eissn
0006-291Xissn
1090-2104pii
S0006-291X(97)97783-4journal_volume
241pub_type
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