Phosphorylation of A170 stress protein by casein kinase II-like activity in macrophages.
Phosphorylation of A170 stress protein by casein kinase II-like activity in macrophages.
复制标题
巨噬细胞中酪蛋白激酶 II 样活性对 A170 应激蛋白的磷酸化。
DOI:
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发表时间:
1997
期刊:
影响因子:
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通讯作者:
T. Ishii
中科院分区:
文献类型:
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作者:
T. Yanagawa;K. Yuki;H. Yoshida;S. Bannai;T. Ishii
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.
DOI:
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发表时间:
1993
期刊:
The Journal of biological chemistry
影响因子:
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作者:
Schieven,GL;Kirihara,JM;Burg,DL;Geahlen,RL;Ledbetter,JA
通讯作者:
Ledbetter,JA
影响因子:
56.9
作者:
ROGERS, S;WELLS, R;RECHSTEINER, M
通讯作者:
RECHSTEINER, M
DOI:
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发表时间:
1980
期刊:
The Journal of biological chemistry
影响因子:
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作者:
Hathaway,GM;Lubben,TH;Traugh,JA
通讯作者:
Traugh,JA